@book{sonenshine_roe_2014, title={Biology of ticks}, publisher={New York: Oxford University Press}, year={2014} }
 @article{cabrera_donohue_khalil_sonenshine_roe_2009, title={Characterization of vitellin protein in the twospotted spider mite, Tetranychus urticae (Acari: Tetranychidae)}, volume={55}, ISSN={["1879-1611"]}, DOI={10.1016/j.jinsphys.2009.04.006}, abstractNote={In mites, vitellogenin synthesis, regulation and uptake by the oocytes as vitellin remain practically unknown. Although a partial sequence of the gene is now available, no previous studies have been conducted that describe the native vitellin protein in mites. The objective of this study was to characterize vitellin in the twospotted spider mite, Tetranychus urticae. The native twospotted spider mite vitellin migrated as a single major band with a molecular weight of 476 ± 14.5 kDa as compared to 590 ± 25.5 kDa for vitellin from the American dog tick, Dermacentor variabilis. However, isoelectric focusing analysis of native spider mite vitellin showed five bands with pI values slightly acidic to neutral (pH 5.8, 6.2, 6.7, 7.0 and 7.2), as is the case for insect and tick vitellins. Reducing conditions (SDS-PAGE) also revealed multiple subunits ranging from 290.9 to 3.6 kDa and was similar to that found in D. variabilis. Spider mite vitellin weakly bound lipids and carbohydrates compared to the tick. Unlike D. variabilis, the spider mite egg yolk protein does not bind heme. The significance of non-heme binding in mites is discussed.}, number={7}, journal={JOURNAL OF INSECT PHYSIOLOGY}, author={Cabrera, Ana R. and Donohue, Kevin V. and Khalil, Sayed M. S. and Sonenshine, Daniel E. and Roe, R. Michael}, year={2009}, month={Jul}, pages={655–661} }
 @article{bissinger_apperson_sonenshine_watson_roe_2009, title={Efficacy of the new repellent BioUD(A (R)) against three species of ixodid ticks}, volume={48}, ISSN={["1572-9702"]}, DOI={10.1007/s10493-008-9235-x}, abstractNote={BioUD ® with the active ingredient 2-undecanone originally derived from wild tomato plants is a new repellent recently registered by the US EPA. Repellent efficacy of BioUD ® (7.75% 2-undecanone) and DEET (98.11%) was examined in the laboratory using a choice test between repellent-treated and control filter paper surfaces for Amblyomma americanum, Dermacentor variabilis, and Ixodes scapularis. BioUD ® provided greater repellency against A. americanum and I. scapularis than DEET. No difference was found between BioUD ® and DEET against D. variabilis. In head-to-head assays between BioUD ® and DEET, undiluted and 50% dilutions of BioUD® were more repellent than undiluted DEET against all three species tested. Similarly, a 25% dilution of BioUD® was more repellent than DEET against A. americanum while no difference in mean percentage repellency was found between a 25% dilution of BioUD® and DEET against I. scapularis. Based on regression analysis, the concentration of BioUD® required for equivalent repellency to 98.11% DEET was 39.5% for D. variabilis and 29.7% for I. scapularis. A log-probit model could not be constructed for A. americanum from the dosages tested. Based on filter paper head-to-head assays, BioUD® is at least 2–4 times more active as a repellent than DEET against three species of ixodid ticks under the conditions of our laboratory bioassays.}, number={3}, journal={EXPERIMENTAL AND APPLIED ACAROLOGY}, author={Bissinger, B. W. and Apperson, C. S. and Sonenshine, D. E. and Watson, D. W. and Roe, R. M.}, year={2009}, month={Jul}, pages={239–250} }
 @misc{donohue_khalil_sonenshine_roe_2009, title={Heme-binding storage proteins in the Chelicerata}, volume={55}, ISSN={["1879-1611"]}, DOI={10.1016/j.jinsphys.2009.01.002}, abstractNote={Lipoglycoproteins in the Chelicerata that bind and store heme appear to represent a unique evolutionary strategy to both mitigate the toxicity of heme and utilize the molecule as a prosthetic group. Knowledge of heme-binding storage proteins in these organisms is in its infancy and much of what is known is from studies with vitellogenins (Vg) and more recently the main hemolymph storage protein in ixodid ticks characterized as a hemelipoglyco-carrier protein (CP). Data have also been reported from another arachnid, the black widow spider, Latrodectus mirabilis, and seem to suggest that the heme-binding capability of these large multimeric proteins is not a phenomenon found only in the Acari. CP appears to be most closely related to Vg in ticks in terms of primary structure but post-translational processing is different. Tick CP and L. mirabilis high-density lipoprotein 1 (HDL1) are similar in that they consist of two subunits of approximate molecular masses of 90 and 100 kDa, are found in the hemolymph as the dominant protein, and bind lipids, carbohydrates and cholesterol. CP binds heme which may also be the case for HDL1 since the protein was found to contain a brown pigment when analyzed by native polyacrylamide gel electrophoresis. Vgs in ticks are composed of multiple subunits and are the precursor of the yolk protein, vitellin. The phylogeny of these proteins, regulation of gene expression and putative functions of binding and storing heme throughout reproduction, blood-feeding and development are discussed. Comparisons with non-chelicerate arthropods are made in order to highlight the mechanisms and putative functions of heme-binding storage proteins and their possible critical function in the evolution of hematophagy.}, number={4}, journal={JOURNAL OF INSECT PHYSIOLOGY}, author={Donohue, Kevin V. and Khalil, Sayed M. S. and Sonenshine, Daniel E. and Roe, R. Michael}, year={2009}, month={Apr}, pages={287–296} }
 @misc{roe_donohue_khalil_sonenshine_2008, title={Hormonal regulation of metamorphosis and reproduction in ticks}, volume={13}, journal={Frontiers in Bioscience}, author={Roe, R. M. and Donohue, K. V. and Khalil, S. M. S. and Sonenshine, D. E.}, year={2008}, pages={7250–7268} }
 @article{donohue_khalil_mitchell_sonenshine_roe_2008, title={Molecular characterization of the major hemelipoglycoprotein in ixodid ticks}, volume={17}, ISSN={["1365-2583"]}, DOI={10.1111/j.1365-2583.2008.00794.x}, abstractNote={AbstractThe major hemelipoglyco‐carrier protein (CP) found throughout the development of male and female adult American dog ticks, Dermacentor variabilis (Say) was sequenced. DvCP is a single transcript coding for two protein subunits that together contain three motifs: (1) a lipoprotein n‐terminal domain that is a common attribute of proteins that bind lipids, carbohydrates and metals; (2) a domain of unknown function characteristic of proteins with several large open beta sheets; and (3) a von Willebrand factor type D domain near the carboxy‐terminus apparently important for multimerization. These motifs, which are also found in tick vitellogenin, are not shared by heme‐binding proteins studied thus far in other hematophagous insects. DvCP message was highest in fat body and salivary gland but was also found in midgut and ovary tissue. Expression was initiated by blood feeding in virgin females and not by mating, as is typical of tick vitellogenin; and the message was found in fed males at levels similar to part fed, virgin females. CP appears to be highly conserved among the Ixodida. The closest match by BlastP to DvCP is vitellogenin from Caenorhabditis elegans (AAC04423), suggesting that CP is a novel protein. The role of CP in heme sequestration, the evolution of hematophagy and host complementation are discussed.}, number={3}, journal={INSECT MOLECULAR BIOLOGY}, author={Donohue, K. V. and Khalil, S. M. S. and Mitchell, R. D. and Sonenshine, D. E. and Roe, R. Michael}, year={2008}, month={Jun}, pages={197–208} }
 @article{deborah_khalil_jeffers_sonenshine_mitchell_osgood_roe_2007, title={Sequence and the developmental and tissue-specific regulation of the first complete vitellogenin messenger RNA from ticks responsible for heme sequestration}, volume={37}, ISSN={["0965-1748"]}, DOI={10.1016/j.ibmb.2007.01.004}, abstractNote={The first full-length mRNA for vitellogenin (Vg) from ticks was sequenced. This also represents the first complete sequence of Vg from the Chelicerata and of a heme binding Vg. The Vg cDNA from the American dog tick, Dermacentor variabilis was 5744 nt in length (GenBank Accession number AY885250), which coded for a protein of 1843 aa with a calculated molecular weight of 208 kD. This protein had an 18 aa signal sequence, a single RXXR cleavage signal that would generate two subunits (49.5 and 157 K in molecular weight) and lipoprotein N-terminal and carboxy von Willebrand factor type D domains. Tryptic digest MS analysis of vitellin protein confirmed the function of the cDNA as the tick yolk protein. Apparently, vitellin in D. variabilis is oligomeric (possibly dimeric) and is comprised of a mixture of the uncleaved monomer and subunits that were predicted from the single RXXR cleavage signal. The highly conserved GL/ICG motif close to the C-terminus in insect Vg genes was different in the tick Vg message, i.e., GLCS. This variant was also present in a partial sequence of Vg from Boophilus microplus. Phylogenic analysis showed that the full length Vg cDNA from D. variabilis and the partial cDNA from B. microplus were distinct from insects and Crustacea. The Vg message was not found in whole body RNA from unfed or fed males or in unfed and partially fed (virgin) females as determined by Northern blotting. The message was found in replete (mated) pre-ovipositional females, increased to higher levels in ovipositing females and was absent after egg laying was complete. The endocrine regulation of the Vg mRNA is discussed. The tissue sources of the Vg message are both the gut and fat body. Tryptic digest MS fingerprinting suggests that a second Vg mRNA might be present in the American dog tick, which needs further study.}, number={4}, journal={INSECT BIOCHEMISTRY AND MOLECULAR BIOLOGY}, author={Deborah, M. Thompson and Khalil, Sayed M. S. and Jeffers, Laura A. and Sonenshine, Daniel E. and Mitchell, Robert D. and Osgood, Christopher J. and Roe, R. Michael}, year={2007}, month={Apr}, pages={363–374} }
 @misc{gudderra_sonenshine_apperson_roe_2002, title={Hemolymph proteins in ticks}, volume={48}, ISSN={["1879-1611"]}, DOI={10.1016/S0022-1910(02)00050-1}, abstractNote={In comparison to insects and Crustacea, our knowledge of the predominant hemolymph proteins in ticks is minimal. The hemolymph protein most studied in ticks has been vitellogenin (Vg). Vg is synthesized by the tick fat body after female adults obtain a blood meal, is released into the hemolymph and is absorbed by developing oocytes as vitellin (Vn). Much of what we know about Vg is from studies of Vn. In general, the carbohydrate, lipid and amino acid composition is similar to insects except that in the tick, Vg contains heme, most likely from the digestion of host hemoglobin. In the American dog tick, Dermacentor variabilis, Vg is comprised of two native proteins and seven subunits on SDS-PAGE. Vg has been characterized in five tick species but the amino acid sequence is not yet available. Another predominant hemolymph protein, apparently a carrier protein (CP), has recently been studied in two tick species. This protein is found in the hemolymph of both male and females adults, in adult tissues outside of the hemolymph in some tick species, in coxal fluid of soft ticks and in whole body homogenates from eggs, larvae and nymphs. CP from the hard tick, D. variabilis, contains cholesterol, phospholipids, monoacylglycerides, triacylglycerides, free fatty acids, carbohydrate and heme. Under identical assay conditions, the analogous protein in the soft tick, Ornithodoros parkeri, did not contain heme. CP in the American dog tick consists of two subunits, one of which has 61% identity to the biliprotein, artemocyanin, from the fairy shrimp. CP is identical to a heme-lipoprotein (HeLp) from Boophilus microplus. The exact roles of CP and HeLp have not yet been fully determined, but they apparently are important in heme sequestration and as a storage depot for protein and lipid. Macroglobulin, lectin, antimicrobial, JH binding, JH esterase, and other tick hemolymph proteins are also discussed.}, number={3}, journal={JOURNAL OF INSECT PHYSIOLOGY}, author={Gudderra, NP and Sonenshine, DE and Apperson, CS and Roe, RM}, year={2002}, month={Mar}, pages={269–278} }
 @article{gudderra_sonenshine_apperson_roe_2002, title={Tissue distribution and characterization of predominant hemolymph carrier proteins from Dermacentor variabilis and Ornithodoros parkeri}, volume={48}, ISSN={["0022-1910"]}, DOI={10.1016/S0022-1910(01)00160-3}, abstractNote={The tissue distribution of the predominant hemolymph protein found throughout tick development was examined in the hard tick, Dermacentor variabilis, and in the soft tick, Ornithodoros parkeri. In D. variabilis, the predominant (purified) hemolymph protein was a lipoglycoheme-carrier protein (DvCP) with a molecular weight of 200K. A protein with a similar mobility on native-PAGE was found in fat body, salivary gland, muscle and ovary from partially fed females which was most abundant in the plasma and salivary gland. DvCP from plasma, salivary gland and fat body of partially fed females consisted of two subunits on SDS-PAGE (98 and 92K). In replete females, only salivary gland exhibited protein subunits equivalent to hemolymph CP. CP in salivary gland and fat body stained positive for lipids. The concentration of CP in tissues varied between partially fed and replete females, indicating a difference in the expression and/or sequestration of CP during adult development. The predominant hemolymph carrier protein from O. parkeri (OpCP) was purified to homogeneity for the first time and is presumed to have similar functions to CP from D. variabilis. Purified OpCP exhibited a molecular weight of 668K by native-PAGE. Unlike CP from D. variabilis, OpCP was not detected in fat body or salivary gland tissues but occurred abundantly in coxal fluid. By SDS-PAGE, purified hemolymph OpCP consisted of two major subunits (114 and 93K) and a less abundant protein with an apparent molecular weight of 48K. Purified native OpCP was a lipoprotein like DvCP. A spectral analysis of purified OpCP failed to demonstrate the presence of heme like that found for CP from D. variabilis, purified by the same methods. However, plasma from O. parkeri contained heme with a lambda(max) of 410nm.}, number={2}, journal={JOURNAL OF INSECT PHYSIOLOGY}, author={Gudderra, NP and Sonenshine, DE and Apperson, CS and Roe, RM}, year={2002}, month={Feb}, pages={161–170} }
 @article{gudderra_neese_sonenshine_apperson_roe_2001, title={Developmental profile, isolation, and biochemical characterization of a novel lipoglycoheme-carrier protein from the American dog tick, Dermacentor variabilis (Acari : Ixodidae) and observations on a similar protein in the soft tick, Ornithodoros parkeri (Acari : Argasidae)}, volume={31}, ISSN={["0965-1748"]}, DOI={10.1016/s0965-1748(00)00122-3}, abstractNote={A novel lipoglycoheme-carrier protein (CP) in the American dog tick, Dermacentor variabilis (Say) has been purified and characterized. CP was purified by native–PAGE from partially fed virgin females. CP has a density of 1.25 g/ml with a molecular weight of 200 K by native–PAGE and 340 K by gel filtration chromatography. CP is comprised of two majour subunits, 98 K and 92 K in molecular weight by SDS–PAGE. Separate amino acid composition of the two subunits indicated high contents of As(x), Gl(x) and leucine. However, the N-terminal amino acid sequence of the two subunits was only 13% identical. The lower molecular weight subunit showed 61% identity to artemocyanin (biliprotein) in fairy shrimps, 46% identity to minor vitellogenin in chickens and 13% identity to vitellin of the black-legged tick. No similarity match was found for the other subunit. CP is a lipoglycoheme-protein as indicated by selective staining of native–PAGE gel for lipids, carbohydrates and heme. Lipid analysis by thin layer chromatography revealed the presence of cholesterol, phospholipids, monoacylglycerides, triacylglycerides and free fatty acids. Heme associated with purified CP demonstrated a λmax of 397.5 nm while the λmax of crude hemolymph plasma was 402.5 nm. The presence of CP in whole body homogenates of eggs, unfed and fed larvae and fed nymphs as well as in the plasma of unfed and fed adults including vitellogenic females was demonstrated by native–PAGE. Although a protein of analogous size was not found in the soft tick, Ornithodoros parkeri Cooley, a high molecular weight protein (500 K) is the predominant plasma protein in both unfed and fed male and female adults of that species as determined by native–PAGE. Also, CP appears to function as a biliprotein which sequesters heme.}, number={4-5}, journal={INSECT BIOCHEMISTRY AND MOLECULAR BIOLOGY}, author={Gudderra, NP and Neese, PA and Sonenshine, DE and Apperson, CS and Roe, RM}, year={2001}, month={Mar}, pages={299–311} }
 @article{neese_sonenshine_kallapur_apperson_roe_2000, title={Absence of insect juvenile hormones in the American dog tick, Dermacentor variabilis (Say) (Acari : Ixodidae), and in Ornithodoros parkeri Cooley (Acari : Argasidae)}, volume={46}, ISSN={["0022-1910"]}, DOI={10.1016/S0022-1910(99)00134-1}, abstractNote={Synganglia, salivary gland, midgut, ovary, fat body and muscle alone and in combination from the ixodid tick, Dermacentor variabilis (Say), or the argasid tick, Ornithodoros parkeri Cooley, were incubated in vitro in separate experiments with L-[methyl-(3)H]methionine and farnesoic acid or with [1-(14)C]acetate. Life stages examined in D. variabilis were 3 and 72 h old (after ecdysis) unfed nymphs, partially fed nymphs (18 and 72 h after attachment to the host), fully engorged nymphs (2 d after detachment from host), 3 and 72 h old (after eclosion) unfed females, partially fed unmated females (12-168 h after attachment to host) and mated replete females (2 d after detachment from the host). Those from O. parkeri were third and fourth stadium nymphs and female O. parkeri, 1-2 d after detachment. Corpora allata from Diploptera punctata, Periplaneta americana and Gromphadorina portentosa were used as positive controls in these experiments. No farnesol, methyl farnesoate, JH I, JH II, JH III, or JHIII bisepoxide was detected by radio HPLC from any tick analysis while JH III, methyl farnesoate, and farnesol were detected in the positive controls. To examine further for the presence of a tick, insect-juvenilizing agent, Galleria pupal-cuticle bioassays were conducted on lipid extracts from 10 and 15 d old eggs, unfed larvae (1-5 d after ecdysis), unfed nymphs (1-7 d after ecdysis), and partially fed, unmated female adults (completed slow feeding phase) of D. variabilis. Whole body extracts of fourth stadium D. punctata and JH III standard were used as positive controls. No juvenilizing activity in any of the tick extracts could be detected. Electron impact, gas chromatography-mass spectrometry of hemolymph extracts from fed, virgin (forcibly detached 7 d after attachment) and mated, replete (allowed to drop naturally) D. variabilis and fully engorged (1-2 d after detachment) O. parkeri females also failed to identify the common insect juvenile hormones. The same procedures were successful in the identification of JH III in hemolymph of fourth stadium D. punctata. Last stadium nymphal (female) O. parkeri implanted with synganglia from second nymphal instars underwent normal eclosion to the adult. The above studies in toto suggest that D. variabilis and O. parkeri do not have the ability to make the common insect juvenile hormones, and these juvenile hormones do not regulate tick metamorphosis or reproduction as hypothesized in the literature.}, number={4}, journal={JOURNAL OF INSECT PHYSIOLOGY}, author={Neese, PA and Sonenshine, DE and Kallapur, VL and Apperson, CS and Roe, RM}, year={2000}, month={Apr}, pages={477–490} }