@article{borst_suyemoto_scholl_fuller_barnes_2015, title={Comparative Genomic Analysis Identifies Divergent Genomic Features of Pathogenic Enterococcus cecorum Including a Type IC CRISPR-Cas System, a Capsule Locus, an epa-Like Locus, and Putative Host Tissue Binding Proteins}, volume={10}, ISSN={["1932-6203"]}, DOI={10.1371/journal.pone.0121294}, abstractNote={Enterococcus cecorum (EC) is the dominant enteric commensal of adult chickens and contributes to the gut consortia of many avian and mammalian species. While EC infection is an uncommon zoonosis, like other enterococcal species it can cause life-threating nosocomial infection in people. In contrast to other enterococci which are considered opportunistic pathogens, emerging pathogenic strains of EC cause outbreaks of musculoskeletal disease in broiler chickens. Typical morbidity and mortality is comparable to other important infectious diseases of poultry. In molecular epidemiologic studies, pathogenic EC strains were found to be genetically clonal. These findings suggested acquisition of specific virulence determinants by pathogenic EC. To identify divergent genomic features and acquired virulence determinants in pathogenic EC; comparative genomic analysis was performed on genomes of 3 pathogenic and 3 commensal strains of EC. Pathogenic isolates had smaller genomes with a higher GC content, and they demonstrated large regions of synteny compared to commensal isolates. A molecular phylogenetic analysis demonstrated sequence divergence in pathogenic EC genomes. At a threshold of 98% identity, 414 predicted proteins were identified that were highly conserved in pathogenic EC but not in commensal EC. Among these, divergent CRISPR-cas defense loci were observed. In commensal EC, the type IIA arrangement typical for enterococci was present; however, pathogenic EC had a type IC locus, which is novel in enterococci but commonly observed in streptococci. Potential mediators of virulence identified in this analysis included a polysaccharide capsular locus similar to that recently described for E. faecium, an epa-like locus, and cell wall associated proteins which may bind host extracellular matrix. This analysis identified specific genomic regions, coding sequences, and predicted proteins which may be related to the divergent evolution and increased virulence of emerging pathogenic strains of EC.}, number={4}, journal={PLOS ONE}, author={Borst, Luke B. and Suyemoto, M. Mitsu and Scholl, Elizabeth H. and Fuller, Fredrick J. and Barnes, H. John}, year={2015}, month={Apr} }
 @article{mothapo_chen_cubeta_grossman_fuller_shi_2015, title={Phylogenetic, taxonomic and functional diversity of fungal denitrifiers and associated N2O production efficacy}, volume={83}, ISSN={0038-0717}, url={http://dx.doi.org/10.1016/j.soilbio.2015.02.001}, DOI={10.1016/j.soilbio.2015.02.001}, abstractNote={Fungi generally dominate microbial biomass in various soils and play critical roles in ecosystem functioning including nutrient cycling, disease ecology and food production. Therefore, fungal denitrification, phenotypically typified by nitrous oxide (N2O) production, presents another avenue other than N mineralization and heterotrophic nitrification for progress to better understand the multiple roles of fungi in sustaining the biosphere. The discovery of N2O production and consequently denitrification in Fusarium oxysporum Schltdl. in early 1970's has led to identification of many taxonomically diverse species of N2O-producing fungi. This review evaluates the current status of knowledge on species composition of fungal denitrifiers and their N2O-producing activity. Here we describe challenges with assessment of fungal N2O-producing activity across genera and suggest prospects for future studies. We also discuss species diversity in order to gain knowledge of important taxonomic and phylogenetic groups mediating N2O production and provide insight on ecological cues associated with fungal N2O production. Currently, the extent to which species phylogeny and the functional trait, i.e. N2O-producing activity, are linked remains to be determined; even so, it is evident that some related taxa exhibit similar N2O production efficacy than distant relatives.}, journal={Soil Biology and Biochemistry}, publisher={Elsevier BV}, author={Mothapo, Nape and Chen, Huaihai and Cubeta, Marc A. and Grossman, Julie M. and Fuller, Fred and Shi, Wei}, year={2015}, month={Apr}, pages={160–175} }
 @inbook{fuller_2013, edition={Third}, title={Retroviridae}, booktitle={Veterinary Microbiology}, publisher={Blackwell-Wiley}, author={Fuller, F.J.}, editor={McVey, DavidEditor}, year={2013} }
 @article{guy_west_fuller_marusak_shivaprasad_davis_fletcher_2011, title={Detection of Chicken Proventricular Necrosis Virus (R11/3 Virus) in Experimental and Naturally Occurring Cases of Transmissible Viral Proventriculitis with the Use of a Reverse Transcriptase-PCR Procedure}, volume={55}, ISSN={["0005-2086"]}, DOI={10.1637/9586-102110-reg.1}, abstractNote={SUMMARY. A reverse-transcriptase–polymerase-chain-reaction (RT-PCR) procedure was evaluated for detection of chicken proventricular necrosis virus (CPNV) in transmissible viral proventriculitis (TVP) –affected chickens. The RT-PCR procedure was compared with indirect immunofluorescence (IFA) and virus isolation for detection of CPNV in experimentally infected chickens. Microscopic lesions characteristic of TVP were detected on days 5–35 postexposure (PE) in CPNV-infected chickens; CPNV was detected by RT-PCR on days 3–14 PE in freshly collected proventriculi, and on days 1–14 PE in formalin-fixed paraffin-embedded (FFPE) proventriculi. CPNV was detected in proventriculi of experimentally infected chickens by IFA on days 3–10 PE, and by virus isolation on days 1–14 PE. With IFA used as a reference, sensitivity of the RT-PCR procedure with freshly collected and FFPE proventriculi was 88% and 100%, respectively; specificity was 83% and 86%, respectively. Proventriculi (FFPE) obtained from suspect TVP cases (n  =  19) were evaluated for presence of CPNV by RT-PCR and microscopic lesions consistent with TVP. CPNV was detected by RT-PCR in proventriculi from 8/11 TVP (+) cases (24/36 tissue sections). TVP (+) cases were defined by microscopic lesions characteristic of TVP; CPNV was not detected in proventriculi (0/8 cases, 0/32 tissue sections) in the absence of these lesions. The association between presence of TVP-characteristic microscopic lesions and presence of CPNV was highly significant (P  =  0.0014). These findings indicate the utility of the RT-PCR procedure for detection of CPNV and provide additional evidence for an etiologic role for this virus in TVP.}, number={1}, journal={AVIAN DISEASES}, author={Guy, James S. and West, Melissa A. and Fuller, Frederick J. and Marusak, Rosemary A. and Shivaprasad, H. L. and Davis, James L. and Fletcher, Oscar J.}, year={2011}, month={Mar}, pages={70–75} }
 @article{guy_west_fuller_2011, title={Physical and Genomic Characteristics Identify Chicken Proventricular Necrosis Virus (R11/3 Virus) as a Novel Birnavirus}, volume={55}, ISSN={["1938-4351"]}, DOI={10.1637/9504-081610-reg.1}, abstractNote={SUMMARY. Chicken proventricular necrosis virus (CPNV), isolate R11/3, previously was isolated from transmissible viral proventriculitis–affected chickens and was determined to be the likely etiology of this disease. CPNV was identified as a birnavirus on the basis of virion size and morphology (icosahedral, approximately 75 nm in diameter, nonenveloped); buoyant density in cesium chloride (1.32 g/ml); a genome comprising bisegmented, double-stranded RNA (approximately 3.8 and 3.4 kilobase pairs); and nucleotide sequence analyses. Nucleotide sequencing of CPNV RNA, segment B, identified a single large open reading frame that encodes a 903–amino acid protein. The 903–amino acid protein was identified as the putative VP1, the viral RNA-dependent RNA polymerase (RdRp), on the basis of sequence homologies with other birnavirus VP1 proteins. The CPNV VP1 possessed the unique permuted RdRp sequence motif arrangement characteristic of birnaviruses; however, phylogenetic analyses based on VP1 demonstrated that CPNV is deeply divergent from other birnaviruses.}, number={1}, journal={AVIAN DISEASES}, author={Guy, James S. and West, Melissa A. and Fuller, Frederick J.}, year={2011}, month={Mar}, pages={2–7} }
 @article{covaleda_fuller_payne_2010, title={EIAV S2 enhances pro-inflammatory cytokine and chemokine response in infected macrophages}, volume={397}, ISSN={["0042-6822"]}, DOI={10.1016/j.virol.2009.11.005}, abstractNote={Equine infectious anemia virus (EIAV) infection is distinctive in that it causes a rapid onset of clinical disease relative to other retroviruses. In order to understand the interaction dynamics between EIAV and the host immune response, we explored the effects of EIAV and its S2 protein in the regulation of the cytokine and chemokine response in macrophages. EIAV infection markedly altered the expression pattern of a variety of pro-inflammatory cytokines and chemokines monitored in the study. Comparative studies in the cytokine response between EIAV(17) and EIAV(17DeltaS2) infection revealed that S2 enhances the expression of IL-1alpha, IL-1beta, IL-8, MCP-2, MIP-1beta and IP-10. Moreover, S2 specifically induced the expression of the newly discovered cytokine, IL-34. Taken together, these results may help explain the effect of cytokine and chemokine dysregulation in EIAV pathogenesis and suggest a role of S2 in optimizing the host cell environment to promote viral dissemination and replication.}, number={1}, journal={VIROLOGY}, author={Covaleda, Lina and Fuller, Frederick J. and Payne, Susan L.}, year={2010}, month={Feb}, pages={217–223} }
 @article{covaleda_gno_fuller_payne_2010, title={Identification of cellular proteins interacting with equine infectious anemia virus S2 protein}, volume={151}, ISSN={["1872-7492"]}, DOI={10.1016/j.virusres.2010.04.007}, abstractNote={The macrophage-tropic lentivirus, equine infectious anemia virus (EIAV), encodes the small auxiliary protein S2 from a short open reading frame that overlaps the amino terminus of env EIAV S2 is dispensable for virus replication in cultured cells but is required for disease production. S2 is approximately 7 kDa and has no overall amino acid sequence homology to other cellular or viral proteins. Therefore it is likely that S2 plays a role as an adaptor protein. To further investigate S2 function we performed a yeast-2-hybrid screen to identify cellular proteins that interact with EIAV S2. The screen identified two human cellular proteins, amplified in osteosarcoma (OS-9) and proteasome 26S ATPase subunit 3 (PSMC3) that interact with S2. The equine homologues of these proteins were cloned and their interactions with S2 confirmed using co-immunoprecipitation assays. We identified two OS-9 isoforms that interact with S2 and a third splice variant that does not, indicating a region of OS-9 apparently required for the S2 interaction. The roles of these cellular proteins during EIAV infection have not been determined.}, number={2}, journal={VIRUS RESEARCH}, author={Covaleda, Lina and Gno, Bich-Ty and Fuller, Fredrick J. and Payne, Susan L.}, year={2010}, month={Aug}, pages={235–239} }
 @article{payne_fuller_2010, title={Virulence Determinants of Equine Infectious Anemia Virus}, volume={8}, ISSN={["1873-4251"]}, DOI={10.2174/157016210790416352}, abstractNote={Equine infectious anemia virus (EIAV) is a macrophage-tropic lentivirus that rapidly Induces disease in experimentally infected horses. Because EIAV infection and replication is centered on the monocyte/macrophage and has a pronounced acute disease stage, it is a useful model system for understanding the contribution of monocyte/macrophages to other lentivirus-induced diseases. Genetic mapping studies utilizing chimeric proviruses in which parental viruses are acutely virulent or avirulent have allowed the identification of important regions that influence acute virulence. U3 regions in the viral LTR, surface envelope (SU) protein and the accessory S2 gene strongly influence acute disease expression. While the chimeric proviruses provide insight into genes or genome regions that affect viral pathogenesis, it is then necessary to further dissect those regions to focus on specific virus-host mechanisms that lead to disease expression. The V6 region of the viral env protein is an example of one identified region that may interact with the ELR-1 receptor in an important way and we are currently identifying S2 protein motifs required for disease expression.}, number={1}, journal={CURRENT HIV RESEARCH}, author={Payne, Susan L. and Fuller, Frederick J.}, year={2010}, month={Jan}, pages={66–72} }
 @article{miller_fuller_gebreyes_lewbart_shchelkunov_shivappa_joiner_woolford_stone_dixon_et al._2007, title={Phylogenetic analysis of spring virema of carp virus reveals distinct subgroups with common origins for recent isolates in North America and the UK}, volume={76}, ISSN={["1616-1580"]}, DOI={10.3354/dao076193}, abstractNote={Genetic relationships between 35 spring viremia of carp virus (SVCV) genogroup Ia isolates were determined based on the nucleotide sequences of the phosphoprotein (P) gene and glycoprotein (G) genes. Phylogenetic analysis based on P gene sequences revealed 2 distinct subgroups within SVCV genogroup Ia, designated SVCV Iai and Iaii, and suggests at least 2 independent introductions of the virus into the USA in 2002. Combined P- and G-sequence data support the emergence of SVCV in Illinois, USA, and in Lake Ontario, Canada, from the initial outbreak in Wisconsin, USA, and demonstrate a close genetic link to viruses isolated during routine import checks on fish brought into the UK from Asia. The data also showed a genetic link between SVCV isolations made in Missouri and Washington, USA, in 2004 and the earlier isolation made in North Carolina, USA, in 2002. However, based on the close relationship to a 2004 UK isolate, the data suggest than the Washington isolate represents a third introduction into the US from a common source, rather than a reemergence from the 2002 isolate. There was strong phylogenetic support for an Asian origin for 9 of 16 UK viruses isolated either from imported fish, or shown to have been in direct contact with fish imported from Asia. In one case, there was 100% nucleotide identity in the G-gene with a virus isolated in China.}, number={3}, journal={DISEASES OF AQUATIC ORGANISMS}, author={Miller, O. and Fuller, F. J. and Gebreyes, W. A. and Lewbart, G. A. and Shchelkunov, I. S. and Shivappa, R. B. and Joiner, C. and Woolford, G. and Stone, D. M. and Dixon, P. F. and et al.}, year={2007}, month={Jul}, pages={193–204} }
 @article{fagerness_flaherty_perry_jia_payne_fuller_2006, title={The S2 accessory gene of equine infectious anemia virus is essential for expression of disease in ponies}, volume={349}, ISSN={["0042-6822"]}, DOI={10.1016/j.virol.2005.12.041}, abstractNote={Equine infectious anemia virus (EIAV) is a macrophage-tropic lentivirus that persistently infects horses and causes a disease that is characterized by periodic episodes of fever, thrombocytopenia, and viremia. EIAV encodes only four regulatory/accessory genes, (tat, rev, ttm, and S2) and is the least genetically complex of all known lentiviruses. We sought to determine the role of the EIAV S2 accessory gene of EIAV by introducing mutations that would prevent S2 expression on the p19/wenv17 infectious molecular clone. Virus derived from the p19/wenv17 molecular clone is highly virulent and routinely fatal when given in high doses (J. Virol. 72 (1998) 483). In contrast, an S2 deletion mutant on the p19/wenv17 background is unable to induce acute disease and plasma virus loads were reduced by 2.5 to 4.0 logs at 15 days post-infection. The S2 deleted virus failed to produce any detectable clinical signs during a 5-month observation period. These results demonstrate that S2 gene expression is essential for disease expression of EIAV.}, number={1}, journal={VIROLOGY}, author={Fagerness, Angela J. and Flaherty, Maureen T. and Perry, Stephanie T. and Jia, Bin and Payne, Susan L. and Fuller, Frederick J.}, year={2006}, month={May}, pages={22–30} }
 @article{guy_barnes_smith_owen_fuller_2005, title={Partial characterization of an adenovirus-like virus isolated from broiler chickens with transmissible viral proventriculitis}, volume={49}, ISSN={["0005-2086"]}, DOI={10.1637/7352-030205R.1}, abstractNote={Abstract Transmissible viral proventriculitis (TVP) was experimentally reproduced in specific-pathogen-free chickens using a homogenate of proventricular tissue obtained from TVP-affected commercial broiler chickens. Thin-section electron microscopy revealed intranuclear, approximately 70-nanometer (nm), adenovirus-like viruses (AdLV) within proventricular lesions. The AdLV, designated AdLV (R11/3), could not be propagated using various avian and mammalian cell cultures or by inoculation of embryonated chicken eggs by yolk, allantoic, or chorioallantoic membrane routes. However, AdLV (R11/3) was successfully propagated by amniotic inoculation of embryonated chicken eggs, with detection of the virus in proventriculi and intestinal contents of hatched 2-day-old chicks (8 days postinoculation). Virus propagation was evident in in ovo–inoculated chicks by 1) gross and microscopic lesions in proventriculi consistent with TVP, 2) immunohistochemical localization of AdLV (R11/3) antigens in proventricular epithelium, 3) thin-section electron microscopic detection of intranuclear, approximately 70-nm AdLVs within proventricular epithelium, and 4) negative-stain electron microscopic detection of extracellular, approximately 70-nm AdLVs in intestinal contents. Indirect immunofluorescence and polymerase chain reaction procedures that specifically recognize groups I, II, and III avian adenoviruses failed to recognize AdLV (R11/3). The findings suggest an etiologic role for AdLV (R11/3) in TVP and indicate that this virus is distinct from known avian adenoviruses.}, number={3}, journal={AVIAN DISEASES}, author={Guy, JS and Barnes, HJ and Smith, L and Owen, R and Fuller, FJ}, year={2005}, month={Sep}, pages={344–351} }
 @article{guy_miles_smith_fuller_schultz-cherry_2004, title={Antigenic and genomic characterization of turkey enterovirus-like virus (North Carolina, 1988 isolate): Identification of the virus as turkey astrovirus 2}, volume={48}, ISSN={["1938-4351"]}, DOI={10.1637/7077}, abstractNote={Abstract A small round virus (SRV) was isolated in 1988 from droppings of enteritis-affected turkeys in North Carolina and tentatively identified as an enterovirus on the basis of size (18–24 nm in diameter), intracytoplasmic morphogenesis, and a single-stranded RNA genome of approximately 7.5 kb. Additional characterization studies based on antigenic and genomic analyses were done to determine the relationship of this turkey enterovirus-like virus (TELV) to turkey astrovirus 2 (TAstV2), a recently characterized SRV of turkeys. Cross-immunofluorescence studies with TELV- and TAstV2-specific antisera indicated a close antigenic relationship between these viruses. TELV RNA was amplified by reverse transcriptase–polymerase chain reaction (RT-PCR) procedures with oligonucleotide primers specific for TAstV2 polymerase gene (open reading frame [ORF] 1b) and capsid protein gene (ORF 2). Subsequent sequence analyses of these TELV-derived RT-PCR products indicated a high degree of similarity with polymerase gene (98.8%) and capsid gene (96.9%) of TAstV2. These studies definitively identify TELV (North Carolina, 1988 isolate) as TAstV2.}, number={1}, journal={AVIAN DISEASES}, author={Guy, JS and Miles, AM and Smith, L and Fuller, FJ and Schultz-Cherry, S}, year={2004}, pages={206–211} }
 @article{payne_pei_jia_fagerness_fuller_2004, title={Influence of long terminal repeat and Env on the virulence phenotype of equine infectious anemia virus}, volume={78}, ISSN={["0022-538X"]}, DOI={10.1128/JVI.78.5.2478-2485.2004}, abstractNote={ABSTRACT}, number={5}, journal={JOURNAL OF VIROLOGY}, author={Payne, SL and Pei, XF and Jia, B and Fagerness, A and Fuller, FJ}, year={2004}, month={Mar}, pages={2478–2485} }
 @article{garg_fuller_tompkins_2004, title={Mechanism of feline immunodeficiency virus envelope glycoprotein-mediated fusion}, volume={321}, ISSN={["0042-6822"]}, DOI={10.1016/j.virol.2004.01.006}, abstractNote={Feline immunodeficiency virus (FIV) shares remarkable homology to primate lentiviruses, human immunodeficiency virus (HIV) and simian immunodeficiency virus (SIV). The process of lentiviral env glycoprotein-mediated fusion of membranes is essential for viral entry and syncytia formation. A detailed understanding of this phenomenon has helped identify new targets for antiviral drug development. Using a model based on syncytia formation between FIV env-expressing cells and a feline CD4+ T cell line we have studied the mechanism of FIV env-mediated fusion. Using this model we show that FIV env-mediated fusion mechanism and kinetics are similar to HIV env. Syncytia formation could be blocked by CXCR4 antagonist AMD3100, establishing the importance of this receptor in FIV gp120 binding. Interestingly, CXCR4 alone was not sufficient to allow fusion by a primary isolate of FIV, as env glycoprotein from FIV-NCSU1 failed to induce syncytia in several feline cell lines expressing CXCR4. Syncytia formation could be inhibited at a post-CXCR4 binding step by synthetic peptide T1971, which inhibits interaction of heptad repeat regions of gp41 and formation of the hairpin structure. Finally, using site-directed mutagenesis, we also show that a conserved tryptophan-rich region in the membrane proximal ectodomain of gp41 is critical for fusion, possibly at steps post hairpin structure formation.}, number={2}, journal={VIROLOGY}, author={Garg, H and Fuller, FJ and Tompkins, WAF}, year={2004}, month={Apr}, pages={274–286} }
 @inbook{donovan_fuller_2004, place={Ames, Iowa}, edition={2nd}, title={Retroviridae}, booktitle={Veterinary Microbiology}, publisher={Blackwell Publishing}, author={Donovan, Richard M. and Fuller, Frederick}, editor={Hirsch, Dwight and Maclachlan, Nigel James and Walker, Richard L.Editors}, year={2004}, pages={409–426} }
 @article{harms_kennedy-stoskopf_horne_fuller_tompkins_2000, title={Cloning and sequencing hybrid striped bass (Morone saxatilis x M. chrysops) transforming growth factor-β (TGF-β), and development of a reverse transcription quantitative competitive polymerase chain reaction (RT-qcPCR) assay to measure TGF-β mRNA of teleost fish}, volume={10}, ISSN={1050-4648}, url={http://dx.doi.org/10.1006/fsim.1999.0230}, DOI={10.1006/fsim.1999.0230}, abstractNote={A transforming growth factor (TGF)-beta was isolated and cloned from hybrid striped bass (Morone saxatilis x M. chrysops) anterior kidney mononuclear cells. This isolate (Genbank accession number AF140363) contains an open reading frame of 1146 bases coding for a 382 amino acid protein most similar to rainbow trout TGF-beta (57.3 and 78.6% identity with precursor and active protein, respectively) and rat TGF-beta 1 (41.1 and 68.8% identity with precursor and active protein, respectively). Consensus primers were demonstrated to amplify specifically by polymerase chain reaction (PCR), a TGF-beta segment from 14 species of teleost fish comprising 10 taxonomic families in 7 orders. A reverse transcription quantitative competitive polymerase chain reaction (RT-qcPCR) assay was devised to measure TGF-beta mRNA expression in teleost fish. Higher levels of TGF-beta mRNA expression were detected in mononuclear cells of peripheral blood than from spleen or anterior kidney.}, number={1}, journal={Fish & Shellfish Immunology}, publisher={Elsevier BV}, author={Harms, C.A and Kennedy-Stoskopf, S and Horne, W.A and Fuller, F.J and Tompkins, W.A.F}, year={2000}, month={Jan}, pages={61–85} }
 @article{ward_fuller_mehrotra_de buysscher_2000, title={Nucleotide sequence and vaccinia expression of the nucleoprotein of a highly virulent, neurotropic strain of Newcastle disease virus}, volume={44}, ISSN={["0005-2086"]}, DOI={10.2307/1592505}, abstractNote={The nucleoprotein (NP) of Newcastle disease virus (NDV) was selected to study the relative importance of an internal structural protein in the avian immune response. The NP gene of the virulent, neurotropic NDV Texas GB (TGB) strain was cloned and sequenced. Nucleotide sequence data for the NP gene allowed comparison of the deduced amino acid sequences for the NP genes of NDV-TGB and the avirulent duck isolate NDV-D26. These comparisons demonstrated an 89% nucleotide sequence homology and a 97% homology between the deduced amino acid sequences. The NDV-TGB NP expressed in recombinant vaccinia virus (rVAC) was electrophoretically and immunologically identical to the wild-type NDV-TGB. Although inoculation of chickens with the recombinant vaccinia virus expressing the NDV NP gene elicited anti-NDV antibodies in higher titers than in birds inoculated with live LaSota NDV, this strong anti-NDV response did not protect against lethal challenge with NDV-TGB.}, number={1}, journal={AVIAN DISEASES}, author={Ward, MDW and Fuller, FJ and Mehrotra, Y and De Buysscher, EV}, year={2000}, pages={34–44} }
 @article{payne_qi_fuller_shao_la celle_steagall_pei_perry_1999, title={Long terminal repeat sequences of equine infectious anaemia virus are a major determinant of cell tropism.}, volume={80}, ISSN={0022-1317 1465-2099}, url={http://dx.doi.org/10.1099/0022-1317-80-3-755}, DOI={10.1099/0022-1317-80-3-755}, abstractNote={The Wyoming strain of equine infectious anaemia virus (EIAV) is a highly virulent field strain that replicates to high titre in vitro only in primary equine monocyte-derived macrophages. In contrast, Wyoming-derived fibroblast-adapted EIAV strains (Malmquist virus) replicate in primary foetal equine kidney and equine dermis cells as well as in the cell lines FEA and Cf2Th. Wyoming and Malmquist viruses differ extensively both in long terminal repeat (LTR) and envelope region sequences. We have compared the promoter activities of the Wyoming LTR with those of LTRs derived from fibroblast-adapted viruses by examining their abilities to drive a luciferase reporter gene as well as by construction of infectious molecular clones differing only in LTR sequence. Our results indicate that LTR sequences are a major restriction for growth of the Wyoming strain of EIAV in fibroblasts.}, number={3}, journal={Journal of General Virology}, publisher={Microbiology Society}, author={Payne, S L and Qi, X M and Fuller, F and Shao, H and La Celle, K and Steagall, W K and Pei, X F and Perry, S}, year={1999}, month={Mar}, pages={755–759} }
 @article{russell_perkins_hoffman_miller_walker_fuller_sellon_1999, title={Platelets from thrombocytopenic ponies acutely infected with equine infectious anemia virus are activated in vivo and hypofunctional}, volume={259}, ISSN={["0042-6822"]}, DOI={10.1006/viro.1999.9737}, abstractNote={Thrombocytopenia is a consistent finding and one of the earliest hematological abnormalities in horses acutely infected with equine infectious anemia virus (EIAV), a lentivirus closely related to human immunodeficiency virus. Multifactorial mechanisms, including immune-mediated platelet destruction and impaired platelet production, are implicated in the pathogenesis of EIAV-associated thrombocytopenia. This study was undertaken to investigate whether regenerative thrombopoiesis and platelet destruction occurred in ponies acutely infected with EIAV. Circulating large, immature platelets were increased in ponies acutely infected with EIAV late in the infection when platelet count was at a nadir. Morphometric analysis of bone marrow from acutely infected ponies revealed significant increased in megakaryocyte area and megakaryocyte nuclear area. A trend toward increased numbers of megakaryocytes was also observed. Platelets from acutely infected ponies had increased surface-bound fibrinogen and ultrastructural changes consistent with in vivo platelet activation. Platelets also had hypofunctional aggregation responses to three agonists in vitro. We conclude that thrombocytopenia in ponies acutely infected with EIAV is regenerative and suggest that bone marrow platelet production is not severely compromised in these ponies. Our findings reveal that in vivo platelet activation occurs in ponies acutely infected with EIAV, and as a result platelets are hypofunctional in vitro. Activation of platelets in vivo may cause platelet degranulation or formation of platelet aggregates, which would result in removal of these damages platelets from circulation. This may represent a form of nonimmune-mediated platelet destruction in ponies acutely infected with EIAV.}, number={1}, journal={VIROLOGY}, author={Russell, KE and Perkins, PC and Hoffman, MR and Miller, RT and Walker, KM and Fuller, FJ and Sellon, DC}, year={1999}, month={Jun}, pages={7–19} }
 @article{breslin_smith_fuller_guy_1999, title={Sequence analysis of the matrix nucleocapsid gene region of turkey coronavirus}, volume={42}, ISSN={["0300-5526"]}, DOI={10.1159/000024956}, abstractNote={A reverse transcriptase, polymerase chain reaction (RT-PCR) procedure was used to amplify a segment of the genome of turkey coronavirus (TCV) spanning portions of the matrix and nucleocapsid (MN) protein genes (approximately 1.1 kb). The MN gene region of three epidemiologically distinct TCV strains (Minnesota, NC95, Indiana) was amplified, cloned into pUC19, and sequenced. TCV MN gene sequences were compared with published sequences of other avian and mammalian coronaviruses. A high degree of similarity (>90%) was observed between the nucleotide, matrix protein, and nucleocapsid protein sequences of TCV strains and published sequences of infectious bronchitis virus (IBV). The matrix and nucleocapsid protein sequences of TCV had limited homology (<30%) with MN sequences of mammalian coronaviruses. These results demonstrate a close genetic relationship between the avian coronaviruses, IBV and TCV.}, number={1}, journal={INTERVIROLOGY}, author={Breslin, JJ and Smith, LG and Fuller, FJ and Guy, JS}, year={1999}, pages={22–29} }
 @article{breslin_smith_fuller_guy_1999, title={Sequence analysis of the turkey coronavirus nucleocapsid protein gene and 3 ' untranslated region identifies the virus as a close relative of infectious bronchitis virus}, volume={65}, ISSN={["0168-1702"]}, DOI={10.1016/S0168-1702(99)00117-3}, abstractNote={The 3' end of the turkey coronavirus (TCV) genome (1740 bases) including the nucleocapsid (N) gene and 3' untranslated region (UTR) were sequenced and compared with published sequences of other avian and mammalian coronaviruses. The deduced sequence of the TCV N protein was determined to be 409 amino acids with a molecular mass of approximately 45 kDa. The TCV N protein was identical in size and had greater than 90% amino acid identity with published N protein sequences of infectious bronchitis virus (IBV); less than 21% identity was observed with N proteins of bovine coronavirus and transmissible gastroenteritis virus. The 3' UTR showed some variation among the three TCV strains examined, with two TCV strains, Minnesota and Indiana, containing 153 base segments which are not present in the NC95 strain. Nucleotide sequence identity between the 3' UTRs of TCV and IBV was greater than 78%. Similarities in both size and sequence of TCV and IBV N proteins and 3' UTRs provide additional evidence that these avian coronaviruses are closely related.}, number={2}, journal={VIRUS RESEARCH}, author={Breslin, JJ and Smith, LG and Fuller, FJ and Guy, JS}, year={1999}, month={Dec}, pages={187–193} }
 @article{payne_qi_shao_dwyer_fuller_1998, title={Disease induction by virus derived from molecular clones of equine infectious anemia virus}, volume={72}, number={1}, journal={Journal of Virology}, author={Payne, S. L. and Qi, X. M. and Shao, H. and Dwyer, A. and Fuller, F. J.}, year={1998}, pages={483–487} }
 @article{shao_robek_threadgill_mankowski_cameron_fuller_payne_1997, title={Characterization and mutational studies of equine infectious anemia virus dUTPase}, volume={1339}, ISSN={["0167-4838"]}, DOI={10.1016/S0167-4838(96)00229-4}, abstractNote={The macrophage tropic lentivirus, equine infectious anemia virus (EIAV), encodes a dUTPase in the pol gene that is required for efficient replication in macrophages. Two naturally occurring variants of the enzyme were expressed as recombinant proteins in Escherichia coli; metal chelate affinity chromatography was used to purify histidine-tagged recombinant enzymes to greater than 80% homogeneity in a single chromatographic step. Biochemical and enzymatic analyses of these preparations suggest that this method yields dUTPase that is suitable for detailed mutational analysis. Specific activities of preparations ranged from 4 x 10(3) to 5 x 10(4) units/mg. Recombinant EIAV dUTPase was highly specific for dUTP with a Km in the range of 3 to 8 microM. The enzyme was sensitive to inhibition by dUDP with little inhibition by other nucleotides or the reaction products, dUMP and PPi. The subunit organization of recombinant EIAV dUTPase was probed by gel filtration, glycerol gradient centrifugation, and chemical cross-linking, and is a trimer. We have begun mutational analyses by targeting a conserved domain present at the carboxyl terminus of all dUTPases that shares high homology to the phosphate binding loops (P-loops) of a number of ATP- and GTP-binding phosphatases. The P-loop-like motif of dUTPases is glycine rich but lacks the invariant lysine found in authentic P-loops. Deletion of this motif leads to loss of dUTPase activity; a series of point mutations that have been shown to inactivate authentic P-loops also abolish EIAV dUTPase activity.}, number={2}, journal={BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY}, author={Shao, H and Robek, MD and Threadgill, DS and Mankowski, LS and Cameron, CE and Fuller, FJ and Payne, SL}, year={1997}, month={May}, pages={181–191} }
 @article{fuller_1997, title={Genes controlling retroviral virulence}, volume={40}, DOI={10.1016/s0065-3519(97)80007-9}, abstractNote={Retroviruses under normal circumstances infect cells and yet inflict relatively little damage to the infected cell. The cell, however, remains infected for the lifespan of that cell or any daughter cells derived from that infected cell. Retroviruses that belong to the lentivirus subgroup are an exception because these viruses typically can directly kill the infected cell. The types of diseases induced by lentiviruses are also somewhat different presumably, at least in part, because of additional genes encoded in these complex retroviruses. Some retrovirus and retrovirus-like sequences are present in germline cells and are referred to as endogenous retroviruses. These sequences usually are nonexpressed or are expressed at very low levels and are discussed in this chapter. A wide range of biologic effects are discerned from a variety of retrovirus infections from malignancies, benign proliferative states that can lead to malignancies, degenerative diseases, viremias, and insertional activation or the inactivations of cellular genes and transactivations of cellular genes. These activities can result from the normal replication of these retroviruses or the less frequent generation of replication-defective viruses that can arise during persistent infections.}, number={1997}, journal={Advances in Veterinary Medicine}, author={Fuller, Frederick}, year={1997}, pages={135–155} }
 @article{sellon_walker_russell_perry_covington_fuller_1996, title={Equine infectious anemia virus replication is upregulated during differentiation of blood monocytes from acutely infected horses}, volume={70}, number={1}, journal={Journal of Virology}, author={Sellon, D.C. and Walker, K.M. and Russell, K.E. and Perry, S.T. and Covington, P. and Fuller, F.J.}, year={1996}, pages={590–594} }
 @article{sellon_walker_russell_perry_fuller_1996, title={Phorbol ester stimulation of equine macrophage cultures alters expression of equine infectious anemia virus}, volume={52}, ISSN={0378-1135}, url={http://dx.doi.org/10.1016/s0378-1135(96)00071-5}, DOI={10.1016/s0378-1135(96)00071-5}, abstractNote={Equine infectious anemia virus (EIAV) is a lentivirus that replicates predominantly in mature tissue macrophages. Viral expression is strongly influenced by the state of differentiation of the host cell. While blood monocytes can be infected, viral transcription is limited until the cell differentiates into a mature macrophage. Activation of mature macrophages infected with EIAV might also alter viral expression, presumably through binding of cellular transcription factors to viral nucleic acid sequences within the long terminal repeat (LTR). Using DNA amplification techniques, we compared LTR sequences of U.S. field strains of EIAV to sequences of a laboratory adapted strain of the virus. All field strain sequences were more closely related to Wyoming strain than to the Malmquist laboratory adapted strain or a previously sequenced infectious molecular clone of EIAV. Primary equine monocyte-derived macrophage cultures were infected with virulent and avirulent strains of EIAV and the effects of macrophage stimulation on EIAV expression were determined. Stimulation of macrophages with phorbol ester activated the cells to secrete tumor necrosis factor α (TNFα). This activation signal also resulted in a significant downregulation of viral expression as determined by supernatant reverse transcriptase activity. This effect occurred independent of the virulence of the virus strain used or the nucleic acid sequence of the viral LTR. This may represent an adaptive response of EIAV to evade the host immune response and establish a persistent infection.}, number={3-4}, journal={Veterinary Microbiology}, publisher={Elsevier BV}, author={Sellon, Debra C. and Walker, Kathy M. and Russell, Karen E. and Perry, Stephanie T. and Fuller, Frederick J.}, year={1996}, month={Oct}, pages={209–221} }
 @article{brown_shin_fuller_1995, title={Detection of pseudorabies viral DNA in tonsillar epithelial cells of latently infected pigs}, volume={56}, number={5}, journal={American Journal of Veterinary Research}, author={Brown, T.T. and Shin, K.O. and Fuller, F.J.}, year={1995}, pages={587–594} }
 @article{steagall_robek_perry_fuller_payne_1995, title={Incorporation of Uracil into Viral DNA Correlates with Reduced Replication of EIAV in Macrophages}, volume={210}, ISSN={0042-6822}, url={http://dx.doi.org/10.1006/viro.1995.1347}, DOI={10.1006/viro.1995.1347}, abstractNote={The retrovirus equine infectious anemia virus (EIAV) encodes a dUTPase situated between reverse transcriptase and integrase. We have described the inability of EIAV with a 270-bp dUTPase deletion, delta DU EIAV, to replicate to wild-type (WT) levels in equine macrophages (D. S. Threadgill, W. K. Steagall, M. T. Flaherty, F. J. Fuller, S. T. Perry, K. E. Rushlow, S. F. J. LeGrice, and S. L. Payne, J. Virol. 67, 2592-2600, 1993). Here we describe the construction of a second dUTPase-deficient virus (DUD71E) containing a single amino acid substitution in dUTPase. delta DU and DUD71E replicate to 2% of WT levels in macrophages by 7 days postinfection, when WT EIAV is highly cytopathic. To identify the replication block(s), we analyzed DNA synthesis, integration, and transcription. DNA synthesis was normal in macrophages, with evidence of full-length viral DNA by 24 hr postinfection. The level of integrated delta DU and DUD71E DNA appeared to be decreased 2- to 3-fold compared to WT. Steady-state levels of full-length viral transcripts were decreased over 100-fold, indicating that replication of dUTPase-deficient EIAV is blocked between viral DNA synthesis and transcription. As dUTP hydrolysis normally plays a role in preventing incorporation of uracil into newly synthesized DNA, we investigated the possibility that dUTPase-deficient EIAV DNA contains uracil. In vitro assays showed that while WT virions do not utilize dUTP, dUTPase-deficient virus and recombinant RT synthesize uracil-containing DNA. The presence of uracil in viral DNA recovered from delta DU- and DUD71E-infected macrophages was also demonstrated. In macrophages, a virally encoded dUTPase may be necessary to prevent the incorporation of uracil into viral DNA.}, number={2}, journal={Virology}, publisher={Elsevier BV}, author={Steagall, Wendy K. and Robek, Michael D. and Perry, Stephanie T. and Fuller, Frederick J. and Payne, Susan L.}, year={1995}, month={Jul}, pages={302–313} }
 @article{payne_rausch_rushlow_montelaro_issel_flaherty_perry_sellon_fuller_1994, title={Characterization of infectious molecular clones of equine infectious anaemia virus}, volume={75}, ISSN={0022-1317 1465-2099}, url={http://dx.doi.org/10.1099/0022-1317-75-2-425}, DOI={10.1099/0022-1317-75-2-425}, abstractNote={We have recovered five infectious molecular clones of the lentivirus equine infectious anaemia virus (EIAV). The clones were recovered from fetal equine kidney (FEK) cells infected with a virulent, cell culture-adapted virus stock (designated PV) and have been characterized at a molecular level. Each clone has unique envelope and long terminal repeat (LTR) sequences. We further investigated LTR sequence variation in the PV stock using PCR amplification to obtain additional LTR clones from infected FEK cells and from peripheral blood mononuclear cells (PBMCs) from animals experimentally infected with PV. Sequence analysis of resulting clones indicates a selection for different LTR populations in pony PBMCs compared to FEK cells. Finally, we observed that the cloned EIAV proviruses did not remain infectious when maintained in a derivative of pBR322. However, two proviruses have been stably maintained in a low copy number vector (pLG338-SPORT).}, number={2}, journal={Journal of General Virology}, publisher={Microbiology Society}, author={Payne, S. L. and Rausch, J. and Rushlow, K. and Montelaro, R. C. and Issel, C. and Flaherty, M. and Perry, S. and Sellon, D. and Fuller, F.}, year={1994}, month={Feb}, pages={425–429} }
 @article{sellon_fuller_mcguire_1994, title={The immunopathogenesis of equine infectious anemia virus}, volume={32}, ISSN={0168-1702}, url={http://dx.doi.org/10.1016/0168-1702(94)90038-8}, DOI={10.1016/0168-1702(94)90038-8}, number={2}, journal={Virus Research}, publisher={Elsevier BV}, author={Sellon, Debra C. and Fuller, Frederick J. and McGuire, Travis C.}, year={1994}, month={May}, pages={111–138} }
 @article{threadgill_steagall_flaherty_fuller_perry_rushlow_grice_payne_1993, title={Characterization of equine infectious anemia virus dUTPase: Growth properties of a dUTPase-deficient mutant}, volume={67}, journal={Journal of Virology}, author={Threadgill, D.S. and Steagall, W.K. and Flaherty, M.T. and Fuller, F.J. and Perry, S.T. and Rushlow, K.E. and Grice, S.F.Le and Payne, S.L.}, year={1993}, pages={2592–2600} }
 @article{sellon_cullen_whetter_gebhard_coggins_fuller_1993, title={Production and characterization of a monoclonal antibody recognizing a cytoplasmic antigen of equine mononuclear phagocytes}, volume={36}, ISSN={0165-2427}, url={http://dx.doi.org/10.1016/0165-2427(93)90027-2}, DOI={10.1016/0165-2427(93)90027-2}, abstractNote={An IgG1 mouse monoclonal antibody, designated 1.646, is described which recognizes a cytoplasmic antigen of equine mononuclear phagocytes. Indirect fluorescent antibody staining of peripheral blood leukocytes reveals a granular cytoplasmic staining, predominantly in adherent blood mononuclear cells. Indirect fluorescent antibody staining is positive for alveolar and peritoneal macrophages. In some horses, a few neutrophils are also stained. In equine tissue samples stained by immunohistochemistry, the distribution of positive cells is consistent with the distribution of tissue macrophages. The most intense and reliable staining occurs with splenic and lymph node macrophages. Hepatic Kupffer cells also stain with antibody 1.646, although the intensity of that staining is somewhat variable between horses. A granular pattern of staining typical of lipofuscin deposition is also seen in liver sections. There is also pale staining of some biliary and renal tubular epithelium. Equine erythrocytes, platelets and lymphocytes are not recognized by this antibody, and neither are monocyte/macrophages of human, canine or feline origin. Antibody 1.646 recognizes two proteins (150 and 30 kDa) of equine monocyte-derived macrophages when assayed by Western immunoblot. Because of the distribution of staining (tissue mononuclear phagocytes, lipofuscin-containing storage granules, biliary and renal tubular epithelium, and some neutrophils) we hypothesize that antibody 1.646 recognizes a cytoplasmic antigen that is closely associated with lysosomal membranes.}, number={4}, journal={Veterinary Immunology and Immunopathology}, publisher={Elsevier BV}, author={Sellon, Debra C. and Cullen, John M. and Whetter, Linda E. and Gebhard, Douglas H. and Coggins, Leroy and Fuller, Frederick J.}, year={1993}, month={May}, pages={303–318} }
 @article{clay_fuller_1992, title={Nucleotide Sequence of the Tick-borne Orthomyxo-like Dhori/India/1313/61 Virus Membrane Protein Gene}, volume={73}, ISSN={0022-1317 1465-2099}, url={http://dx.doi.org/10.1099/0022-1317-73-10-2609}, DOI={10.1099/0022-1317-73-10-2609}, abstractNote={The complete nucleotide sequence of the sixth largest segment of ssRNA (RNA-6) of the tick-borne orthomyxo-like Dhori/India/1313/61 virus was determined by using cloned cDNA derived from infected cell mRNA and dideoxynucleotide sequencing of viral RNA. RNA-6 contains 962 nucleotides and is predicted to encode a protein of 270 amino acids with an M(r) of 30,498 in its first open reading frame (ORF). This protein is likely to represent the viral membrane (M1) protein, based on its predicted M(r) of 29,000 (estimated by PAGE), its relatively high abundance in infected cells and amino acid composition analysis. In addition, a second ORF was found which overlaps the M1 protein gene sequence by 327 nucleotides. This additional reading frame, in the +3 frame, potentially can encode a protein of 141 amino acids. However, S1 nuclease analysis of RNA-6 mRNA from infected cells indicated that there was only a single abundant RNA species corresponding in size to the full-length genomic RNA (0.96 kb). Further studies are needed to determine whether expression of the second ORF occurs and how that expression might arise.}, number={10}, journal={Journal of General Virology}, publisher={Microbiology Society}, author={Clay, W. C. and Fuller, F. J.}, year={1992}, month={Oct}, pages={2609–2616} }
 @article{perry_flaherty_kelley_clabough_tronick_coggins_whetter_lengel_fuller_1992, title={The surface envelope protein gene region of equine infectious anemia virus is not an important determinant of tropism in vitro}, volume={66}, number={7}, journal={Journal of Virology}, author={Perry, S.T. and Flaherty, M.T. and Kelley, M. and Clabough, D.L. and Tronick, S. and Coggins, L. and Whetter, L. and Lengel, C.R. and Fuller, F.J.}, year={1992}, pages={4085–4097} }
 @article{sellon_perry_coggins_fuller_1992, title={Wild-type equine infectious anemia virus replicates in vivo predominantly in tissue macrophages, not in peripheral blood monocytes}, volume={66}, number={10}, journal={Journal of Virology}, author={Sellon, D.C. and Perry, S.T. and Coggins, L. and Fuller, F.J.}, year={1992}, pages={5906–5913} }
 @article{lin_roychoudhury_palese_clay_fuller_1991, title={Evolutionary relatedness of the predicted gene product of RNA segment 2 of the Tick-Borne Dhori virus and the PB1 polymerase gene of influenza viruses}, volume={182}, ISSN={0042-6822}, url={http://dx.doi.org/10.1016/0042-6822(91)90641-n}, DOI={10.1016/0042-6822(91)90641-n}, abstractNote={The complete nucleotide sequence of the second largest RNA segment of Dhori/India/1313/61 virus was determined and the deduced amino acid sequence was compared with the polymerase (P) proteins of influenza A, B, and C viruses. RNA segment 2 (2224 nucleotides) of Dhori virus contains a single long open reading frame that can encode a 716-amino amid polypeptide (81.3 kDa). The predicted polypeptide shares between 27 and 31% sequence identities with the PB1 polypeptides of influenza A, B, and C viruses. Among the regions most highly conserved are the sequences around the Asp-Asp motif common to many RNA polymerases. In spite of the high level of sequence identity between the Dhori RNA segment 2 gene product and the influenza A, B, and C virus PB1 proteins the amino acid composition of the Dhori protein indicates an acidic charge feature at pH 7.0 in contrast to the basic nature of the PB1 proteins of the influenza viruses. We suggest that the Dhori PB1-like protein be designated the Pα protein of this virus.}, number={1}, journal={Virology}, publisher={Elsevier BV}, author={Lin, Debby A. and Roychoudhury, Sonali and Palese, Peter and Clay, William C. and Fuller, Frederick J.}, year={1991}, month={May}, pages={1–7} }
 @article{clabough_gebhard_flaherty_whetter_perry_coggins_fuller_1991, title={Immune-mediated thrombocytopenia in horses infected with equine infectious anemia virus}, volume={65}, number={11}, journal={Journal of Virology}, author={Clabough, D.L. and Gebhard, D. and Flaherty, M.T. and Whetter, L.E. and Perry, S.T. and Coggins, L. and Fuller, F.J.}, year={1991}, pages={6242–6251} }
 @article{whetter_archambault_perry_gazit_coggins_yaniv_clabough_dahlberg_fuller_tronick_1990, title={Equine infectious anemia virus derived from a molecular clone persistently infects horses}, volume={64}, number={12}, journal={Journal of Virology}, author={Whetter, L. and Archambault, D. and Perry, S. and Gazit, A. and Coggins, L. and Yaniv, A. and Clabough, D. and Dahlberg, J. and Fuller, F. and Tronick, S.}, year={1990}, pages={5750–5756} }
 @article{freedman-faulstich_fuller_1990, title={Nucleotide sequence of the tick-borne, orthomyxo-like Dhori/Indian/1313/61 virus envelope gene}, volume={175}, ISSN={0042-6822}, url={http://dx.doi.org/10.1016/0042-6822(90)90181-p}, DOI={10.1016/0042-6822(90)90181-p}, abstractNote={The complete nucleotide sequence of the fourth largest segment of single-stranded RNA of the tick-borne, orthomyxo-like Dhori/Indian/1313/61 virus was determined by using cloned cDNA derived from infected cell mRNA. The fourth RNA contains 1586 nucleotides and can code for a protein of 521 amino acids with a molecular weight of 58,675 Da. The predicted polypeptide possesses an amino-terminal hydrophobic region that may function as a signal sequence to initiate translocation across the endoplasmic reticulum membrane and a carboxyl-terminal hydrophobic region that could serve as a stop transfer sequence for anchoring this protein in the membrane. The envelope protein of Dhori virus does not display significant amino acid sequence homology with any of the envelope proteins (hemagglutinin or neuraminidase) of the influenza virus family members (or any other virus group) suggesting that the Dhori envelope protein is unique and may at least in part account for its divergent biological properties with other orthomyxoviruses.}, number={1}, journal={Virology}, publisher={Elsevier BV}, author={Freedman-Faulstich, Elizabeth Z. and Fuller, Frederick J.}, year={1990}, month={Mar}, pages={10–18} }
 @article{heidner_maclachlan_fuller_richards_whetter_1988, title={Bluetongue Virus Genome Remains Stable throughout Prolonged Infection of Cattle}, volume={69}, ISSN={0022-1317 1465-2099}, url={http://dx.doi.org/10.1099/0022-1317-69-10-2629}, DOI={10.1099/0022-1317-69-10-2629}, abstractNote={Infection of three calves with a highly plaque-purified strain of bluetongue virus (BTV) resulted in prolonged infections, during which virus and neutralizing antibodies co-circulated in peripheral blood. Oligonucleotide fingerprint analyses of the original challenge virus and of the final virus isolate obtained from each calf demonstrated the BTV genome to remain stable throughout prolonged infection as no differences in fingerprint patterns were detected. Six neutralizing monoclonal antibodies (MAbs), and a polyclonal rabbit antiserum, were produced against the challenge virus. This panel of MAbs recognized at least two distinct neutralizing epitopes as demonstrated by immune precipitation. Neutralizing epitopes remained stable through the prolonged infections, as all MAbs and the polyclonal rabbit antiserum neutralized the challenge virus and the final calf isolates to equivalent titres. These results suggest that antigenic drift is not the mechanism by which BTV is able to persist in cattle in spite of a strong humoral immune response.}, number={10}, journal={Journal of General Virology}, publisher={Microbiology Society}, author={Heidner, H. W. and MacLachlan, N. J. and Fuller, F. J. and Richards, R. G. and Whetter, L. E.}, year={1988}, month={Oct}, pages={2629–2636} }
 @article{richards_maclachlan_heidner_fuller_1988, title={Comparison of virologic and serologic responses of lambs and calves infected with bluetongue virus Serotype 10}, volume={18}, ISSN={0378-1135}, url={http://dx.doi.org/10.1016/0378-1135(88)90090-9}, DOI={10.1016/0378-1135(88)90090-9}, abstractNote={Four lambs and 3 calves, seronegative to bluetongue virus (BTV), were inoculated intravenously with a highly plaque-purified strain of BTV Serotype 10. A single calf and lamb served as controls and were inoculated with uninfected cell culture lysate. All BTV-inoculated lambs exhibited mild clinical manifestations of bluetongue, whereas infected calves were asymptomatic. Viremia persisted in BTV-infected lambs for 35–42 days, and for 42–56 days in BTV-infected calves. Neutralizing antibodies were first detected in sera collected at Day 14 post-inoculation (PI) from 2 BTV-infected calves and all 4 infected lambs, and at Day 28 PI in the remaining calf. The appearance of neutralizing antibody in serum did not coincide with clearance of virus from blood; BTV and specific neutralizing antibody-coexisted in peripheral blood of infected lambs and calves for as long as 28 days. The sequential development, specificity and intensity of virus protein-specific humoral immune responses of lambs and calves were evaluated by immunoprecipitation of [35S]-labelled proteins in BTV-infected cell lysates by sera collected from inoculated animals at bi-weekly intervals PI. Sera from infected lambs and calves reacted most consistently with BTV structural proteins VP2 and VP7, and nonstructural protein NS2, and less consistently with structural protein VP5, and nonstructural protein NS1. Lambs developed humoral immune responses to individual BTV proteins more rapidly than calves, and one calf had especially weak virus protein-specific humural immune responses; viremia persisted longer in this calf than any other animal in the study. The clearance of virus from the peripheral blood of BTV-infected lambs and calves is not caused simply by the production of virus-specific neutralizing antibody, however the intensity of humoral immune responses to individual BTV proteins might influence the duration of viremia in different animals.}, number={3-4}, journal={Veterinary Microbiology}, publisher={Elsevier BV}, author={Richards, R.G. and Maclachlan, N.J. and Heidner, H.W. and Fuller, F.J.}, year={1988}, month={Dec}, pages={233–242} }
 @article{schaper_fuller_ward_mehrotra_stone_stripp_de buysscher_1988, title={Nucleotide sequence of the envelope protein genes of a highly virulent, neurotropic strain of newcastle disease virus}, volume={165}, ISSN={0042-6822}, url={http://dx.doi.org/10.1016/0042-6822(88)90686-1}, DOI={10.1016/0042-6822(88)90686-1}, abstractNote={The envelope glycoproteins of Newcastle disease virus (NDV), hemagglutinin-neuraminidase (HN) and fusion (F) proteins, play important roles in determining the host immune response and the virulence of that particular virus strain. The complete nucleotide sequence of the HN and F genes of a highly neurovirulent strain of NDV (Texas G. B., 1948) was determined in an effort to study the molecular basis of this strain's neurotropic properties. Comparison of the predicted amino acid sequences for the HN and F among the American NDV strains revealed that the Texas G. B. and Beaudette C envelope genes are closely related to each other and are less closely related to the avirulent B1 Hitchner strain. We have found 11 amino acid changes in the predicted HN protein between the Beaudette C and Texas G. B. strain but only 2 conservative amino acid changes (amino acids 11 and 197) in the F protein between these two strains. Although the virulence of NDV strains has been related to sequences at the cleavage site of F0, the property of neurovirulence cannot depend solely upon these sequences because there are no sequence differences between the Beaudette C and Texas G. B. strains. We suggest that the neurovirulence phenotype could be due to the molecular properties of the HN protein; however, we cannot exclude the possibility that the two conservative amino acid differences between the two F proteins could also play a role in determining the phenotypic differences between these two virus strains.}, number={1}, journal={Virology}, publisher={Elsevier BV}, author={Schaper, Ulrike M. and Fuller, Frederick J. and Ward, Marsha D.W. and Mehrotra, Yasmin and Stone, Henry O. and Stripp, Barry R. and De Buysscher, Edward V.}, year={1988}, month={Jul}, pages={291–295} }
 @article{fuller_clay_freedman_barnes_1988, title={Nucleotide sequence of the major structural protein genes of the tick-borne, orthomyxo-like Dhori/Indian/1313/61 virus}, volume={11}, ISSN={0168-1702}, url={http://dx.doi.org/10.1016/0168-1702(88)90190-6}, DOI={10.1016/0168-1702(88)90190-6}, journal={Virus Research}, publisher={Elsevier BV}, author={Fuller, Frederick J. and Clay, William C. and Freedman, Elizabeth Z. and Barnes, Julie A.}, year={1988}, month={Sep}, pages={49} }
 @article{fuller_man-faulstich_barnes_1987, title={Complete nucleotide sequence of the tick-borne, orthomyxo-like Dhori/Indian/1313/61 virus nucleoprotein gene}, volume={160}, ISSN={0042-6822}, url={http://dx.doi.org/10.1016/0042-6822(87)90047-x}, DOI={10.1016/0042-6822(87)90047-x}, abstractNote={The complete nucleotide sequence of the fifth largest segment of single-stranded RNA of the tick-borne, orthomyxo-like Dhori/Ind/1313/61 virus was determined by using cloned cDNA derived from infected cell mRNA and dideoxynucleotide sequencing of viral RNA. The fifth RNA contains 1479 nucleotides and can code for a protein of 477 amino acids with a molecular weight of 53,679 Da. The RNA 5 protein of the Dhori/Ind/1313/61 virus possesses five short regions (16-26 amino acids) which share a high degree (50-59%) of amino acid sequence homology with a computer-aligned consensus sequence of the influenza nucleoprotein gene family. These and other structural features of the RNA 5 protein suggest that RNA 5 of Dhori viruses codes for the nucleoprotein. The data also suggest that Dhori viruses are orthomyxoviruses, but that they are more distantly related to the influenza viruses than type A, B, and C viruses are to each other.}, number={1}, journal={Virology}, publisher={Elsevier BV}, author={Fuller, F.J. and Man-Faulstich, E.Z. Freed and Barnes, J.A.}, year={1987}, month={Sep}, pages={81–87} }
 @article{maclachlan_heidner_fuller_1987, title={Humoral immune response of calves to bluetongue virus infection}, volume={48}, number={7}, journal={American Journal of Veterinary Research}, author={MacLachlan, James N. and Heidner, Hans W. and Fuller, Frederick J.}, year={1987}, pages={1031–1035} }
 @inproceedings{johnston_davis_pence_gidwitz_fuller_1987, place={New York}, series={UCLA symposia on molecular and cellular biology}, title={Nucleic acid sequence analysis of Sindbis pathogenesis and penetration mutants}, booktitle={Positive strand RNA viruses : proceedings of a UCLA symposium held in Keystone, Colorado, April 20-26, 1986}, publisher={Alan R. Liss, Inc}, author={Johnston, R.E. and Davis, N.L. and Pence, D.F. and Gidwitz, S. and Fuller, F.J.}, editor={Brinton, M.A. and Rueckert, R.Editors}, year={1987}, collection={UCLA symposia on molecular and cellular biology} }
 @article{davis_fuller_dougherty_olmsted_johnston_1986, title={A single nucleotide change in the E2 glycoprotein gene of Sindbis virus affects penetration rate in cell culture and virulence in neonatal mice.}, volume={83}, ISSN={0027-8424 1091-6490}, url={http://dx.doi.org/10.1073/pnas.83.18.6771}, DOI={10.1073/pnas.83.18.6771}, abstractNote={The nucleotide sequence of the glycoprotein genes of fully virulent Sindbis virus and derived mutants that have reduced neurovirulence for neonatal mice (attenuated mutants) has been determined. A single amino acid difference, arginine instead of serine at position 114 of the mature E2 glycoprotein, distinguished the prototype attenuated mutant from its virulent wild-type parent. Virulent revertants of the attenuated mutant showed same-site reversion to the wild-type sequence. An identical single amino acid substitution, an arginine for the serine at E2 position 114, was found in a second independently selected attenuated mutant. The strains are characterized by genetic linkage between attenuation, accelerated penetration of baby hamster kidney cells, and efficient neutralization by the E2-specific monoclonal antibodies R6 and R13; selection for change in one property simultaneously selected for change in the other two (Olmsted, R. A., Baric, R. S., Sawyer, B. A. & Johnston, R. E. (1984) Science 225, 424-427 and Olmsted, R. A., Meyer, W. J. & Johnston, R. E. (1986) Virology 148, 1-10). The nucleotide sequence data suggest that a single mutation in the E2 gene is sufficient to cause these coordinate phenotypic changes. These findings identify a single locus in a Sindbis virus surface glycoprotein gene that determines both efficiency of interaction with cultured baby hamster kidney cells and degree of virulence in neonatal mice.}, number={18}, journal={Proceedings of the National Academy of Sciences}, publisher={Proceedings of the National Academy of Sciences}, author={Davis, N. L. and Fuller, F. J. and Dougherty, W. G. and Olmsted, R. A. and Johnston, R. E.}, year={1986}, month={Sep}, pages={6771–6775} }
 @article{maclachlan_fuller_1986, title={Genetic stability in calves of a single strain of bluetongue virus}, volume={47}, number={4}, journal={American Journal of Veterinary Research}, author={MacLachlan, N. J. and Fuller, F.J.}, year={1986}, pages={762–764} }
 @article{simmons_rose_fuller_maurer_luginbuhl_1986, title={Turkey Coryza: Lack of Correlation between Plasmids and Pathogenicity of Bordetella avium}, volume={30}, ISSN={0005-2086}, url={http://dx.doi.org/10.2307/1590427}, DOI={10.2307/1590427}, abstractNote={Plasmids were removed from pathogenic Bordetella avium using a variety of treatments. The plasmid-cure rates depended on the treatment and isolate. Pathogenicity of B. avium in turkey poults was not altered by removal of plasmids.}, number={3}, journal={Avian Diseases}, publisher={JSTOR}, author={Simmons, D. G. and Rose, L. P. and Fuller, F. J. and Maurer, L. C. and Luginbuhl, G. H.}, year={1986}, month={Jul}, pages={593} }
 @inbook{bishop_rud_belloncik_akashi_fuller_ihara_matsuoka_eshita_1984, title={Coding Analyses of Bunya­virus RNA Species}, ISBN={9780121835019}, url={http://dx.doi.org/10.1016/b978-0-12-183501-9.50007-8}, DOI={10.1016/b978-0-12-183501-9.50007-8}, abstractNote={The genome of bunya viruses consists of three single-stranded, negative-sense, RNA molecules designated as L, M, and S. For snowshoe hare (SSH) virus, a member of the California encephalitis serogroup of bunyaviruses, it has been demonstrated by genetic, molecular, and DNA sequencing studies that the S RNA (3.3x10 daltons) codes for the structural nucleocapsid polypeptide N (26.3x10 daltons) as well as a nonstructural protein NSs (10.5x10 daltons) that is found in virus infected cells. Tne function of the NSs protein is unknown. The two gene products are read from overlapping open reading frames in the S viral complementary RNA species. The S RNA species and the encoded gene products of SSH and LAC viruses are comparable in sequence. Although most of the 114 nucleotide differences do not predict amino acid changes, there are a total of 22 N and 12 NSs differences. The direct RNA sequencing of SSH and LAC RNA species has demonstrated that the 3' ends of the three viral RNA species (L, M, and S) are conserved, at least for 10–15 nucleotides.}, booktitle={Segmented Negative Strand Viruses}, publisher={Elsevier}, author={Bishop, David H.L. and Rud, Erling and Belloncik, Serge and Akashi, Hiroomi and Fuller, Frederick and Ihara, Takeshi and Matsuoka, Yumiko and Eshita, Yuki}, year={1984}, pages={3–11} }
 @inbook{bishop_fuller_akashi_beaty_shope_1984, title={The Use of Reassortant Bunyaviruses to Deduce their Coding and Pathogenic Potentials}, ISBN={9781461338963 9781461338949}, url={http://dx.doi.org/10.1007/978-1-4613-3894-9_2}, DOI={10.1007/978-1-4613-3894-9_2}, booktitle={Mechanisms of Viral Pathogenesis}, publisher={Springer US}, author={Bishop, D. H. L. and Fuller, F. and Akashi, H. and Beaty, B. and Shope, R. E.}, year={1984}, pages={49–60} }
 @inbook{beaty_fuller_bishop_1983, place={New York}, series={Progress in clinical and biological research}, title={Bunyavirus Gene Structure‐Function Relationships and Potential for RNA Segment Reassortment In The Vector: La Crosse and Snowshoe Hare Reassortant Viruses In Mosquitoes}, ISBN={9780845101230}, booktitle={California serogroup viruses : proceedings of an International Symposium, held in Cleveland, Ohio, November 12 and 13, 1982}, publisher={A.R. Liss}, author={Beaty, B.J. and Fuller, F.J. and Bishop, D.H.L.}, editor={Calisher, C.H. and Thompson, W.H.Editors}, year={1983}, pages={119–128}, collection={Progress in clinical and biological research} }
 @article{fuller_bhown_bishop_1983, title={Bunyavirus Nucleoprotein, N, and a Non-structural Protein, NSS, Are Coded by Overlapping Reading Frames in the S RNA}, volume={64}, ISSN={0022-1317 1465-2099}, url={http://dx.doi.org/10.1099/0022-1317-64-8-1705}, DOI={10.1099/0022-1317-64-8-1705}, abstractNote={It has been shown previously, by sequence analysis of the S RNA segment of snowshoe hare (SSH) bunyavirus, that two overlapping open reading frames in the viral complementary sequence code for proteins with molecular weights of 26.8 X 10(3) and 10.5 X 10(3) respectively. In addition to the viral nucleocapsid (N) protein, which is coded by the S RNA, analyses of parental and reassortant bunyavirus-infected cell extracts have shown that the viral S RNA and M RNA species each code for non-structural proteins (NSS and NSM, respectively). In the present report, in vitro translation analyses of the S mRNA species recovered from virus-infected cells indicate that a single size class of mRNA directs the synthesis of N and NSS. Compositional analyses of selected tryptic peptides of N and NSS have provided proof that N is the product of the first open reading frame, and NSS the product of the second.}, number={8}, journal={Journal of General Virology}, publisher={Microbiology Society}, author={Fuller, F. and Bhown, A. S. and Bishop, D. H. L.}, year={1983}, month={Aug}, pages={1705–1714} }
 @article{beaty_fuller_bishop_1983, title={Bunyavirus gene structure-function relationships and potential for RNA segment reassortment in the vector: La Crosse and snowshoe hare reassortant viruses in mosquitoes}, volume={123}, journal={Progress in Clinical Biological Research}, author={Beaty, F.J. and Fuller, F. and Bishop, D.H.}, year={1983}, pages={119–128} }
 @inbook{bishop_fuller_akashi_1983, place={New York}, series={Progress in clinical and biological research}, title={Coding Assignments of the RNA Genome Segments of California Serogroup Viruses}, ISBN={9780845101230}, booktitle={California serogroup viruses : proceedings of an International Symposium, held in Cleveland, Ohio, November 12 and 13, 1982}, publisher={A.R. Liss}, author={Bishop, D.H.L. and Fuller, F.J. and Akashi, H.}, editor={Calisher, C.H. and Thompson, W.H.Editors}, year={1983}, pages={107–117}, collection={Progress in clinical and biological research} }
 @article{bishop_fuller_akashi_1983, title={Coding assignments of the RNA genome segments of California serogroup viruses}, volume={123}, journal={Progress in Clinical Biological Research}, author={Bishop, D.H. and Fuller, F.J. and Akashi, H.}, year={1983}, pages={107–117} }
 @article{beaty_bishop_gay_fuller_1983, title={Interference between bunyaviruses in Aedes triseriatus mosquitoes}, volume={127}, ISSN={0042-6822}, url={http://dx.doi.org/10.1016/0042-6822(83)90373-2}, DOI={10.1016/0042-6822(83)90373-2}, abstractNote={Inhibition of the replication of alternate California serogroup bunyaviruses in Aedes triseriatus mosquitoes has been observed for mosquitoes previously infected with La Crosse (LAC) virus. By contrast, prior infection of mosquitoes with LAC virus did not interfere significantly with the subsequent infection and replication of Guaroa bunyavirus (Bunyamwera serogroup), or heterologous viruses such as West Nile flavivirus, or vesicular stomatitis rhabdovirus.}, number={1}, journal={Virology}, publisher={Elsevier BV}, author={Beaty, Barry J. and Bishop, David H.L. and Gay, Mary and Fuller, Frederick}, year={1983}, month={May}, pages={83–90} }
 @article{cler_fuller_bishop_1983, title={Tick-borne viruses structurally similar to orthomyxoviruses}, volume={127}, ISSN={0042-6822}, url={http://dx.doi.org/10.1016/0042-6822(83)90384-7}, DOI={10.1016/0042-6822(83)90384-7}, abstractNote={Members of the Orthomyxoviridae are characterized at the structural level as enveloped, negative sense, RNA viruses that bud from the outer plasma membranes of infected cells and have seven or eight species of single-stranded RNA. None of the three types of orthomyxoviruses (influenza A, B, C) has been shown to be transmitted by arthropods; rather, the viruses are transmitted directly or indirectly from one infected vertebrate to another. Analyses of the virion RNA species and polypeptides of the tick-borne Thogoto and Dhori viruses indicate that they have structural characteristics similar to accepted members of the Orthomyxoviridae. For example, the viruses have seven size classes of single-stranded RNA with 3′ end consensus sequences of HOUCGUUG (or U or A) UUGUUC…. The viruses contain 54–56 × 103 Da nucleocapsid protein, an internal 28 × 103 Da putative matrix protein plus minor 85–90 × 103 Da proteins, and a major outer 65 × 103 Da glycoprotein. In addition to their sensitivity to actinomycin D and α-amanitin the viruses morphologically and morphogenetically resemble orthomyxoviruses.}, number={1}, journal={Virology}, publisher={Elsevier BV}, author={Cler, John P.M. and Fuller, Frederick and Bishop, David H.L.}, year={1983}, month={May}, pages={205–219} }
 @article{bishop_fuller_akashi_1982, title={Coding assignments of the RNA genome segments of California serogroup viruses}, volume={123}, journal={Progress in Clinical Biological Research}, author={Bishop, D.H.L. and Fuller, F.J. and Akashi, H.}, year={1982}, pages={107–117} }
 @article{fuller_bishop_1982, title={Identification of viral coded non‐structural polypeptides in Bunyavirus infected cells}, volume={41}, number={2}, journal={Journal of Virology}, author={Fuller, Frederick J. and Bishop, David H.L.}, year={1982}, pages={643–648} }
 @article{collins_fuller_marcus_hightower_ball_1982, title={Synthesis and processing of sindbis virus nonstructural proteins in vitro}, volume={118}, ISSN={0042-6822}, url={http://dx.doi.org/10.1016/0042-6822(82)90356-7}, DOI={10.1016/0042-6822(82)90356-7}, abstractNote={Polyadenylated 42 S genome RNA of Sindbis virus was extracted from purified virions, selected by binding to oligo(dT)-cellulose, and used to direct cell-free protein synthesis in nuclease-treated reticulocyte lysates. The translation products comprised a series of polypeptides which included distinct species with apparent molecular weights of 250, 205, 155,145, 89, 76, and 60 × 103. Their interrelationships were examined by analysis of their kinetics of synthesis, peptide maps, and incorporation of radioisotopic label from formyl[35S]methionyl-tRNAf. Polypeptides p89, p76, and p60 were unique, nonoverlapping, and stable. However, their sequences were contained in one or more of the larger products p250, p205, p145, which comprised a set of overlapping polypeptides that shared a common N-terminus. Radioisotope chase experiments showed that p250, p205, p155, and p145 were unstable; that p89, p76, and p60 were generated by proteolytic processing of larger precursors; and that the RNA regions encoding these three stable products were translated in the order: p60, p89, p76. On the basis of their electrophoretic mobilities and peptide maps, p89 and p76 were indistinguishable from two polypeptides found in Sindbis virus-infected cells and are candidates to be components of the Sindbis virus RNA-dependent RNA polymerases. When translation was performed under conditions that were designed to inhibit proteolysis, the accumulation of p89 and p76 was prevented, and that of p60 was severely inhibited. Under certain translation conditions, heterodisperse products larger than p250 accumulated. Even after thermal denaturation of RNA, only small amounts of the viral structural proteins were synthesized, indicating that the 3′-terminal third of the 42 S RNA genome was essentially unavailable for independent translation.}, number={2}, journal={Virology}, publisher={Elsevier BV}, author={Collins, P.L. and Fuller, F.J. and Marcus, P.I. and Hightower, L.E. and Ball, L.A.}, year={1982}, month={Apr}, pages={363–379} }
 @article{clerx-van haaster_clerx_ushijima_akashi_fuller_bishop_1982, title={The 3' Terminal RNA Sequences of Bunyaviruses and Nairoviruses (Bunyaviridae): Evidence of End Sequence Generic Differences within the Virus Family}, volume={61}, ISSN={0022-1317 1465-2099}, url={http://dx.doi.org/10.1099/0022-1317-61-2-289}, DOI={10.1099/0022-1317-61-2-289}, abstractNote={The 3' terminal nucleotide sequences of the three virus RNA species of viruses representing eight serogroups of bunyaviruses (genus Bunyavirus, Bunyaviridae) and six serogroups of nairoviruses (genus Nairovirus, Bunyaviridae) have been characterized. Members of the Bunyavirus genus have conserved 3' end sequences (generally, 3' UCAUCACAUGA...) that differ from the conserved 3' end sequences of members of the Nairovirus genus (generally, 3' AGAGUUUCU...).}, number={2}, journal={Journal of General Virology}, publisher={Microbiology Society}, author={Clerx-van Haaster, C. M. and Clerx, J. P. M. and Ushijima, H. and Akashi, H. and Fuller, F. and Bishop, D. H. L.}, year={1982}, month={Aug}, pages={289–292} }
 @article{fuller_marcus_1980, title={Interferon Induction by Viruses. IV. Sindbis Virus: Early Passage Defective-Interfering Particles Induce Interferon}, volume={48}, ISSN={0022-1317 1465-2099}, url={http://dx.doi.org/10.1099/0022-1317-48-1-63}, DOI={10.1099/0022-1317-48-1-63}, abstractNote={We have shown that a single defective-interfering (DI) particle of early (5th) passage Sindbis virus induces maximal amounts of interferon in an 'aged' primary chick embryo cell. The capacity of such DI particles to induce interferon is inactivated by small amounts of u.v. radiation (i/e dose = 232 ergs/mm2). The I/e dose for inactivation of the interferon-inducing capacity of infectious virus particles is 399 ergs/mm2 and for infectivity is 101 ergs/mm2. Pre-treatment with interferon blocks formation of interferon in response to either DI or infectious virus particles. Our results suggest that Sindbis virus genes must be expressed to form the interferon inducer, which is presumably a molecule of double-stranded (ds)RNA. We postulate that for interferon induction, the genomic RNA which codes for genes G and A must be translated into products whose concerted action produces a dsRNA molecule upon synthesis of a segment of RNA complementary to the genome. The RNA from early passage DI particles is sufficiently large (25S, 1.6 x 10(6) mol. wt.) to accommodate these genes, whereas the RNA from the late passage DI particles (20S, 1.0 x 10(6) mol. wt.) is not. Late (15th) passage DI particles do not induce interferon formation.}, number={1}, journal={Journal of General Virology}, publisher={Microbiology Society}, author={Fuller, F. J. and Marcus, P. I.}, year={1980}, month={May}, pages={63–73} }
 @article{fuller_marcus_1980, title={Interferon Induction by Viruses. Sindbis Virus: Defective-interfering Particles Temperature-sensitive for Interferon Induction}, volume={48}, ISSN={0022-1317 1465-2099}, url={http://dx.doi.org/10.1099/0022-1317-48-2-391}, DOI={10.1099/0022-1317-48-2-391}, abstractNote={A defective-interfering (DI) particle of Sindbis virus was generated from a ts mutant of RNA-complementation group A by serially undiluted passages at 30 degrees C. This mutant induced interferon at a permissive temperature (30 degrees C), but not at a non-permissive temperature (40.5 degrees C); it also expressed homotypic interference throughout the range 30 to 40.5 degrees C. This demonstrates for the first time in a DI particle a ts function, namely, the ability to induce interferon. In addition, our data provide further evidence that the RNA genome of a Sindbis DI particle can be translated within the cell. We postulate that the products of translation function to produce the putative inducer of interferon, namely a molecule of dsRNA.}, number={2}, journal={Journal of General Virology}, publisher={Microbiology Society}, author={Fuller, F. J. and Marcus, P. I.}, year={1980}, month={Jun}, pages={391–394} }
 @article{fuller_marcus_1980, title={Sindbis virus I. Gene order of translation in Vivo}, volume={107}, ISSN={0042-6822}, url={http://dx.doi.org/10.1016/0042-6822(80)90311-6}, DOI={10.1016/0042-6822(80)90311-6}, abstractNote={Abstract Ultraviolet (uv) radiation was used to map the order of translation in vivo of Sindbis virus genes and assign nonstructural proteins to specific RNA − complementation groups. The inactivation of synthesis of individual Sindbis virus proteins in the irradiated cell displayed single-hit kinetics. The target sizes for each protein (gene), relative to infectivity, are consistent with a model in which (i) each molecule of 42 S and 26 S polycistronic mRNA initiates protein synthesis at a single site, (ii) translation does not progress beyond a uvlesion (uracil dimer), and (iii) some critical amount of translation beyond the actual cleavage site may be required to achieve cleavage. A gene order for translation of Sindbis virus proteins, respectively, as: 5′ ns66ns86-ns75 3′ in vivo was deduced for nonstructural and structural proteins, respectively, as: 5′ nss-66-ns86-ns75 and5′ capsid-E2-E1 3′. Sindbis virus RNA − genetic complementation groups were assigned to nonstructural proteins as follows: 5′ ns66(G)-ns86(A)-ns75(B/F) 3′.}, number={2}, journal={Virology}, publisher={Elsevier BV}, author={Fuller, Frederick J. and Marcus, Philip I.}, year={1980}, month={Dec}, pages={441–451} }
 @article{fuller_marcus_1979, title={Cell surface-associated ribonuclease activities}, volume={98}, ISSN={0021-9541 1097-4652}, url={http://dx.doi.org/10.1002/jcp.1040980102}, DOI={10.1002/jcp.1040980102}, abstractNote={Abstract}, number={1}, journal={Journal of Cellular Physiology}, publisher={Wiley}, author={Fuller, Frederick J. and Marcus, Philip I.}, year={1979}, month={Jan}, pages={1–10} }
 @article{marcus_fuller_1979, title={Interferon Induction by Viruses. II. Sindbis Virus: Interferon Induction Requires One-Quarter of the Genome -- Genes G and A}, volume={44}, ISSN={0022-1317 1465-2099}, url={http://dx.doi.org/10.1099/0022-1317-44-1-169}, DOI={10.1099/0022-1317-44-1-169}, abstractNote={We have measured the amounts of interferon formed by chick cells 'aged' in vitro in response to different amounts of infectious wild-type Sindbis virus. Our results suggest that one plaque-forming unit is enough to induce maximum interferon formation. With higher m.o.i. the yield of interferon is less. To inactivate the interferon-inducing activity of Sindbis virus, four times more u.v.-radiation was needed than to inactivate the infectivity of the virus. This suggests that only 25% of the virus genome need be intact in order to induce interferon. Temperature-sensitive Sindbis virus mutants from the three RNA+ complementation groups, C. D and E, gave rise to interferon in chick cells incubated at a non-permissive temperature, Similarly, mutants from two of the RNA- groups, B and F, gave rise to interferon, but not mutants from groups G and A. We conclude that no pre-formed inducer of interferon is present in Sindbis virus. It appears, however, that genes G and A represent a special one-quarter of the genome which must be functional in order to synthesize an interferon-inducing moiety. We suggest that this moiety is a double-stranded RNA molecule formed after synthesis of a segment of RNA complementary to the genome.}, number={1}, journal={Journal of General Virology}, publisher={Microbiology Society}, author={Marcus, P. I. and Fuller, F. J.}, year={1979}, month={Jul}, pages={169–177} }