@misc{bin-hui_xiu-ling_lommel_xue-ping_2022, title={Recent progress in maize lethal necrosis disease: From pathogens to integrated pest management}, volume={21}, ISSN={["2095-3119"]}, DOI={10.1016/j.jia.2022.08.050}, abstractNote={Maize (Zea mays), as a staple food and an important industrial raw material, has been widely cultivated for centuries especially by smallholder farmers. Maize lethal necrosis disease (MLND) is a serious disease infecting maize, which caused devastating damage in the African region recently. MLND is induced by co-infection of maize chlorotic mottle virus and one of several cereal-infecting viruses in the Potyviridae family, with the symptoms ranging from chlorotic mottle to plant death at different infection stages. Integrated pest management for MLND needs strengthening detection, focusing on prevention and effective control. Early detection system of MLND has been successfully established by serological methods, nucleic acid-based methods, next-generation sequencing, etc. The practices, such as using certified seeds, sanitary measures, crop rotation, tolerant or resistant varieties etc., have been considered as the effective, economical and eco-friendly way to prevent and control MLND.}, number={12}, journal={JOURNAL OF INTEGRATIVE AGRICULTURE}, author={Bin-hui, Zhan and Xiu-ling, Yang and Lommel, Steven A. and Xue-ping, Zhou}, year={2022}, month={Dec}, pages={3445–3455} }
 @article{guenther_lommel_opperman_sit_2018, title={Plant Virus-Based Nanoparticles for the Delivery of Agronomic Compounds as a Suspension Concentrate}, volume={1776}, ISBN={["978-1-4939-7806-9"]}, ISSN={["1940-6029"]}, url={http://www.scopus.com/inward/record.url?eid=2-s2.0-85048246738&partnerID=MN8TOARS}, DOI={10.1007/978-1-4939-7808-3_13}, abstractNote={Nanoparticle formulations of agrichemicals may enhance their performance while simultaneously mitigating any adverse environmental effects. Red clover necrotic mosaic virus (RCNMV) is a soil-transmitted plant virus with many inherent attributes that allow it to function as a plant virus-based nanoparticle (PVN) when loaded with biologically active ingredients. Here we describe how to formulate a PVN loaded with the nematicide abamectin (Abm) beginning with the propagation of the virus through the formulation, deactivation, and characterization of the finished product.}, journal={VIRUS-DERIVED NANOPARTICLES FOR ADVANCED TECHNOLOGIES: METHODS AND PROTOCOLS}, publisher={Springer New York}, author={Guenther, Richard H. and Lommel, Steven A. and Opperman, Charles H. and Sit, Tim L.}, year={2018}, pages={203–214} }
 @article{madden_oberhardt_lockney_santos_vennam_arney_franzen_lommel_miller_gehrig_et al._2017, title={Pharmacokinetics and efficacy of doxorubicin-loaded plant virus nanoparticles in preclinical models of cancer}, volume={12}, ISSN={["1748-6963"]}, DOI={10.2217/nnm-2016-0421}, abstractNote={ Aim: To compare the pharmacokinetics and efficacy of doxorubicin containing plant virus nanoparticles (PVNs) with PEGylated liposomal doxorubicin (PLD) and small molecule doxorubicin in two mouse models of cancer. Materials & methods: Studies were performed in A375 melanoma and intraperitoneal SKOV3ip1 ovarian cancer xenografts. The PVNs were administered in lower and more frequent doses in the ovarian model. Results: The PVNs were more efficacious than PLD and small molecule doxorubicin in the ovarian cancer model, but not in the melanoma cancer model. The pharmacokinetics profiles of the PVNs showed fast plasma clearance, but more efficient tumor delivery as compared with other carrier-mediated agents. Conclusion: PVNs administered at lower repeated doses provide both pharmacologic and efficacy advantages compared with PLD. }, number={20}, journal={NANOMEDICINE}, author={Madden, Andrew J. and Oberhardt, Bruce and Lockney, Dustin and Santos, Charlene and Vennam, Preethi and Arney, David and Franzen, Stefan and Lommel, Steven A. and Miller, C. Ryan and Gehrig, Paola and et al.}, year={2017}, month={Oct}, pages={2519–2532} }
 @article{ruark_koenning_davis_opperman_lommel_mitchum_sit_2017, title={Soybean cyst nematode culture collections and field populations from North Carolina and Missouri reveal high incidences of infection by viruses}, volume={12}, ISSN={["1932-6203"]}, url={http://www.scopus.com/inward/record.url?eid=2-s2.0-85011268632&partnerID=MN8TOARS}, DOI={10.1371/journal.pone.0171514}, abstractNote={Five viruses were previously discovered infecting soybean cyst nematodes (SCN; Heterodera glycines) from greenhouse cultures maintained in Illinois. In this study, the five viruses [ScNV, ScPV, ScRV, ScTV, and SbCNV-5] were detected within SCN greenhouse and field populations from North Carolina (NC) and Missouri (MO). The prevalence and titers of viruses in SCN from 43 greenhouse cultures and 25 field populations were analyzed using qRT-PCR. Viral titers within SCN greenhouse cultures were similar throughout juvenile development, and the presence of viral anti-genomic RNAs within egg, second-stage juvenile (J2), and pooled J3 and J4 stages suggests active viral replication within the nematode. Viruses were found at similar or lower levels within field populations of SCN compared with greenhouse cultures of North Carolina populations. Five greenhouse cultures harbored all five known viruses whereas in most populations a mixture of fewer viruses was detected. In contrast, three greenhouse cultures of similar descent to one another did not possess any detectable viruses and primarily differed in location of the cultures (NC versus MO). Several of these SCN viruses were also detected in Heterodera trifolii (clover cyst) and Heterodera schachtii (beet cyst), but not the other cyst, root-knot, or reniform nematode species tested. Viruses were not detected within soybean host plant tissue. If nematode infection with viruses is truly more common than first considered, the potential influence on nematode biology, pathogenicity, ecology, and control warrants continued investigation.}, number={1}, journal={PLOS ONE}, publisher={Public Library of Science (PLoS)}, author={Ruark, Casey L. and Koenning, Stephen R. and Davis, Eric L. and Opperman, Charles H. and Lommel, Steven A. and Mitchum, Melissa G. and Sit, Tim L.}, editor={Rao, A.L.N.Editor}, year={2017}, month={Jan} }
 @article{cao_guenther_sit_lommel_opperman_willoughby_2016, title={Development of abamectin loaded lignocellulosic matrices for the controlled release of nematicide for crop protection}, volume={23}, ISSN={["1572-882X"]}, url={http://www.scopus.com/inward/record.url?eid=2-s2.0-84955651797&partnerID=MN8TOARS}, DOI={10.1007/s10570-015-0817-6}, number={1}, journal={CELLULOSE}, publisher={Springer Science and Business Media LLC}, author={Cao, Jing and Guenther, Richard H. and Sit, Tim L. and Lommel, Steven A. and Opperman, Charles H. and Willoughby, Julie A.}, year={2016}, month={Feb}, pages={673–687} }
 @article{cao_guenther_sit_lommel_opperman_willoughby_2015, title={Development of Abamectin Loaded Plant Virus Nanoparticles for Efficacious Plant Parasitic Nematode Control}, volume={7}, ISSN={1944-8244 1944-8252}, url={http://dx.doi.org/10.1021/ACSAMI.5B00940}, DOI={10.1021/ACSAMI.5B00940}, abstractNote={Plant parasitic nematodes are one of the world's major agricultural pests, causing in excess of $157 billion in worldwide crop damage annually. Abamectin (Abm) is a biological pesticide with a strong activity against a wide variety of plant parasitic nematodes. However, Abm's poor mobility in the soil compromises its nematicide performance because of the limited zone of protection surrounding the growing root system of the plant. In this study, we manipulated Abm's soil physical chemistry by encapsulating Abm within the Red clover necrotic mosaic virus (RCNMV) to produce a plant virus nanoparticle (PVN) delivery system for Abm. The transmission electron microscopic and dynamic light scattering characterization of Abm-loaded PVN (PVN(Abm)) indicated the resultant viral capsid integrity and morphology comparable to native RCNMV. In addition, the PVN(Abm) significantly increased Abm's soil mobility while enabling a controlled release strategy for Abm's bioavailability to nematodes. As a result, PVN(Abm) enlarged the zone of protection from Meloidogyne hapla root knot nematodes in the soil as compared to treating with free Abm molecules. Tomato seedlings treated with PVN(Abm) had healthier root growth and a reduction in root galling demonstrating the success of this delivery system for the increased efficacy of Abm to control nematode damage in crops.}, number={18}, journal={ACS Applied Materials & Interfaces}, publisher={American Chemical Society (ACS)}, author={Cao, Jing and Guenther, Richard H. and Sit, Tim L. and Lommel, Steven A. and Opperman, Charles H. and Willoughby, Julie A.}, year={2015}, month={May}, pages={9546–9553} }
 @article{cao_guenther_sit_opperman_lommel_willoughby_2014, title={Loading and Release Mechanism of Red Clover Necrotic Mosaic Virus Derived Plant Viral Nanoparticles for Drug Delivery of Doxorubicin}, volume={10}, ISSN={["1613-6829"]}, url={http://www.scopus.com/inward/record.url?eid=2-s2.0-84919761332&partnerID=MN8TOARS}, DOI={10.1002/smll.201400558}, abstractNote={Loading and release mechanisms of Red clover necrotic mosaicvirus (RCNMV) derived plant viral nanoparticle (PVN) are shown for controlled delivery of the anticancer drug, doxorubicin (Dox). Previous studies demonstrate that RCNMV's structure and unique response to divalent cation depletion and re‐addition enables Dox infusion to the viral capsid through a pore formation mechanism. However, by controlling the net charge of RCNMV outer surface and accessibility of RCNMV interior cavity, tunable release of PVN is possible via manipulation of the Dox loading capacity and binding locations (external surface‐binding or internal capsid‐encapsulation) with the RCNMV capsid. Bimodal release kinetics is achieved via a rapid release of surface‐Dox followed by a slow release of encapsulated Dox. Moreover, the rate of Dox release and the amount of released Dox increases with an increase in environmental pH or a decrease in concentration of divalent cations. This pH‐responsive Dox release from PVN is controlled by Fickian diffusion kinetics where the release rate is dependent on the location of the bound or loaded active molecule. In summary, controllable release of Dox‐loaded PVNs is imparted by 1) formulation conditions and 2) driven by the capsid's pH‐ and ion‐ responsive functions in a given environment.}, number={24}, journal={SMALL}, publisher={Wiley}, author={Cao, Jing and Guenther, Richard H. and Sit, Tim L. and Opperman, Charles H. and Lommel, Steven A. and Willoughby, Julie A.}, year={2014}, month={Dec}, pages={5126–5136} }
 @article{martin_he_meilleur_guenther_sit_lommel_heller_2013, title={New insight into the structure of RNA in red clover necrotic mosaic virus and the role of divalent cations revealed by small-angle neutron scattering}, volume={158}, ISSN={["0304-8608"]}, url={http://europepmc.org/abstract/med/23483344}, DOI={10.1007/s00705-013-1650-6}, number={8}, journal={ARCHIVES OF VIROLOGY}, publisher={Springer Science and Business Media LLC}, author={Martin, Stanton L. and He, Lilin and Meilleur, Flora and Guenther, Richard H. and Sit, Tim L. and Lommel, Steven A. and Heller, William T.}, year={2013}, month={Aug}, pages={1661–1669} }
 @article{honarbakhsh_guenther_willoughby_lommel_pourdeyhimi_2013, title={Polymeric Systems Incorporating Plant Viral Nanoparticles for Tailored Release of Therapeutics}, volume={2}, ISSN={["2192-2659"]}, DOI={10.1002/adhm.201200434}, abstractNote={Abstract}, number={7}, journal={ADVANCED HEALTHCARE MATERIALS}, author={Honarbakhsh, Sara and Guenther, Richard H. and Willoughby, Julie A. and Lommel, Steven A. and Pourdeyhimi, Behnam}, year={2013}, month={Jul}, pages={1001–1007} }
 @article{park_sit_kim_lommel_2013, title={The red clover necrotic mosaic virus capsid protein N-terminal amino acids possess specific RNA binding activity and are required for stable virion assembly}, volume={176}, ISSN={["0168-1702"]}, url={http://www.scopus.com/inward/record.url?eid=2-s2.0-84881374230&partnerID=MN8TOARS}, DOI={10.1016/j.virusres.2013.05.014}, abstractNote={The red clover necrotic mosaic virus (RCNMV) bipartite RNA genome is packaged into two virion populations containing either RNA-1 and RNA-2 or multiple copies of RNA-2 only. To understand this distinctive packaging scheme, we investigated the RNA-binding properties of the RCNMV capsid protein (CP). Maltose binding protein-CP fusions exhibited the highest binding affinities for RNA probes containing the RNA-2 trans-activator or the 3′ non-coding region from RNA-1. Other viral and non-viral RNA probes displayed CP binding but to a much lower degree. Deletion of the highly basic N-terminal 50 residues abolished CP binding to viral RNA transcripts. In planta studies of select CP deletion mutants within this N-terminal region revealed that it was indispensable for stable virion formation and the region spanning CP residues 5–15 is required for systemic movement. Thus, the N-terminal region of the CP is involved in both producing two virion populations due to its RNA binding properties and virion stability.}, number={1-2}, journal={VIRUS RESEARCH}, publisher={Elsevier BV}, author={Park, Sang-Ho and Sit, Tim L. and Kim, Kook-Hyung and Lommel, Steven A.}, year={2013}, month={Sep}, pages={107–118} }
 @article{park_sit_kim_lommel_2012, title={The Red clover necrotic mosaic virus capsid protein N-terminal lysine-rich motif is a determinant of symptomatology and virion accumulation}, volume={13}, ISSN={["1364-3703"]}, url={http://www.scopus.com/inward/record.url?eid=2-s2.0-84864388918&partnerID=MN8TOARS}, DOI={10.1111/j.1364-3703.2011.00784.x}, abstractNote={SUMMARY}, number={7}, journal={MOLECULAR PLANT PATHOLOGY}, publisher={Wiley}, author={Park, Sang-Ho and Sit, Tim L. and Kim, Kook-Hyung and Lommel, Steven A.}, year={2012}, month={Sep}, pages={744–754} }
 @article{kim_thammarat_lommel_hogan_charkowski_2011, title={Pectobacterium carotovorum Elicits Plant Cell Death with DspE/F but the P. carotovorum DspE Does Not Suppress Callose or Induce Expression of Plant Genes Early in Plant-Microbe Interactions}, volume={24}, ISSN={["1943-7706"]}, DOI={10.1094/mpmi-06-10-0143}, abstractNote={The broad-host-range bacterial soft rot pathogen Pectobacterium carotovorum causes a DspE/F-dependent plant cell death on Nicotiana benthamiana within 24 h postinoculation (hpi) followed by leaf maceration within 48 hpi. P. carotovorum strains with mutations in type III secretion system (T3SS) regulatory and structural genes, including the dspE/F operon, did not cause hypersensitive response (HR)-like cell death and or leaf maceration. A strain with a mutation in the type II secretion system caused HR-like plant cell death but no maceration. P. carotovorum was unable to impede callose deposition in N. benthamiana leaves, suggesting that P. carotovorum does not suppress this basal immunity function. Within 24 hpi, there was callose deposition along leaf veins and examination showed that the pathogen cells were localized along the veins. To further examine HR-like plant cell death induced by P. carotovorum, gene expression profiles in N. benthamiana leaves inoculated with wild-type and mutant P. carotovorum and Pseudomonas syringae strains were compared. The N. benthamiana gene expression profile of leaves infiltrated with Pectobacterium carotovorum was similar to leaves infiltrated with a Pseudomonas syringae T3SS mutant. These data support a model where Pectobacterium carotovorum uses the T3SS to induce plant cell death in order to promote leaf maceration rather than to suppress plant immunity.}, number={7}, journal={MOLECULAR PLANT-MICROBE INTERACTIONS}, author={Kim, Hye-Sook and Thammarat, Phanit and Lommel, Steven A. and Hogan, Clifford S. and Charkowski, Amy O.}, year={2011}, month={Jul}, pages={773–786} }
 @article{lockney_guenther_loo_overton_antonelli_clark_hu_luft_lommel_franzen_2011, title={The Red clover necrotic mosaic virus Capsid as a Multifunctional Cell Targeting Plant Viral Nanoparticle}, volume={22}, ISSN={["1520-4812"]}, DOI={10.1021/bc100361z}, abstractNote={Multifunctional nanoparticles hold promise as the next generation of therapeutic delivery and imaging agents. Nanoparticles comprising many types of materials are being tested for this purpose, including plant viral capsids. It has been found that Red clover necrotic mosaic virus (RCNMV) can be loaded with significant amounts of therapeutic molecules with molecular weights of 600 or even greater. Formulation of RCNMV into a plant viral nanoparticle (PVN) involves the loading of cargo and attachment of peptides. In this study, we show that targeting peptides (less than 16 amino acids) can be conjugated to the capsid using the heterobifunctional chemical linker sulfosuccinimidyl-4-(N-maleimidomethyl)cyclohexane-1-carboxylate (Sulfo-SMCC). The uptake of both native RCNMV capsids and peptide-conjugated RCNMV was tested in the HeLa cell line for peptides with and without fluorescent labels. Uptake of RCNMV conjugate with a CD46 targeting peptide was monitored by flow cytometry. When formulated PVNs loaded with doxorubicin and armed with a targeting peptide were delivered to HeLa cells, a cytotoxic effect was observed. The ability to modify RCNMV for specific cell targeting and cargo delivery offers a method for the intracellular delivery of reagents for research assays as well as diagnostic and therapeutic applications.}, number={1}, journal={BIOCONJUGATE CHEMISTRY}, author={Lockney, Dustin M. and Guenther, Richard N. and Loo, Lina and Overton, Wesley and Antonelli, Ray and Clark, Jennifer and Hu, Mei and Luft, Chris and Lommel, Steven A. and Franzen, Stefan}, year={2011}, month={Jan}, pages={67–73} }
 @article{martin_guenther_sit_swartz_meilleur_lommel_rose_section_2010, title={Crystallization and preliminary X-ray diffraction analysis of red clover necrotic mosaic virus}, volume={66}, ISSN={["2053-230X"]}, url={http://europepmc.org/abstract/med/21045294}, DOI={10.1107/s1744309110032483}, abstractNote={Red clover necrotic mosaic virus (RCNMV) is a species that belongs to the Tombusviridae family of plant viruses with a T = 3 icosahedral capsid. RCNMV virions were purified and were crystallized for X-ray analysis using the hanging-drop vapor-diffusion method. Self-rotation functions and systematic absences identified the space group as I23, with two virions in the unit cell. The crystals diffracted to better than 4 Å resolution but were very radiation-sensitive, causing rapid decay of the high-resolution reflections. The data were processed to 6 Å in the analysis presented here.}, number={Pt 11}, journal={ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS}, author={Martin, S.L. and Guenther, R.H. and Sit, T.L. and Swartz, P.D. and Meilleur, Flora and Lommel, S.A. and Rose, Robert and Section, F.}, year={2010}, month={Nov}, pages={1458–1462} }
 @misc{franzen_lommel_2009, title={Targeting cancer with 'smart bombs': equipping plant virus nanoparticles for a 'seek and destroy' mission}, volume={4}, ISSN={["1743-5889"]}, DOI={10.2217/nnm.09.23}, abstractNote={ This article discusses plant virus nanoparticles as a weapon in the war on cancer. The successes and failures of numerous nanoparticle strategies are discussed as a background to consideration of the plant virus nanoparticle approach. To have therapeutic benefit, the advantages of the targeted nanoparticle must outweigh the problems of colloidal stability, uptake by the reticuloendothelial system as well as the requirement for clearance from the body. Biodegradable nanoparticles are considered to have the most promise to address these complex phenomena. After justifying the choice of biodegradable particles, the article focuses on comparison of micelles, liposomes, polymers and modified plant viruses. The structural uniformity, cargo capacity, responsive behavior and ease of manufacturing of plant virus nanoparticles are unique properties that suggest they have a wider role to play in targeted therapy. The loading of chemotherapeutic cargo is discussed, with specific reference to the advantage of reversible transitions of the capsid of Red clover necrotic mosaic virus. These features will be contrasted and compared with other biodegradable ‘smart bombs’ that target cancer cells. }, number={5}, journal={NANOMEDICINE}, author={Franzen, Stefan and Lommel, Steven A.}, year={2009}, month={Jul}, pages={575–588} }
 @article{basnayake_sit_lommel_2009, title={The Red clover necrotic mosaic virus origin of assembly is delimited to the RNA-2 trans-activator}, volume={384}, ISSN={["0042-6822"]}, url={http://www.scopus.com/inward/record.url?eid=2-s2.0-58549086327&partnerID=MN8TOARS}, DOI={10.1016/j.virol.2008.11.005}, abstractNote={The bipartite RNA genome of Red clover necrotic mosaic virus (RCNMV) is encapsidated into icosahedral virions that exist as two populations: i) virions that co-package both genomic RNAs and ii) virions packaging multiple copies of RNA-2. To elucidate the packaging mechanism, we sought to identify the RCNMV origin of assembly sequence (OAS). RCNMV RNA-1 cannot package in the absence of RNA-2 suggesting that it does not contain an independent packaging signal. A 209 nt RNA-2 element expressed from the Tomato bushy stunt virus CP subgenomic promoter is co-assembled with genomic RNA-1 into virions. Deletion mutagenesis delimited the previously characterized 34 nt trans-activator (TA) as the minimal RCNMV OAS. From this study we hypothesize that RNA-1 must be base-paired with RNA-2 at the TA to initiate co-packaging. The addition of viral assembly illustrates the critical importance of the multifunctional TA element as a key regulatory switch in the RCNMV life cycle.}, number={1}, journal={VIROLOGY}, publisher={Elsevier BV}, author={Basnayake, Veronica R. and Sit, Tim L. and Lommel, Steven A.}, year={2009}, month={Feb}, pages={169–178} }
 @article{powers_sit_qu_morris_kim_lommel_2008, title={A versatile assay for the identification of RNA silencing suppressors based on complementation of viral movement}, volume={21}, ISSN={["1943-7706"]}, url={http://www.scopus.com/inward/record.url?eid=2-s2.0-47549110190&partnerID=MN8TOARS}, DOI={10.1094/MPMI-21-7-0879}, abstractNote={ The cell-to-cell movement of Turnip crinkle virus (TCV) in Nicotiana benthamiana requires the presence of its coat protein (CP), a known suppressor of RNA silencing. RNA transcripts of a TCV construct containing a reporter gene (green fluorescent protein) (TCV-sGFP) in place of the CP open reading frame generated foci of three to five cells. TCV CP delivered in trans by Agrobacterium tumefaciens infiltration potentiated movement of TCV-sGFP and increased foci diameter, on average, by a factor of four. Deletion of the TCV movement proteins in TCV-sGFP (construct TCVΔ92-sGFP) abolished the movement complementation ability of TCV CP. Other known suppressors of RNA silencing from a wide spectrum of viruses also complemented the movement of TCV-sGFP when delivered in trans by Agrobacterium tumefaciens. These include suppressors from nonplant viruses with no known plant movement function, demonstrating that this assay is based solely on RNA silencing suppression. While the TCV-sGFP construct is primarily used as an infectious RNA transcript, it was also subcloned for direct expression from Agrobacterium tumefaciens for simple quantification of suppressor activity based on fluorescence levels in whole leaves. Thus, this system provides the flexibility to assay for suppressor activity in either the cytoplasm or nucleus, depending on the construct employed. }, number={7}, journal={MOLECULAR PLANT-MICROBE INTERACTIONS}, publisher={Scientific Societies}, author={Powers, Jason G. and Sit, Tim L. and Qu, Feng and Morris, T. Jack and Kim, Kook-Hyung and Lommel, Steven A.}, year={2008}, month={Jul}, pages={879–890} }
 @article{loo_guenther_lommel_franzen_2008, title={Infusion of dye molecules into Red clover necrotic mosaic virus}, ISSN={["1359-7345"]}, DOI={10.1039/b714748a}, abstractNote={The Red clover necrotic mosaic virus capsid is utilized to package and release molecules through reversible depletion and re-addition of divalent cations.}, number={1}, journal={CHEMICAL COMMUNICATIONS}, author={Loo, LiNa and Guenther, Richard H. and Lommel, Steven A. and Franzen, Stefan}, year={2008}, pages={88–90} }
 @misc{goodin_zaitlin_naidu_lommel_2008, title={Nicotiana benthamiana: Its history and future as a model for plant-pathogen interactions}, volume={21}, ISSN={["1943-7706"]}, DOI={10.1094/mpmi-21-8-1015}, abstractNote={Nicotiana benthamiana is the most widely used experimental host in plant virology, due mainly to the large number of diverse plant viruses that can successfully infect it. Additionally, N. benthamiana is susceptible to a wide variety of other plant-pathogenic agents (such as bacteria, oomycetes, fungi, and so on), making this species a cornerstone of host–pathogen research, particularly in the context of innate immunity and defense signaling. Moreover, because it can be genetically transformed and regenerated with good efficiency and is amenable to facile methods for virus-induced gene silencing or transient protein expression, N. benthamiana is rapidly gaining popularity in plant biology, particularly in studies requiring protein localization, interaction, or plant-based systems for protein expression and purification. Paradoxically, despite being an indispensable research model, little is known about the origins, genetic variation, or ecology of the N. benthamiana accessions currently used by the research community. In addition to addressing these latter topics, the purpose of this review is to provide information regarding sources for tools and reagents that can be used to support research in N. benthamiana. Finally, we propose that N. benthamiana is well situated to become a premier plant cell biology model, particularly for the virology community, who as a group were the first to recognize the potential of this unique Australian native.}, number={8}, journal={MOLECULAR PLANT-MICROBE INTERACTIONS}, author={Goodin, Michael M. and Zaitlin, David and Naidu, Rayapati A. and Lommel, Steven A.}, year={2008}, month={Aug}, pages={1015–1026} }
 @article{powers_sit_heinsohn_george_kim_lommel_2008, title={The Red clover necrotic mosaic virus RNA-2 encoded movement protein is a second suppressor of RNA silencing}, volume={381}, ISSN={["0042-6822"]}, url={http://www.scopus.com/inward/record.url?eid=2-s2.0-54549091972&partnerID=MN8TOARS}, DOI={10.1016/j.virol.2008.09.004}, abstractNote={The replication complex of Red clover necrotic mosaic virus (RCNMV) has been shown to possess silencing suppression activity. Here a newly developed viral-based assay for the identification of silencing suppression activity was used to provide evidence for a second, mechanistically distinct method of silencing suppression provided for by the RCNMV movement protein (MP). This new assay relies on Turnip crinkle virus with its capsid protein replaced with green fluorescent protein to act as a reporter (TCV-sGFP). In the presence of a protein with silencing suppression activity TCV-sGFP readily moves from cell-to-cell, but in the absence of such a protein TCV-sGFP is confined to small foci of infection. This TCV-sGFP assay was used to identify MP as a suppressor of RNA silencing, to delimit essential amino acids for this activity and uncouple silencing and movement functions.}, number={2}, journal={VIROLOGY}, publisher={Elsevier BV}, author={Powers, Jason G. and Sit, Tim L. and Heinsohn, Curtis and George, Carol G. and Kim, Kook-Hyung and Lommel, Steven A.}, year={2008}, month={Nov}, pages={277–286} }
 @article{loo_guenther_lommel_franzen_2007, title={Encapsidation of nanoparticles by Red Clover Necrotic Mosaic Virus}, volume={129}, ISSN={["1520-5126"]}, DOI={10.1021/ja071896b}, abstractNote={Icosahedral virus capsids demonstrate a high degree of selectivity in packaging cognate nucleic acid genome components during virion assembly. The 36 nm icosahedral plant virus Red clover necrotic mosaic virus (RCNMV) packages its two genomic ssRNAs via a specific capsid protein (CP) genomic RNA interaction. A 20-nucleotide hairpin structure within the genomic RNA-2 hybridizes with RNA-1 to form a bimolecular complex, which is the origin of assembly (OAS) in RCNMV that selectively recruits and orients CP subunits initiating virion assembly. In this Article, an oligonucleotide mimic of the OAS sequence was attached to Au, CoFe2O4, and CdSe nanoparticles ranging from 3 to 15 nm, followed by addition of RNA-1 to form a synthetic OAS to direct the virion-like assembly by RCNMV CP. Dynamic light scattering (DLS) and transmission electron microscopy (TEM) measurements were consistent with the formation of virus-like particles (VLPs) comparable in size to native RCNMV. Attempts to encapsidate nanoparticles with diameters larger than 17 nm did not result in well-formed viral capsids. These results are consistent with the presence of a 17 nm cavity in native RCNMV. Covalent linkage of the OAS to nanoparticles directs RNA-dependent encapsidation and demonstrates that foreign cargo can be packaged into RCNMV virions. The flexibility of the RCNMV CP to encapsidate different materials, as long as it is within encapsidation constraint, is a critical factor to be considered as a drug delivery and diagnostic vehicle in biomedical applications.}, number={36}, journal={JOURNAL OF THE AMERICAN CHEMICAL SOCIETY}, author={Loo, LiNa and Guenther, Richard H. and Lommel, Steven A. and Franzen, Stefan}, year={2007}, month={Sep}, pages={11111–11117} }
 @article{loo_guenther_basnayake_lommel_franzen_2006, title={Controlled encapsidation of gold nanoparticles by a viral protein shell}, volume={128}, ISSN={["0002-7863"]}, DOI={10.1021/ja057332u}, abstractNote={Icosahedral virus capsids demonstrate a high degree of selectivity in packaging cognate nucleic acid components during assembly. This packaging specificity, when integrated as part of a nanotechnological protocol, has the potential to encapsidate a wide array of foreign materials for delivery of therapeutics or biosensors into target cells. Red clover necrotic mosaic virus (RCNMV) exclusively packages two genomic ssRNAs initiated by a specific protein:RNA interaction between the RCNMV coat protein (CP) and the viral RNA origin of assembly (OAS) element. In the present work, an oligonucleotide mimic of the RCNMV OAS sequences is attached to Au nanoparticles as a recognition signal to initiate the virion-like assembly by RCNMV CP. Covalent linkage of the OAS to Au functions as a trigger for specific encapsidation and demonstrates that foreign cargo can be packaged into RCNMV virions.}, number={14}, journal={JOURNAL OF THE AMERICAN CHEMICAL SOCIETY}, author={Loo, L and Guenther, RH and Basnayake, VR and Lommel, SA and Franzen, S}, year={2006}, month={Apr}, pages={4502–4503} }
 @article{franzen_belyea_gilvey_davis_chaudhary_sit_lommel_2006, title={Proximal cavity, distal histidine, and substrate hydrogen-bonding mutations modulate the activity of Amphitrite ornata dehaloperoxidase}, volume={45}, ISSN={["0006-2960"]}, url={http://www.scopus.com/inward/record.url?eid=2-s2.0-33746584767&partnerID=MN8TOARS}, DOI={10.1021/bi060020z}, abstractNote={Dehaloperoxidase (DHP) from Amphitrite ornata is the first globin that has peroxidase activity that approaches that of heme peroxidases. The substrates 2,4,6-tribromophenol (TBP) and 2,4,6-trichlorophenol are oxidatively dehalogenated by DHP to form 2,6-dibromo-1,4-benzoquinone and 2,6-dichloro-1,4-benzoquinone, respectively. There is a well-defined internal substrate-binding site above the heme, a feature not observed in other globins or peroxidases. Given that other known heme peroxidases act on the substrate at the heme edge there is great interest in understanding the possible modes of substrate binding in DHP. Stopped-flow studies (Belyea, J., Gilvey, L. B., Davis, M. F., Godek, M., Sit, T. L., Lommel, S. A., and Franzen, S. (2005) Biochemistry 44, 15637-15644) show that substrate binding must precede the addition of H2O2. This observation suggests that the mechanism of DHP relies on H2O2 activation steps unlike those of other known peroxidases. In this study, the roles of the distal histidine (H55) and proximal histidine (H89) were probed by the creation of site-specific mutations H55R, H55V, H55V/V59H, and H89G. Of these mutants, only H55R shows significant enzymatic activity. H55R is 1 order of magnitude less active than wild-type DHP and has comparable activity to sperm whale myoglobin. The role of tyrosine 38 (Y38), which hydrogen bonds to the hydroxyl group of the substrate, was probed by the mutation Y38F. Surprisingly, abolishing this hydrogen bond increases the activity of the enzyme for the substrate TBP. However, it may open a pathway for the escape of the one-electron product, the phenoxy radical leading to polymeric products.}, number={30}, journal={BIOCHEMISTRY}, publisher={American Chemical Society (ACS)}, author={Franzen, Stefan and Belyea, Jennifer and Gilvey, Lauren B. and Davis, Michael F. and Chaudhary, Chelsea E. and Sit, Tim L. and Lommel, Steven A.}, year={2006}, month={Aug}, pages={9085–9094} }
 @article{sherman_guenther_tama_sit_brooks_mikhailov_orlova_baker_lommel_2006, title={Removal of divalent cations induces structural transitions in Red clover necrotic mosaic virus, revealing a potential mechanism for RNA release}, volume={80}, ISSN={["1098-5514"]}, url={http://www.scopus.com/inward/record.url?eid=2-s2.0-33750318283&partnerID=MN8TOARS}, DOI={10.1128/JVI.01137-06}, abstractNote={ABSTRACT}, number={21}, journal={JOURNAL OF VIROLOGY}, publisher={American Society for Microbiology}, author={Sherman, Michael B. and Guenther, Richard H. and Tama, Florence and Sit, Tim L. and Brooks, Charles L. and Mikhailov, Albert M. and Orlova, Elena V. and Baker, Timothy S. and Lommel, Steven A.}, year={2006}, month={Nov}, pages={10395–10406} }
 @article{basnayake_sit_lommel_2006, title={The genomic RNA packaging scheme of Red clover necrotic mosaic virus}, volume={345}, ISSN={["0042-6822"]}, url={http://www.scopus.com/inward/record.url?eid=2-s2.0-31944440651&partnerID=MN8TOARS}, DOI={10.1016/j.virol.2005.10.017}, abstractNote={Red clover necrotic mosaic virus (RCNMV) is a small icosahedral plant virus with a bipartite RNA genome. While the RCNMV genome consists of two RNAs, it has not been definitively established whether these RNAs are co-packaged into a single virion or packaged individually into separate virions. Biochemical evidence exists to support both hypotheses. To determine the genomic RNA complement within RCNMV, virions were subjected to heat treatments and UV crosslinking. A stable RNA-1:RNA-2 heterodimer was formed with both treatments establishing that RCNMV genomic RNAs are co-packaged into a single virion. Furthermore, RNA-2 homodimer and homotrimers were also observed indicating that some virions contain multiple copies of RNA-2 exclusively. These results indicate that RCNMV virions consist of two distinct populations: (i) virions containing both genomic RNAs; and (ii) virions with multiple copies of RNA-2. This type of hybrid packaging arrangement was unexpected and appears to be unique among the multipartite RNA viruses.}, number={2}, journal={VIROLOGY}, publisher={Elsevier BV}, author={Basnayake, VR and Sit, TL and Lommel, SA}, year={2006}, month={Feb}, pages={532–539} }
 @article{tremblay_vaewhongs_turner_sit_lommel_2005, title={Cell wall localization of Red clover necrotic mosaic virus movement protein is required for cell-to-cell movement}, volume={333}, ISSN={["0042-6822"]}, url={http://www.scopus.com/inward/record.url?eid=2-s2.0-13644249879&partnerID=MN8TOARS}, DOI={10.1016/j.virol.2004.12.019}, abstractNote={The Red clover necrotic mosaic virus movement protein (MP) is essential for cell-to-cell movement. Eight previously characterized alanine-scanning mutants of the MP were fused to the green fluorescent protein (GFP) and expressed from viral infectious transcripts. Inoculated plants were assayed for movement and intracellular accumulation of MP by confocal laser-scanning microscopy. A strict correlation was observed between the targeting to the cell wall (presumably the plasmodesmata) and cell-to-cell movement. Complementation of dysfunctional MP mutants with either wild-type MP or other null mutants in some cases rescued intracellular targeting and movement. The data suggest the presence of distinct domains in the MP for virus movement (near residues 27–31), complementarity (near residues 122 and 128), and intracellular localization (near residue 161). These data support a model of MP interacting cooperatively with itself to bind viral RNA, localize to and modify plasmodesmata and effect virus movement.}, number={1}, journal={VIROLOGY}, publisher={Elsevier BV}, author={Tremblay, D and Vaewhongs, AA and Turner, KA and Sit, TL and Lommel, SA}, year={2005}, month={Mar}, pages={10–21} }
 @article{belyea_gilvey_davis_godek_sit_lommel_franzen_2005, title={Enzyme function of the globin dehaloperoxidase from Amphitrite ornata is activated by substrate binding}, volume={44}, ISSN={["0006-2960"]}, url={http://www.scopus.com/inward/record.url?eid=2-s2.0-28544440508&partnerID=MN8TOARS}, DOI={10.1021/bi051731k}, abstractNote={Amphitrite ornata dehaloperoxidase (DHP) is a heme enzyme with a globin structure, which is capable of oxidizing para-halogenated phenols to the corresponding quinones. Cloning, high-level expression, and purification of recombinant DHP are described. Recombinant DHP was assayed by stopped-flow experiments for its ability to oxidatively debrominate 2,4,6-tribromophenol (TBP). The enzymatic activity of the ferric form of recombinant DHP is intermediate between that of a typical peroxidase (horseradish peroxidase) and a typical globin (horse heart myoglobin). The present study shows that, unlike other known peroxidases, DHP activity requires the addition of substrate, TBP, prior to the cosubstrate, peroxide. The presence of a substrate-binding site in DHP is consistent with a two-electron oxidation mechanism and an obligatory order for activation of the enzyme by addition of the substrate prior to the cosubstrate.}, number={48}, journal={BIOCHEMISTRY}, publisher={American Chemical Society (ACS)}, author={Belyea, J and Gilvey, LB and Davis, MF and Godek, M and Sit, TL and Lommel, SA and Franzen, S}, year={2005}, month={Dec}, pages={15637–15644} }
 @article{ladipo_lommel_barnett_2005, title={Identification and characterization of cowpea aphid-borne mosaic virus as the second virus from mixed-infected Crotalaria juncea plants in Nigeria}, volume={112}, number={3}, journal={Zeitschrift fur Pflanzenkrankheiten und Pflanzenschutz}, author={Ladipo, J. L. and Lommel, S. A. and Barnett, O. W.}, year={2005}, pages={222–228} }
 @article{callaway_george_lommel_2004, title={A Sobemovirus coat protein gene complements long-distance movement of a coat protein-null Dianthovirus}, volume={330}, ISSN={["0042-6822"]}, DOI={10.1016/j.virol.2004.09.037}, abstractNote={Red clover necrotic mosaic virus (RCNMV; genus Dianthovirus) and Turnip rosette virus (TRoV; genus Sobemovirus) are taxonomically and ecologically distinct plant viruses. In addition, the two genera differ in the role of coat protein (CP) in cell-to-cell movement. However, both are small icosahedral viruses requiring CP for systemic movement in the host vasculature. Here, we show that the TRoV CP gene is capable of facilitating the vascular movement of a Dianthovirus. Substitution of the RCNMV CP gene with the TRoV CP gene permits movement of the resulting chimeric virus to non-inoculated leaves. RCNMV lacking a CP gene or containing a non-translatable TRoV CP gene do not move systemically. This report introduces the molecular characterization of TRoV and describes the unprecedented complementation of systemic movement function by intergenic complete substitution of a plant virus CP gene.}, number={1}, journal={VIROLOGY}, author={Callaway, AS and George, CG and Lommel, SA}, year={2004}, month={Dec}, pages={186–195} }
 @article{turner_sit_callaway_allen_lommel_2004, title={Red clover necrotic mosaic virus replication proteins accumulate at the endoplasmic reticulum}, volume={320}, ISSN={["0042-6822"]}, url={http://www.scopus.com/inward/record.url?eid=2-s2.0-1542285421&partnerID=MN8TOARS}, DOI={10.1016/j.virol.2003.12.006}, abstractNote={Red clover necrotic mosaic virus (RCNMV) encodes N-terminally overlapping proteins of 27 and 88 kDa (p27 and p88) known to be required for replication. Green fluorescent protein (GFP) fusions were used to visualize the location of p27 and p88 within Nicotiana benthamiana cells. GFP:p27 fusions localized to the endoplasmic reticulum (ER), co-localized with ER-targeted yellow fluorescent protein and caused membrane restructuring and proliferation. Cellular fractionation of virus-inoculated N. benthamiana leaves confirmed the association of p27 with ER membranes. GFP:p88 fusions also localized to the ER and co-localized with GFP:p27. Both fusion proteins co-localize to the cortical and cytoplasmic ER and were associated with invaginations of the nuclear envelope. Independent accumulation in, and perturbation of, the ER suggests that p27 and p88 function together in the replication complex. This is the first report of a member of the Tombusviridae replicating in association with the ER.}, number={2}, journal={VIROLOGY}, publisher={Elsevier BV}, author={Turner, KA and Sit, TL and Callaway, AS and Allen, NS and Lommel, SA}, year={2004}, month={Mar}, pages={276–290} }
 @article{guenther_sit_gracz_dolan_townsend_liu_newman_agris_lommel_2004, title={Structural characterization of an intermolecular RNA-RNA interaction involved in the transcription regulation element of a bipartite plant virus}, volume={32}, ISSN={["1362-4962"]}, url={http://www.scopus.com/inward/record.url?eid=2-s2.0-3042761419&partnerID=MN8TOARS}, DOI={10.1093/nar/gkh585}, abstractNote={The 34-nucleotide trans-activator (TA) located within the RNA-2 of Red clover necrotic mosaic virus folds into a simple hairpin. The eight-nucleotide TA loop base pairs with eight complementary nucleotides in the TA binding sequence (TABS) of the capsid protein subgenomic promoter on RNA-1 and trans-activates subgenomic RNA synthesis. Short synthetic oligoribonucleotide mimics of the RNA-1 TABS and the RNA-2 TA form a weak 1:1 bimolecular complex in vitro with a K(a) of 5.3 x 10(4) M(-1). K(a) determination for a series of RNA-1 and RNA-2 mimic variants indicated optimum stability is obtained with seven-base complementarity. Thermal denaturation and NMR show that the RNA-1 TABS 8mers are weakly ordered in solution while RNA-2 TA oligomers form the predicted hairpin. NMR diffusion studies confirmed RNA-1 and RNA-2 oligomer complex formation in vitro. MC-Sym generated structural models suggest that the bimolecular complex is composed of two stacked helices, one being the stem of the RNA-2 TA hairpin and the other formed by the intermolecular base pairing between RNA-1 and RNA-2. The RCNMV TA structural model is similar to those for the Simian retrovirus frameshifting element and the Human immunodeficiency virus-1 dimerization kissing hairpins, suggesting a conservation of form and function.}, number={9}, journal={NUCLEIC ACIDS RESEARCH}, publisher={Oxford University Press (OUP)}, author={Guenther, RH and Sit, TL and Gracz, HS and Dolan, MA and Townsend, HL and Liu, GH and Newman, WH and Agris, PF and Lommel, SA}, year={2004}, month={May}, pages={2819–2828} }
 @article{sherman_orlova_guenther_lommel_mikhailov_baker_2004, title={The Structure of Red Clover Necrostic Mosaic Dianthovirus at 10 Å Resolution}, volume={10}, ISSN={1431-9276 1435-8115}, url={http://dx.doi.org/10.1017/S1431927604880103}, DOI={10.1017/S1431927604880103}, abstractNote={Extended abstract of a paper presented at Microscopy and Microanalysis 2004 in Savannah, Georgia, USA, August 1–5, 2004.}, number={S02}, journal={Microscopy and Microanalysis}, publisher={Cambridge University Press (CUP)}, author={Sherman, Michael B and Orlova, Elena V and Guenther, Richard H and Lommel, Steven A and Mikhailov, Albert M and Baker, Timothy S}, year={2004}, month={Aug}, pages={1486–1487} }
 @article{fellers_tremblay_handest_lommel_2002, title={The Potato virus Y (MNR)-N-S Nlb-replicase is the elicitor of a veinal necrosis-hypersensitive response in root knot nematode resistant tobacco}, volume={3}, ISSN={["1464-6722"]}, DOI={10.1046/j.1364-3703.2002.00106.x}, abstractNote={Summary}, number={3}, journal={MOLECULAR PLANT PATHOLOGY}, author={Fellers, JP and Tremblay, D and Handest, MF and Lommel, SA}, year={2002}, month={May}, pages={145–152} }
 @article{sit_haikal_callaway_lommel_2001, title={A single amino acid mutation in the Carnation ringspot virus capsid protein allows virion formation but prevents systemic infection}, volume={75}, ISSN={["0022-538X"]}, url={http://www.scopus.com/inward/record.url?eid=2-s2.0-0034853341&partnerID=MN8TOARS}, DOI={10.1128/JVI.75.19.9538-9542.2001}, abstractNote={ABSTRACT}, number={19}, journal={JOURNAL OF VIROLOGY}, publisher={American Society for Microbiology}, author={Sit, TL and Haikal, PR and Callaway, AS and Lommel, SA}, year={2001}, month={Oct}, pages={9538–9542} }
 @misc{callaway_giesman-cookmeyer_gillock_sit_lommel_2001, title={The multifunctional capsid proteins of plant RNA viruses}, volume={39}, ISSN={["1545-2107"]}, url={http://www.scopus.com/inward/record.url?eid=2-s2.0-0034799288&partnerID=MN8TOARS}, DOI={10.1146/annurev.phyto.39.1.419}, abstractNote={▪ Abstract  This article summarizes studies of viral coat (capsid) proteins (CPs) of RNA plant viruses. In addition, we discuss and seek to interpret the knowledge accumulated to date. CPs are named for their primary function; to encapsidate viral genomic nucleic acids. However, encapsidation is only one feature of an extremely diverse array of structural, functional, and ecological roles played during viral infection and spread. Herein, we consider the evolution of viral CPs and their multitude of interactions with factors encoded by the virus, host plant, or viral vector (biological transmission agent) that influence the infection and epidemiological facets of plant disease. In addition, applications of today's understanding of CPs in the protection of crops from viral infection and use in the manufacture of valuable compounds are considered.}, number={1}, journal={ANNUAL REVIEW OF PHYTOPATHOLOGY}, publisher={Annual Reviews}, author={Callaway, A and Giesman-Cookmeyer, D and Gillock, ET and Sit, TL and Lommel, SA}, year={2001}, pages={419-+} }
 @article{wang_wang_giesman-cookmeyer_lommel_lucas_1998, title={Mutations in viral movement protein alter systemic infection and identify an intercellular barrier to entry into the phloem long-distance transport system}, volume={245}, ISSN={["0042-6822"]}, DOI={10.1006/viro.1998.9154}, abstractNote={Viral systemic infection of a plant host involves two processes, cell-to-cell movement and long-distance transport. Molecular determinants associated with these two processes were probed by investigating the effects that alanine scanning mutations in the movement protein (MP) of red clover necrotic mosaic virus (RCNMV) had on viral infection in the plant hosts Nicotiana edwardsonii, Vigna unguiculata (cowpea), and the experimental plant Nicotiana benthamiana. Plants were inoculated with RCNMV expressing wild-type and mutant forms of the MP. Immunocytochemical studies at the light and electron microscope levels were performed on these plants, using a polyclonal antibody raised against the RCNMV capsid protein to identify the cells/tissues that RCNMV could infect. These experiments demonstrated that one cellular boundary at which the RCNMV MP functions to facilitate entry into the phloem long-distance transport system is located at the interfaces between the bundle sheath and phloem parenchyma cells and the companion cell-sieve element complex. Interestingly, in Nicotiana tabacum, a host that only allows a local infection, RCNMV cell-to-cell movement was found to be blocked at this same intercellular boundary. Four mutants that were able to systemically infect N. benthamiana were partially or completely defective for systemic infection of N. edwardsonii and cowpea, which indicated that these MP mutants exhibited host-specific defects. Thus, the roles of the RCNMV MP in cell-to-cell movement and in long-distance transport appear to be genetically distinct. These results are discussed in terms of the mechanism by which RCN MV enters the phloem to establish a systemic infection.}, number={1}, journal={VIROLOGY}, author={Wang, HL and Wang, Y and Giesman-Cookmeyer, D and Lommel, SA and Lucas, WJ}, year={1998}, month={May}, pages={75–89} }
 @article{sit_vaewhongs_lommel_1998, title={RNA-mediated trans-activation of transcription from a viral RNA}, volume={281}, ISSN={["0036-8075"]}, url={http://www.scopus.com/inward/record.url?eid=2-s2.0-0032493916&partnerID=MN8TOARS}, DOI={10.1126/science.281.5378.829}, abstractNote={The red clover necrotic mosaic virus genome is composed of two single-stranded RNA components, RNA-1 and RNA-2. The viral capsid protein is translated from a subgenomic RNA (sgRNA) that is transcribed from genomic RNA-1. Here, a 34-nucleotide sequence in RNA-2 is shown to be required for transcription of sgRNA. Mutations that prevent base-pairing between the RNA-1 subgenomic promoter and the 34-nucleotide trans-activator prevent expression of a reporter gene. A model is proposed in which direct binding of RNA-2 to RNA-1 trans-activates sgRNA synthesis. This RNA-mediated regulation of transcription is unusual among RNA viruses, which typically rely on protein regulators.}, number={5378}, journal={SCIENCE}, publisher={American Association for the Advancement of Science (AAAS)}, author={Sit, TL and Vaewhongs, AA and Lommel, SA}, year={1998}, month={Aug}, pages={829–832} }
 @article{walker_leath_murphy_lommel_1998, title={Selection for resistance and tolerance to oat mosaic virus and oat golden stripe virus in hexaploid oats}, volume={82}, ISSN={["0191-2917"]}, DOI={10.1094/PDIS.1998.82.4.423}, abstractNote={ Coker 716, a hexaploid oat cultivar resistant to both oat mosaic virus (OMV) and oat golden stripe virus (OGSV) was crossed to three susceptible cultivars (Brooks, Madison, and Tech) to form three individual populations. Individual breeding lines were derived from each cross in the F2 generation and tested in plots consisting of equally spaced individual hills in OMV- and OGSV-infested soils and non-infested soils to evaluate resistance and yield loss of individual lines. Foliar symptoms, harvest index, and yield loss were examined as selection criteria for resistant genotypes. The study was conducted over 2 years at two North Carolina locations that differed in soil type and climate. Multiple regression models describing yield loss in each cross due to rating, year, and location were calculated. Coefficients of multiple determination in these models ranged from 0.39 to 0.51. Yield loss ranged from 39 to 60% among different crosses. Infection by OMV and OGSV accounted for the majority of yield loss in two of the populations. Disease severity varied widely over years and locations. The results suggest that selection of lines with symptomatic tissue of 10% or less, or selection of tolerant lines, is needed for breeding progress. }, number={4}, journal={PLANT DISEASE}, author={Walker, SL and Leath, S and Murphy, JP and Lommel, SA}, year={1998}, month={Apr}, pages={423–427} }
 @article{kim_lommel_1998, title={Sequence element required for efficient -1 ribosomal frameshifting in red clover necrotic mosaic dianthovirus}, volume={250}, ISSN={["0042-6822"]}, DOI={10.1006/viro.1998.9358}, abstractNote={The RNA-1 of the bipartite red clover necrotic mosaic dianthovirus (RCNMV) genome encodes the 88-kDa polymerase. The polymerase is translated from both 5' proximal and internal open reading frames by a -1 ribosomal frameshifting event. A shifty heptanucleotide conforming to the simultaneous slippage model is identified, and a downstream stem-loop structure and atypical pseudoknot are predicted. A beta-glucuronidase reporter assay identified a 118-nucleotide element containing both the shifty heptanucleotide and the predicted secondary structures that were required for efficient -1 ribosomal frameshift expression in vivo. A series of site-directed and compensatory mutations affecting the base-paired regions of the predicted secondary structure were introduced into a RCNMV RNA-1 cDNA clone from which infectious transcripts were derived. Mutations that destroyed the predicted pseudoknot had no effect on frameshifting efficiency in vitro or infectivity of the virus, whereas mutations destabilizing the stem-loop structure abolished both ribosomal frameshifting in vitro and biological activity. These results demonstrate the essential role of a predicted secondary structure that does not involve a pseudoknot in the expression of the RCNMV polymerase by ribosomal frameshifting.}, number={1}, journal={VIROLOGY}, author={Kim, KH and Lommel, SA}, year={1998}, month={Oct}, pages={50–59} }
 @misc{lommel_sit_1998, title={Trans-activation of transcription from viral RNA}, volume={6,433,248}, number={1998 Jun 01}, publisher={Washington, DC: U.S. Patent and Trademark Office}, author={Lommel, S. A. and Sit, T. L.}, year={1998} }
 @article{heidel_rush_kendall_lommel_french_1997, title={Characteristics of beet soilborne mosaic virus, a furo-like virus infecting sugar beet}, volume={81}, ISSN={["1943-7692"]}, DOI={10.1094/PDIS.1997.81.9.1070}, abstractNote={ Beet soilborne mosaic virus (BSBMV) is a rigid rod-shaped virus transmitted by Polymyxa betae. Particles were 19 nm wide and ranged from 50 to over 400 nm, but no consistent modal lengths could be determined. Nucleic acids extracted from virions were polyadenylated and typically separated into three or four discrete bands of variable size by agarose-formaldehyde gel electrophoresis. RNA 1 and 2, the largest of the RNAs, consistently averaged 6.7 and 4.6 kb, respectively. The sizes and number of smaller RNA species were variable. The molecular mass of the capsid protein of BSBMV was estimated to be 22.5 kDa. In Northern blots, probes specific to the 3′ end of individual beet necrotic yellow vein virus (BNYVV) RNAs 1–4 hybridized strongly with the corresponding BNYVV RNA species and weakly with BSBMV RNAs 1, 2, and 4. Probes specific to the 5′ end of BNYVV RNAs 1–4 hybridized with BNYVV but not with BSBMV. No cross-reaction between BNYVV and BSBMV was detected in Western blots. In greenhouse studies, root weights of BSBMV-infected plants were significantly lower than mock-inoculated controls but greater than root weights from plants infected with BNYVV. Results of serological, hybridization, and virulence experiments indicate that BSBMV is distinct from BNYVV. However, host range, capsid size, and the number, size, and polyadenylation of its RNAs indicate that BSBMV more closely resembles BNYVV than it does other members of the genus Furovirus. }, number={9}, journal={PLANT DISEASE}, author={Heidel, GB and Rush, CM and Kendall, TL and Lommel, SA and French, RC}, year={1997}, month={Sep}, pages={1070–1076} }
 @article{lommel_kendall_siu_nutter_1991, title={CHARACTERIZATION OF MAIZE CHLOROTIC MOTTLE VIRUS}, volume={81}, ISSN={["0031-949X"]}, DOI={10.1094/Phyto-81-819}, abstractNote={Maize chlorotic mottle virus (MCMV) is an icosahedral plant virus 30 nm in diameter, composed of a single 25-kDa capsid protein subunit and a 4.4-kb single-stranded, positive-sense genomic RNA. The genomic RNA is capped at the 5'terminus with m 7 GpppA, and no genome-linked protein was detected. MCMV infection produces two discrete double-stranded RNA species in infected maize plants, corresponding to single-stranded RNAs of 4.4 and 1.1 kb (...)}, number={8}, journal={PHYTOPATHOLOGY}, author={LOMMEL, SA and KENDALL, TL and SIU, NF and NUTTER, RC}, year={1991}, month={Aug}, pages={819–823} }
 @article{lommel_kendall_xiong_nutter_1991, title={IDENTIFICATION OF THE MAIZE CHLOROTIC MOTTLE VIRUS CAPSID PROTEIN CISTRON AND CHARACTERIZATION OF ITS SUBGENOMIC MESSENGER-RNA}, volume={181}, ISSN={["0042-6822"]}, DOI={10.1016/0042-6822(91)90509-A}, abstractNote={Maize chlorotic mottle virus (MCMV) is a 30-nm icosahedral plant virus composed of a single 25-kDa capsid protein component and a 4.4-kb single-stranded, positive-sense genomic RNA. Northern blot hybridization analysis detected a single 3′-terminal 1.1-kb subgenomic RNA in infected plants. Virion RNA directs the synthesis of several polypeptides in a rabbit reticulocyte lysate in vitro translation system of which only the 25-kDa polypeptide is immunoprecipitated by MCMV capsid protein antiserum. The 1.1-kb subgenomic RNA is a highly efficient messenger RNA for capsid protein synthesis. Positive polarity in vitro transcripts from 3′-proximal MCMV cDNA clones direct the synthesis of the capsid protein in in vitro translation experiments. These data suggest that the MCMV capsid protein is expressed from a subgenomic RNA in vivo, and that the 25-kDa capsid protein is encoded by the 3′-proximal open reading frame in the MCMV genome.}, number={1}, journal={VIROLOGY}, author={LOMMEL, SA and KENDALL, TL and XIONG, Z and NUTTER, RC}, year={1991}, month={Mar}, pages={382–385} }