{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,11,4]],"date-time":"2026-11-04T02:56:06Z","timestamp":1793760966968,"version":"4.6.1"},"reference-count":212,"publisher":"Springer Science and Business Media LLC","issue":"1","license":[{"start":{"date-parts":[[2021,3,4]],"date-time":"2021-03-04T00:00:00Z","timestamp":1614816000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0"},{"start":{"date-parts":[[2021,3,4]],"date-time":"2021-03-04T00:00:00Z","timestamp":1614816000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0"}],"funder":[{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["AI138129"],"award-info":[{"award-number":["AI138129"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["AI119873"],"award-info":[{"award-number":["AI119873"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000097","name":"National Center for Research Resources","doi-asserted-by":"publisher","award":["5P41RR011823"],"award-info":[{"award-number":["5P41RR011823"]}],"id":[{"id":"10.13039\/100000097","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000057","name":"National Institute of General Medical Sciences","doi-asserted-by":"publisher","award":["8P41GM103533"],"award-info":[{"award-number":["8P41GM103533"]}],"id":[{"id":"10.13039\/100000057","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["BMC Genomics"],"abstract":"<jats:title>Abstract<\/jats:title><jats:sec>\n                <jats:title>Background<\/jats:title>\n                <jats:p>Lyme disease (LD) caused by <jats:italic>Borrelia burgdorferi<\/jats:italic> is the most prevalent tick-borne disease. There is evidence that vaccines based on tick proteins that promote tick transmission of <jats:italic>B. burgdorferi<\/jats:italic> could prevent LD<jats:italic>.<\/jats:italic> As <jats:italic>Ixodes scapularis<\/jats:italic> nymph tick bites are responsible for most LD cases, this study sought to identify nymph tick saliva proteins associated with <jats:italic>B. burgdorferi<\/jats:italic> transmission using LC-MS\/MS. Tick saliva was collected using a non-invasive method of stimulating ticks (uninfected and infected: unfed, and every 12 h during feeding through 72 h, and fully-fed) to salivate into 2% pilocarpine-PBS for protein identification using LC-MS\/MS.<\/jats:p>\n              <\/jats:sec><jats:sec>\n                <jats:title>Results<\/jats:title>\n                <jats:p>We identified a combined 747 tick saliva proteins of uninfected and <jats:italic>B. burgdorferi<\/jats:italic> infected ticks that were classified into 25 functional categories: housekeeping-like (48%), unknown function (18%), protease inhibitors (9%), immune-related (6%), proteases (8%), extracellular matrix (7%), and small categories that account for &lt;5% each. Notably, <jats:italic>B. burgdorferi<\/jats:italic> infected ticks secreted high number of saliva proteins (<jats:italic>n<\/jats:italic>=645) than uninfected ticks (<jats:italic>n<\/jats:italic>=376). Counter-intuitively, antimicrobial peptides, which function to block bacterial infection at tick feeding site were suppressed 23-85 folds in <jats:italic>B. burgdorferi<\/jats:italic> infected ticks. Similar to glycolysis enzymes being enhanced in mammalian cells exposed to <jats:italic>B. burgdorferi<\/jats:italic> : eight of the 10-glycolysis pathway enzymes were secreted at high abundance by <jats:italic>B. burgdorferi<\/jats:italic> infected ticks. Of significance, rabbits exposed to <jats:italic>B. burgdorferi<\/jats:italic> infected ticks acquired potent immunity that caused 40-60% mortality of <jats:italic>B. burgdorferi<\/jats:italic> infected ticks during the second infestation compared to 15-28% for the uninfected. This might be explained by ELISA data that show that high expression levels of immunogenic proteins in <jats:italic>B. burgdorferi<\/jats:italic> infected ticks.<\/jats:p>\n              <\/jats:sec><jats:sec>\n                <jats:title>Conclusion<\/jats:title>\n                <jats:p>Data here suggest that <jats:italic>B. burgdorferi<\/jats:italic> infection modified protein content in tick saliva to promote its survival at the tick feeding site. For instance, enzymes; copper\/zinc superoxide dismutase that led to production of H<jats:sub>2<\/jats:sub>O<jats:sub>2<\/jats:sub> that is toxic to <jats:italic>B. burgdorferi<\/jats:italic> were suppressed, while, catalase and thioredoxin that neutralize H<jats:sub>2<\/jats:sub>O<jats:sub>2<\/jats:sub>, and pyruvate kinase which yields pyruvate that protects <jats:italic>Bb<\/jats:italic> from H<jats:sub>2<\/jats:sub>O<jats:sub>2<\/jats:sub> killing were enhanced. We conclude data here is an important resource for discovery of effective antigens for a vaccine to prevent LD.<\/jats:p>\n              <\/jats:sec>","DOI":"10.1186\/s12864-021-07429-0","type":"journal-article","created":{"date-parts":[[2021,3,4]],"date-time":"2021-03-04T07:02:56Z","timestamp":1614841376000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":28,"title":["Borrelia burgdorferi infection modifies protein content in saliva of Ixodes scapularis nymphs"],"prefix":"10.1186","volume":"22","author":[{"given":"Tae Kwon","family":"Kim","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lucas","family":"Tirloni","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Emily","family":"Bencosme-Cuevas","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tae Heung","family":"Kim","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jolene K.","family":"Diedrich","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"suffix":"III","given":"John R.","family":"Yates","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Albert","family":"Mulenga","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2021,3,4]]},"reference":[{"issue":"17","key":"7429_CR1","doi-asserted-by":"publisher","first-page":"496","DOI":"10.15585\/mmwr.mm6717e1","volume":"67","author":"R Rosenberg","year":"2018","unstructured":"Rosenberg R, Lindsey NP, Fischer M, Gregory CJ, Hinckley AF, Mead PS, et al. Vital signs: Trends in reported vectorborne disease cases \u2014 United States and Territories, 2004-2016. MMWR Morb Mortal Wkly Rep. 2018;67(17):496\u2013501.","journal-title":"MMWR Morb Mortal Wkly Rep"},{"issue":"2","key":"7429_CR2","doi-asserted-by":"publisher","first-page":"404","DOI":"10.1111\/j.1948-7134.2011.00181.x","volume":"36","author":"JR Harmon","year":"2011","unstructured":"Harmon JR, Hickling GJ, Scott MC, Jones CJ. Evaluation of 4-poster acaricide applicators to manage tick populations associated with disease risk in a Tennessee retirement community. J Vector Ecol. 2011;36(2):404\u201310.","journal-title":"J Vector Ecol"},{"issue":"3","key":"7429_CR3","doi-asserted-by":"publisher","first-page":"446","DOI":"10.1177\/003335491112600321","volume":"126","author":"JM Garnett","year":"2011","unstructured":"Garnett JM, Connally NP, Stafford KC, Cartter ML. Evaluation of deer-targeted interventions on Lyme disease incidence in Connecticut. Public Health Rep. 2011;126(3):446\u201354.","journal-title":"Public Health Rep"},{"issue":"4","key":"7429_CR4","first-page":"697","volume":"57","author":"ML Wilson","year":"1984","unstructured":"Wilson ML, Levine JF, Spielman A. Effect of deer reduction on abundance of the deer tick (Ixodes dammini). Yale J Biol Med. 1984;57(4):697\u2013705.","journal-title":"Yale J Biol Med"},{"issue":"4","key":"7429_CR5","doi-asserted-by":"publisher","first-page":"357","DOI":"10.1089\/vbz.2009.0022","volume":"9","author":"D Fish","year":"2009","unstructured":"Fish D, Childs JE. Community-based prevention of Lyme disease and other tick-borne diseases through topical application of acaricide to white-tailed deer: Background and rationale. Vector Borne Zoonotic Dis. 2009;9(4):357\u201364.","journal-title":"Vector Borne Zoonotic Dis"},{"issue":"4","key":"7429_CR6","doi-asserted-by":"publisher","first-page":"371","DOI":"10.1089\/vbz.2008.0161","volume":"9","author":"KC Stafford","year":"2009","unstructured":"Stafford KC, Denicola AJ, Pound JM, Miller JA, George JE. Topical treatment of white-tailed deer with an acaricide for the control of Ixodes scapularis (Acari: Ixodidae) in a Connecticut Lyme borreliosis hyperendemic community. Vector Borne Zoonotic Dis. 2009;9(4):371\u20139.","journal-title":"Vector Borne Zoonotic Dis"},{"issue":"4","key":"7429_CR7","doi-asserted-by":"publisher","first-page":"381","DOI":"10.1089\/vbz.2008.0197","volume":"9","author":"TJ Daniels","year":"2009","unstructured":"Daniels TJ, Falco RC, Mchugh EE, Vellozzi J, Boccia T, Denicola AJ, et al. Acaricidal treatment of white-tailed deer to control Ixodes scapularis (Acari: Ixodidae) in a New York Lyme disease-endemic community. Vector Borne Zoonotic Dis. 2009;9(4):381\u20137.","journal-title":"Vector Borne Zoonotic Dis"},{"key":"7429_CR8","doi-asserted-by":"crossref","unstructured":"Schuijt TJ, Hovius JW, van der Poll T, van Dam AP, Fikrig E. Lyme borreliosis vaccination: The facts, the challenge, the future. Trends Parasitol 2011;27(1):40\u201347.","DOI":"10.1016\/j.pt.2010.06.006"},{"key":"7429_CR9","doi-asserted-by":"crossref","unstructured":"Hovius JWR, van Dam AP, Fikrig E. Tick-host-pathogen interactions in Lyme borreliosis. Trends Parasitol 2007;23(9):434\u2013438.","DOI":"10.1016\/j.pt.2007.07.001"},{"issue":"5","key":"7429_CR10","doi-asserted-by":"publisher","first-page":"e451","DOI":"10.1371\/journal.pone.0000451","volume":"2","author":"S Narasimhan","year":"2007","unstructured":"Narasimhan S, DePonte K, Marcantonio N, Liang X, Royce TE, Nelson KF, et al. Immunity against Ixodes scapularis salivary proteins expressed within 24 hours of attachment thwarts tick feeding and impairs Borrelia transmission. PLoS One. 2007;2(5):e451.","journal-title":"PLoS One"},{"issue":"Suppl","key":"7429_CR11","doi-asserted-by":"publisher","first-page":"S367","DOI":"10.1017\/S0031182003004657","volume":"129","author":"P Willadsen","year":"2004","unstructured":"Willadsen P. Anti-tick vaccines. Parasitology. 2004;129(Suppl):S367\u201387.","journal-title":"Parasitology."},{"key":"7429_CR12","doi-asserted-by":"publisher","unstructured":"Nuttall PA. Tick saliva and its role in pathogen transmission. Wien Klin Wochenschr. 2019; https:\/\/doi.org\/10.1007\/s00508-019-1500-y.","DOI":"10.1007\/s00508-019-1500-y"},{"issue":"6","key":"7429_CR13","doi-asserted-by":"publisher","first-page":"780","DOI":"10.4269\/ajtmh.1998.58.780","volume":"58","author":"S Nazario","year":"1998","unstructured":"Nazario S, Das S, de Silva AM, Deponte K, Marcantonio N, Anderson JF, et al. Prevention of Borrelia burgdorferi transmission in guinea pigs by tick immunity. Am J Trop Med Hyg. 1998;58(6):780\u20135.","journal-title":"Am J Trop Med Hyg"},{"issue":"3-4","key":"7429_CR14","doi-asserted-by":"publisher","first-page":"291","DOI":"10.1016\/0304-4017(95)00911-6","volume":"63","author":"LE Craig","year":"1996","unstructured":"Craig LE, Norris DE, Sanders ML, Glass GE, Schwartz BS. Acquired resistance and antibody response of raccoons (Procyon lotor) to sequential feedings of Ixodes scapularis (Acari: Ixodidae). Vet Parasitol. 1996;63(3-4):291\u2013301.","journal-title":"Vet Parasitol"},{"issue":"1","key":"7429_CR15","doi-asserted-by":"publisher","first-page":"e15926","DOI":"10.1371\/journal.pone.0015926","volume":"6","author":"TJ Schuijt","year":"2011","unstructured":"Schuijt TJ, Narasimhan S, Daffre S, DePonte K, Hovius JWR, van\u2019t Veer C, et al. Identification and characterization of Ixodes scapularis antigens that elicit tick immunity using yeast surface display. PLoS One. 2011;6(1):e15926.","journal-title":"PLoS One"},{"key":"7429_CR16","doi-asserted-by":"publisher","first-page":"62","DOI":"10.1016\/j.meegid.2015.12.005","volume":"38","author":"XL Xu","year":"2016","unstructured":"Xu XL, Cheng TY, Yang H, Liao ZH. De novo assembly and analysis of midgut transcriptome of Haemaphysalis flava and identification of genes involved in blood digestion, feeding and defending from pathogens. Infect Genet Evol. 2016;38:62\u201372.","journal-title":"Infect Genet Evol"},{"key":"7429_CR17","doi-asserted-by":"publisher","first-page":"476","DOI":"10.3389\/fcimb.2017.00476","volume":"7","author":"E Esteves","year":"2017","unstructured":"Esteves E, Maruyama SR, Kawahara R, Fujita A, Martins LA, Righi AA, et al. Analysis of the salivary gland transcriptome of unfed and partially fed Amblyomma sculptum ticks and descriptive proteome of the saliva. Front Cell Infect Microbiol. 2017;7:476.","journal-title":"Front Cell Infect Microbiol"},{"key":"7429_CR18","doi-asserted-by":"publisher","first-page":"135","DOI":"10.1016\/j.meegid.2015.03.010","volume":"32","author":"XL Xu","year":"2015","unstructured":"Xu XL, Cheng TY, Yang H, Yan F, Yang Y. De novo sequencing, assembly and analysis of salivary gland transcriptome of Haemaphysalis flava and identification of sialoprotein genes. Infect Genet Evol. 2015;32:135\u201342.","journal-title":"Infect Genet Evol"},{"issue":"3","key":"7429_CR19","doi-asserted-by":"publisher","first-page":"424","DOI":"10.1016\/j.ttbdis.2015.03.012","volume":"6","author":"LA Lewis","year":"2015","unstructured":"Lewis LA, Radulovi\u0107 TM, Kim TK, Porter LM, Mulenga A. Identification of 24h Ixodes scapularis immunogenic tick saliva proteins. Ticks Tick Borne Dis. 2015;6(3):424\u201334.","journal-title":"Ticks Tick Borne Dis"},{"key":"7429_CR20","first-page":"51","volume":"32","author":"\u017dM Radulovi\u0107","year":"2014","unstructured":"Radulovi\u0107 \u017dM, Kim TK, Porter LM, Sze SH, Lewis L, Mulenga A. A 24-48 h fed Amblyomma americanum tick saliva immuno-proteome. BMC Genomics. 2014;32:51.","journal-title":"BMC Genomics"},{"issue":"13","key":"7429_CR21","doi-asserted-by":"publisher","first-page":"1029","DOI":"10.1016\/j.ijpara.2014.07.003","volume":"44","author":"L Mudenda","year":"2014","unstructured":"Mudenda L, Pierl\u00e9 SA, Turse JE, Scoles GA, Purvine SO, Nicora CD, et al. Proteomics informed by transcriptomics identifies novel secreted proteins in Dermacentor andersoni saliva. Int J Parasitol. 2014;44(13):1029\u201337.","journal-title":"Int J Parasitol"},{"key":"7429_CR22","doi-asserted-by":"publisher","first-page":"517","DOI":"10.3389\/fcimb.2017.00517","volume":"7","author":"L Tirloni","year":"2017","unstructured":"Tirloni L, Kim TK, Pinto AFM, Yates JR, da Silva VI, Mulenga A. Tick-host range adaptation: Changes in protein profiles in unfed adult Ixodes scapularis and Amblyomma americanum saliva stimulated to feed on different hosts. Front Cell Infect Microbiol. 2017;7:517.","journal-title":"Front Cell Infect Microbiol"},{"issue":"4","key":"7429_CR23","doi-asserted-by":"publisher","first-page":"e94831","DOI":"10.1371\/journal.pone.0094831","volume":"9","author":"L Tirloni","year":"2014","unstructured":"Tirloni L, Reck J, Terra RMS, Martins JR, Mulenga A, Sherman NE, et al. Proteomic analysis of cattle tick Rhipicephalus (Boophilus) microplus saliva: A comparison between partially and fully engorged females. PLoS One. 2014;9(4):e94831.","journal-title":"PLoS One"},{"issue":"1","key":"7429_CR24","doi-asserted-by":"publisher","first-page":"e0004323","DOI":"10.1371\/journal.pntd.0004323","volume":"10","author":"TK Kim","year":"2016","unstructured":"Kim TK, Tirloni L, Pinto AFM, Moresco J, Yates JRIII, da Silva Vaz I Jr, Mulenga A. Ixodes scapularis tick saliva proteins sequentially secreted every 24 h during blood Feeding. PLoS Negl Trop Dis. 2016;10(1):e0004323.","journal-title":"PLoS Negl Trop Dis"},{"key":"7429_CR25","doi-asserted-by":"publisher","first-page":"338","DOI":"10.1186\/s13071-015-0918-y","volume":"8","author":"L Tirloni","year":"2015","unstructured":"Tirloni L, Islam MS, Kim TK, Diedrich JK, Yates JR, Pinto AFM, et al. Saliva from nymph and adult females of Haemaphysalis longicornis: A proteomic study. Parasit Vectors. 2015;8:338.","journal-title":"Parasit Vectors"},{"issue":"2","key":"7429_CR26","doi-asserted-by":"publisher","first-page":"e0007758","DOI":"10.1371\/journal.pntd.0007758","volume":"14","author":"TK Kim","year":"2020","unstructured":"Kim TK, Tirloni L, Pinto AFM, Diedrich JK, Moresco JJ, Yates JR 3rd, da Silva Vaz I Jr, Mulenga A. Time-resolved proteomic profile of Amblyomma americanum tick saliva during feeding. PLoS Negl Trop Dis. 2020;14(2):e0007758.","journal-title":"PLoS Negl Trop Dis"},{"issue":"1","key":"7429_CR27","doi-asserted-by":"publisher","first-page":"81","DOI":"10.1186\/s13071-017-2011-1","volume":"10","author":"KL Mansfield","year":"2017","unstructured":"Mansfield KL, Cook C, Ellis RJ, Bell-Sakyi L, Johnson N, Alberdi P, et al. Tick-borne pathogens induce differential expression of genes promoting cell survival and host resistance in Ixodes ricinus cells. Parasit Vectors. 2017;10(1):81.","journal-title":"Parasit Vectors"},{"key":"7429_CR28","doi-asserted-by":"publisher","first-page":"129","DOI":"10.3389\/fcimb.2017.00129","volume":"7","author":"LA Martins","year":"2017","unstructured":"Martins LA, de Melo Galletti MFB, Ribeiro JM, Fujita A, Costa FB, Labruna MB, et al. The distinct transcriptional response of the midgut of Amblyomma sculptum and Amblyomma aureolatum ticks to Rickettsia rickettsii correlates to their differences in susceptibility to infection. Front Cell Infect Microbiol. 2017;7:129.","journal-title":"Front Cell Infect Microbiol"},{"issue":"9","key":"7429_CR29","doi-asserted-by":"publisher","first-page":"e0137237","DOI":"10.1371\/journal.pone.0137237","volume":"10","author":"M Villar","year":"2015","unstructured":"Villar M, Ayll\u00f3n N, Kocan KM, Bonz\u00f3n-Kulichenko E, Alberdi P, Blouin EF, et al. Identification and characterization of Anaplasma phagocytophilum proteins involved in infection of the tick vector, Ixodes scapularis. PLoS One. 2015;10(9):e0137237.","journal-title":"PLoS One"},{"issue":"12","key":"7429_CR30","doi-asserted-by":"publisher","first-page":"3154","DOI":"10.1074\/mcp.M115.051938","volume":"14","author":"M Villar","year":"2015","unstructured":"Villar M, Ayll\u00f3n N, Alberdi P, Moreno A, Moreno M, Tobes R, et al. Integrated metabolomics, transcriptomics and proteomics identifies metabolic pathways affected by Anaplasma phagocytophilum infection in tick cells. Mol Cell Proteomics. 2015;14(12):3154\u201372.","journal-title":"Mol Cell Proteomics"},{"key":"7429_CR31","doi-asserted-by":"publisher","first-page":"116","DOI":"10.3389\/fcimb.2018.00116","volume":"8","author":"S Antunes","year":"2018","unstructured":"Antunes S, Couto J, Ferrolho J, Rodrigues F, Nobre J, Santos AS, et al. Rhipicephalus bursa sialotranscriptomic response to blood feeding and Babesia ovis infection: Identification of candidate protective antigens. Front Cell Infect Microbiol. 2018;8:116.","journal-title":"Front Cell Infect Microbiol"},{"issue":"5","key":"7429_CR32","doi-asserted-by":"publisher","first-page":"773","DOI":"10.1086\/318818","volume":"183","author":"F Des Vignes","year":"2001","unstructured":"Des Vignes F, Piesman J, Heffernan R, Schulze TL, Stafford KCIII, Fish D. Effect of Tick Removal on Transmission of Borrelia burgdorferi and Ehrlichia phagocytophila by Ixodes scapularis Nymphs. J Infect Dis. 2001;183(5):773\u20138.","journal-title":"J Infect Dis"},{"key":"7429_CR33","doi-asserted-by":"publisher","first-page":"1","DOI":"10.2147\/IJGM.S73791","volume":"8","author":"MJ Cook","year":"2014","unstructured":"Cook MJ. Lyme borreliosis: A review of data on transmission time after tick attachment. Int J Gen Med. 2014;8:1\u20138.","journal-title":"Int J Gen Med"},{"issue":"3","key":"7429_CR34","doi-asserted-by":"publisher","first-page":"538","DOI":"10.1016\/j.ttbdis.2018.01.002","volume":"9","author":"L Eisen","year":"2018","unstructured":"Eisen L. Pathogen transmission in relation to duration of attachment by Ixodes scapularis ticks. Ticks Tick Borne Dis. 2018;9(3):538\u201342.","journal-title":"Ticks Tick Borne Dis"},{"key":"7429_CR35","doi-asserted-by":"publisher","first-page":"285","DOI":"10.1603\/0022-2585-39.2.285","volume":"39","author":"AH Broadwater","year":"2002","unstructured":"Broadwater AH, Sonenshine DE, Hynes WL, Ceraul S, De SA. Glass capillary tube feeding: a method for infecting nymphal Ixodes scapularis (Acari: Ixodidae) with the lyme disease spirochete Borrelia burgdorferi. J Med Entomol. 2002;39:285\u201392.","journal-title":"J Med Entomol"},{"issue":"1","key":"7429_CR36","doi-asserted-by":"publisher","first-page":"20","DOI":"10.1111\/j.0269-283X.2003.0469.x","volume":"18","author":"JMC Ribeiro","year":"2004","unstructured":"Ribeiro JMC, Zeidner NS, Ledin K, Dolan MC, Mather TN. How much pilocarpine contaminates pilocarpine-induced tick saliva? Med Vet Entomol. 2004;18(1):20\u20134.","journal-title":"Med Vet Entomol"},{"issue":"4","key":"7429_CR37","doi-asserted-by":"publisher","first-page":"531","DOI":"10.1111\/j.1365-2583.2009.00897.x","volume":"18","author":"Y Saito","year":"2009","unstructured":"Saito Y, Konnai S, Yamada S, et al. Identification and characterization of antimicrobial peptide, defensin, in the taiga tick, Ixodes persulcatus. Insect Mol Biol. 2009;18(4):531\u20139.","journal-title":"Insect Mol Biol"},{"key":"7429_CR38","doi-asserted-by":"publisher","first-page":"6","DOI":"10.1155\/2010\/840518","volume":"2010","author":"W Zhu","year":"2010","unstructured":"Zhu W, Smith JW, Huang C-M. Mass Spectrometry-Based Label-Free Quantitative Proteomics. Biomed Res Int. 2010;2010:6 Article ID 840518. https:\/\/doi.org\/10.1155\/2010\/840518.","journal-title":"Biomed Res Int"},{"issue":"1","key":"7429_CR39","doi-asserted-by":"publisher","first-page":"49","DOI":"10.1146\/annurev-anchem-061516-045357","volume":"11","author":"JA Ankney","year":"2018","unstructured":"Ankney JA, Muneer A, Chen X. Relative and Absolute Quantitation in Mass Spectrometry\u2013Based Proteomics. Ann Rev Analy Chem. 2018;11(1):49\u201377.","journal-title":"Ann Rev Analy Chem"},{"issue":"50","key":"7429_CR40","doi-asserted-by":"publisher","first-page":"18928","DOI":"10.1073\/pnas.0606379103","volume":"103","author":"AC Paoletti","year":"2006","unstructured":"Paoletti AC, Parmely TJ, Tomomori-Sato C, Sato S, Zhu D, Conaway RC, et al. Quantitative proteomic analysis of distinct mammalian Mediator complexes using normalized spectral abundance factors. Proc Natl Acad Sci U S A. 2006;103(50):18928\u201333.","journal-title":"Proc Natl Acad Sci U S A"},{"key":"7429_CR41","volume-title":"Gplots: Various R programming tools for plotting data","author":"GR Warnes","year":"2016","unstructured":"Warnes GR, Bolker B, Bonebakker L, Gentleman R, Huber W, Liaw A, et al. Gplots: Various R programming tools for plotting data. 2016."},{"key":"7429_CR42","doi-asserted-by":"publisher","first-page":"5","DOI":"10.1016\/j.biochi.2015.10.003","volume":"122","author":"ND Rawlings","year":"2016","unstructured":"Rawlings ND. Peptidase specificity from the substrate cleavage collection in the MEROPS database and a tool to measure cleavage site conservation. Biochimie. 2016;122:5\u201330.","journal-title":"Biochimie."},{"issue":"1","key":"7429_CR43","doi-asserted-by":"publisher","first-page":"152","DOI":"10.1186\/s13071-017-2080-1","volume":"10","author":"LM Porter","year":"2017","unstructured":"Porter LM, Radulovi\u0107 \u017dM, Mulenga A. A repertoire of protease inhibitor families in Amblyomma americanum and other tick species: inter-species comparative analyses. Parasit Vectors. 2017;10(1):152.","journal-title":"Parasit Vectors"},{"issue":"1","key":"7429_CR44","doi-asserted-by":"publisher","first-page":"16","DOI":"10.1016\/j.ttbdis.2014.08.002","volume":"6","author":"L Porter","year":"2015","unstructured":"Porter L, Radulovi\u0107 Z, Kim T, Braz GRC, da Silva VI, Mulenga A. Bioinformatic analyses of male and female Amblyomma americanum tick expressed serine protease inhibitors (serpins). Ticks Tick Borne Dis. 2015;6(1):16\u201330.","journal-title":"Ticks Tick Borne Dis"},{"issue":"Suppl 1","key":"7429_CR45","doi-asserted-by":"publisher","first-page":"102","DOI":"10.1111\/j.1538-7836.2007.02516.x","volume":"5","author":"JC Rau","year":"2007","unstructured":"Rau JC, Beaulieu LM, Huntington JA, Church FC. Serpins in thrombosis, hemostasis and fibrinolysis. J Thromb Haemost. 2007;5(Suppl 1):102\u201315.","journal-title":"J Thromb Haemost"},{"issue":"38","key":"7429_CR46","doi-asserted-by":"publisher","first-page":"33293","DOI":"10.1074\/jbc.R100016200","volume":"276","author":"GA Silverman","year":"2001","unstructured":"Silverman GA, Bird PI, Carrell RW, Church FC, Coughlin PB, Gettins PGW, et al. The serpins are an expanding superfamily of structurally similar but functionally diverse proteins. Evolution, mechanism of inhibition, novel functions, and a revised nomenclature. J Biol Chem. 2001;276(38):33293\u20136.","journal-title":"J Biol Chem"},{"key":"7429_CR47","doi-asserted-by":"publisher","first-page":"185","DOI":"10.1016\/B978-0-12-385504-6.00005-1","volume":"99","author":"ST Olson","year":"2011","unstructured":"Olson ST, Gettins PGW. Regulation of proteases by protein inhibitors of the serpin superfamily. Prog Mol Biol Transl Sci. 2011;99:185\u2013240.","journal-title":"Prog Mol Biol Transl Sci"},{"key":"7429_CR48","doi-asserted-by":"publisher","first-page":"13","DOI":"10.1111\/j.1749-6632.1994.tb12026.x","volume":"714","author":"PA Patston","year":"1994","unstructured":"Patston PA, Gettins PG, Schapira M. The Mechanism by Which Serpins Inhibit Thrombin and Other Serine Proteinases. Ann N Y Acad Sci. 1994;714:13\u201320.","journal-title":"Ann N Y Acad Sci"},{"issue":"10","key":"7429_CR49","doi-asserted-by":"publisher","first-page":"1063","DOI":"10.1292\/jvms.63.1063","volume":"63","author":"A Mulenga","year":"2001","unstructured":"Mulenga A, Sugino M, Nakajima M, Sugimoto C, Onuma M. Tick-Encoded Serine Proteinase Inhibitors (Serpins); Potential Target Antigens for Tick Vaccine Development. J Vet Med Sci. 2001;63(10):1063\u20139.","journal-title":"J Vet Med Sci"},{"key":"7429_CR50","doi-asserted-by":"publisher","first-page":"217","DOI":"10.1186\/1471-2164-10-217","volume":"10","author":"A Mulenga","year":"2009","unstructured":"Mulenga A, Khumthong R, Chalaire KC. Ixodes scapularis tick serine proteinase inhibitor (serpin) gene family; annotation and transcriptional analysis. BMC Genomics. 2009;10:217.","journal-title":"BMC Genomics"},{"issue":"Pt 18","key":"7429_CR51","doi-asserted-by":"publisher","first-page":"3188","DOI":"10.1242\/jeb.006494","volume":"20","author":"A Mulenga","year":"2007","unstructured":"Mulenga A, Khumthong R, Blandon MA. Molecular and expression analysis of a family of the Amblyomma americanum tick Lospins. J Exp Biol. 2007;20(Pt 18):3188\u201398.","journal-title":"J Exp Biol"},{"issue":"6","key":"7429_CR52","doi-asserted-by":"publisher","first-page":"369","DOI":"10.1016\/j.ijpara.2014.01.010","volume":"44","author":"AMG Ibelli","year":"2014","unstructured":"Ibelli AMG, Kim TK, Hill CC, Lewis LA, Bakshi M, Miller S, et al. A blood meal induced Ixodes scapularis tick saliva serpin inhibits trypsin and thrombin, and interferes with platelet aggregation and blood clotting. Int J Parasitol. 2014;44(6):369\u201379.","journal-title":"Int J Parasitol"},{"issue":"9-10","key":"7429_CR53","doi-asserted-by":"publisher","first-page":"613","DOI":"10.1016\/j.ijpara.2015.03.009","volume":"45","author":"TK Kim","year":"2015","unstructured":"Kim TK, Tirloni L, Radulovic Z, Lewis L, Bakshi M, Hill C, et al. Conserved Amblyomma americanum tick Serpin19, an inhibitor of blood clotting factors Xa and XIa, trypsin and plasmin, has anti-haemostatic functions. Int J Parasitol. 2015;45(9-10):613\u201327.","journal-title":"Int J Parasitol"},{"issue":"3","key":"7429_CR54","doi-asserted-by":"publisher","first-page":"506","DOI":"10.1016\/j.ttbdis.2018.01.001","volume":"9","author":"M Bakshi","year":"2018","unstructured":"Bakshi M, Kim TK, Mulenga A. Disruption of blood meal-responsive serpins prevents Ixodes scapularis from feeding to repletion. Ticks Tick Borne Dis. 2018;9(3):506\u201318.","journal-title":"Ticks Tick Borne Dis"},{"issue":"3","key":"7429_CR55","doi-asserted-by":"publisher","first-page":"405","DOI":"10.1016\/j.ttbdis.2015.12.017","volume":"7","author":"TK Kim","year":"2016","unstructured":"Kim TK, Radulovic Z, Mulenga A. Target validation of highly conserved Amblyomma americanum tick saliva serine protease inhibitor 19. Ticks Tick Borne Dis. 2016;7(3):405\u201314.","journal-title":"Ticks Tick Borne Dis"},{"key":"7429_CR56","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1016\/j.ibmb.2016.11.002","volume":"80","author":"\u017dM Radulovi\u0107","year":"2017","unstructured":"Radulovi\u0107 \u017dM, Mulenga A. Heparan sulfate\/heparin glycosaminoglycan binding alters inhibitory profile and enhances anticoagulant function of conserved Amblyomma americanum tick saliva serpin 19. Insect Biochem Mol Biol. 2017;80:1\u201310.","journal-title":"Insect Biochem Mol Biol"},{"issue":"2","key":"7429_CR57","doi-asserted-by":"publisher","first-page":"738","DOI":"10.1182\/blood-2010-06-293241","volume":"117","author":"J Chmelar","year":"2011","unstructured":"Chmelar J, Oliveira CJ, Rezacova P, Francischetti IMB, Kovarova Z, Pejler G, et al. A tick salivary protein targets cathepsin G and chymase and inhibits host inflammation and platelet aggregation. Blood. 2011;117(2):738\u201344.","journal-title":"Blood."},{"issue":"8","key":"7429_CR58","doi-asserted-by":"publisher","first-page":"1665","DOI":"10.1002\/jcp.24266","volume":"228","author":"AA Rehman","year":"2013","unstructured":"Rehman AA, Ahsan H, Khan FH. Alpha-2-macroglobulin: A physiological guardian. J Cell Physiol. 2013;228(8):1665\u201375.","journal-title":"J Cell Physiol"},{"issue":"9","key":"7429_CR59","doi-asserted-by":"publisher","first-page":"911","DOI":"10.1016\/S0965-1748(03)00097-3","volume":"33","author":"A Mulenga","year":"2003","unstructured":"Mulenga A, Macaluso KR, Simser JA, Azad AF. The American dog tick, Dermacentor variabilis, encodes a functional histamine release factor homolog. Insect Biochem Mol Biol. 2003;33(9):911\u20139.","journal-title":"Insect Biochem Mol Biol"},{"issue":"4","key":"7429_CR60","doi-asserted-by":"publisher","first-page":"489","DOI":"10.1016\/j.dci.2008.09.011","volume":"33","author":"V Buresova","year":"2009","unstructured":"Buresova V, Hajdusek O, Franta Z, Sojka D, Kopacek P. IrAM-An \u03b12-macroglobulin from the hard tick Ixodes ricinus: Characterization and function in phagocytosis of a potential pathogen Chryseobacterium indologenes. Dev Comp Immunol. 2009;33(4):489\u201398.","journal-title":"Dev Comp Immunol"},{"key":"7429_CR61","doi-asserted-by":"publisher","first-page":"216","DOI":"10.3389\/fcimb.2017.00216","volume":"7","author":"J Chmela\u0159","year":"2017","unstructured":"Chmela\u0159 J, Kot\u00e1l J, Langhansov\u00e1 H, Kotsyfakis M. Protease inhibitors in tick saliva: The role of serpins and cystatins in tick-host-pathogen interaction. Front Cell Infect Microbiol. 2017;7:216.","journal-title":"Front Cell Infect Microbiol"},{"issue":"1","key":"7429_CR62","doi-asserted-by":"publisher","first-page":"225","DOI":"10.1186\/s13071-017-2161-1","volume":"10","author":"X Yu","year":"2017","unstructured":"Yu X, Zhou Y, Cao J, Zhang H, Gong H, Zhou J. Caspase-1 participates in apoptosis of salivary glands in Rhipicephalus haemaphysaloides. Parasit Vectors. 2017;10(1):225.","journal-title":"Parasit Vectors"},{"key":"7429_CR63","doi-asserted-by":"publisher","first-page":"32","DOI":"10.1016\/j.toxicon.2013.10.025","volume":"77","author":"S Pichu","year":"2014","unstructured":"Pichu S, Ribeiro JMC, Mather TN, Francischetti IMB. Purification of a serine protease and evidence for a protein C activator from the saliva of the tick, Ixodes scapularis. Toxicon. 2014;77:32\u20139.","journal-title":"Toxicon"},{"issue":"10","key":"7429_CR64","doi-asserted-by":"publisher","first-page":"1053","DOI":"10.1016\/j.chembiol.2009.09.009","volume":"16","author":"M Horn","year":"2009","unstructured":"Horn M, Nussbaumerov\u00e1 M, \u0160anda M, Kov\u00e1\u0159ov\u00e1 Z, Srba J, Franta Z, et al. Hemoglobin Digestion in Blood-Feeding Ticks: Mapping a Multipeptidase Pathway by Functional Proteomics. Chem Biol. 2009;16(10):1053\u201363.","journal-title":"Chem Biol"},{"issue":"1\u20132","key":"7429_CR65","doi-asserted-by":"publisher","first-page":"151","DOI":"10.1023\/A:1024278402288","volume":"29","author":"A Mulenga","year":"2003","unstructured":"Mulenga A, Misao O, Sugimoto C. Three serine proteinases from midguts of the hard tick Rhipicephalus appendiculatus; cDNA cloning and preliminary characterization. Exp Appl Acarol. 2003;29(1\u20132):151\u201364.","journal-title":"Exp Appl Acarol"},{"issue":"4","key":"7429_CR66","first-page":"179","volume":"46","author":"A Mulenga","year":"1999","unstructured":"Mulenga A, Sugimoto C, Onuma M. Characterization of proteolytic enzymes expressed in the midgut of Haemaphysalis longicornis. Jpn J Vet Res. 1999;46(4):179\u201384.","journal-title":"Jpn J Vet Res"},{"issue":"5","key":"7429_CR67","doi-asserted-by":"publisher","first-page":"e1000062","DOI":"10.1371\/journal.ppat.1000062","volume":"4","author":"N Tsuji","year":"2008","unstructured":"Tsuji N, Miyoshi T, Battsetseg B, Matsuo T, Xuan X. Fujisaki K. A cysteine protease is critical for Babesia spp. transmission in Haemaphysalis ticks. PLoS Pathog. 2008;4(5):e1000062.","journal-title":"PLoS Pathog"},{"issue":"1-2","key":"7429_CR68","doi-asserted-by":"publisher","first-page":"78","DOI":"10.1016\/j.gene.2011.04.008","volume":"482","author":"A Mulenga","year":"2011","unstructured":"Mulenga A, Erikson K. A snapshot of the Ixodes scapularis degradome. Gene. 2011;482(1-2):78\u201393.","journal-title":"Gene."},{"key":"7429_CR69","doi-asserted-by":"publisher","first-page":"3","DOI":"10.1016\/j.toxicon.2012.09.004","volume":"62","author":"FS Markland","year":"2013","unstructured":"Markland FS, Swenson S. Snake venom metalloproteinases. Toxicon. 2013;62:3\u201318.","journal-title":"Toxicon."},{"issue":"4","key":"7429_CR70","doi-asserted-by":"publisher","first-page":"869","DOI":"10.1016\/S0006-291X(03)00857-X","volume":"305","author":"IMB Francischetti","year":"2003","unstructured":"Francischetti IMB, Mather TN, Ribeiro JMC. Cloning of a salivary gland metalloprotease and characterization of gelatinase and fibrin(ogen)lytic activities in the saliva of the Lyme disease tick vector Ixodes scapularis. Biochem Biophys Res Commun. 2003;305(4):869\u201375.","journal-title":"Biochem Biophys Res Commun"},{"key":"7429_CR71","doi-asserted-by":"crossref","unstructured":"Decrem Y, Mariller M, Lahaye K, Blasioli V, Beaufays J, Zouaoui Boudjeltia K, et al. The impact of gene knock-down and vaccination against salivary metalloproteases on blood feeding and egg laying by Ixodes ricinus. Int J Parasitol. 2008;38(5):549\u201360.","DOI":"10.1016\/j.ijpara.2007.09.003"},{"key":"7429_CR72","first-page":"95","volume-title":"Proteases in blood clotting. Essays in Biochem","author":"PN Walsh","year":"2002","unstructured":"Walsh PN, Ahmad SS. Proteases in blood clotting. Essays in Biochem. London: Portland Press Ltd; 2002. p. 95\u2013111."},{"issue":"6","key":"7429_CR73","doi-asserted-by":"publisher","first-page":"579","DOI":"10.1016\/j.aller.2016.10.011","volume":"45","author":"S Patel","year":"2017","unstructured":"Patel S. A critical review on serine protease: Key immune manipulator and pathology mediator. Allergol Immunopathol. 2017;45(6):579\u201391.","journal-title":"Allergol Immunopathol"},{"issue":"11 Pt B","key":"7429_CR74","doi-asserted-by":"publisher","first-page":"2118","DOI":"10.1016\/j.bbamcr.2017.07.009","volume":"1864","author":"H Weidmann","year":"2017","unstructured":"Weidmann H, Heikaus L, Long AT, Naudin C, Schl\u00fcter H, Renn\u00e9 T. The plasma contact system, a protease cascade at the nexus of inflammation, coagulation and immunity. Biochim Biophys Acta, Mol Cell Res. 2017;1864(11 Pt B):2118\u201327.","journal-title":"Biochim Biophys Acta, Mol Cell Res"},{"issue":"Suppl 1","key":"7429_CR75","doi-asserted-by":"publisher","first-page":"242","DOI":"10.1111\/jth.12247","volume":"11","author":"EAM Bouwens","year":"2013","unstructured":"Bouwens EAM, Stavenuiter F, Mosnier LO. Mechanisms of anticoagulant and cytoprotective actions of the protein C pathway. J Thromb Haemost. 2013;11(Suppl 1):242\u201353.","journal-title":"J Thromb Haemost"},{"key":"7429_CR76","doi-asserted-by":"publisher","first-page":"611","DOI":"10.1146\/annurev.ento.42.1.611","volume":"42","author":"JP Gillespie","year":"1997","unstructured":"Gillespie JP, Kanost MR, Trenczek T. Biological mediators of insect immunity. Annu Rev Entomol. 1997;42:611\u201343.","journal-title":"Annu Rev Entomol"},{"issue":"6","key":"7429_CR77","doi-asserted-by":"publisher","first-page":"263","DOI":"10.1016\/j.it.2008.02.009","volume":"29","author":"L Cerenius","year":"2008","unstructured":"Cerenius L, Lee BL, S\u00f6derh\u00e4ll K. The proPO-system: pros and cons for its role in invertebrate immunity. Trends Immunol. 2008;29(6):263\u201371.","journal-title":"Trends Immunol"},{"key":"7429_CR78","doi-asserted-by":"publisher","first-page":"387","DOI":"10.1186\/1471-2164-10-387","volume":"10","author":"QW Chan","year":"2009","unstructured":"Chan QW, Melathopoulos AP, Pernal SF, Foster LJ. The innate immune and systemic response in honey bees to a bacterial pathogen, Paenibacillus larvae. BMC Genomics. 2009;10:387.","journal-title":"BMC Genomics"},{"issue":"5","key":"7429_CR79","doi-asserted-by":"publisher","first-page":"e10393","DOI":"10.1371\/journal.pone.0010393","volume":"5","author":"YM Choo","year":"2010","unstructured":"Choo YM, Lee KS, Yoon HJ, et al. Dual function of a bee venom serine protease: prophenoloxidase-activating factor in arthropods and fibrin(ogen)olytic enzyme in mammals. PLoS One. 2010;5(5):e10393.","journal-title":"PLoS One"},{"issue":"10","key":"7429_CR80","doi-asserted-by":"publisher","first-page":"1908","DOI":"10.1111\/jth.13441","volume":"14","author":"JJN Posma","year":"2016","unstructured":"Posma JJN, Posthuma JJ, Spronk HMH. Coagulation and non-coagulation effects of thrombin. J Thromb Haemost. 2016;14(10):1908\u201316.","journal-title":"J Thromb Haemost"},{"issue":"2","key":"7429_CR81","doi-asserted-by":"publisher","first-page":"886","DOI":"10.1007\/s10753-014-9999-6","volume":"38","author":"Q Fu","year":"2015","unstructured":"Fu Q, Cheng J, Gao Y, Zhang Y, Chen X, Xie J. Protease-Activated Receptor 4: A Critical Participator in Inflammatory Response. Inflammation. 2015;38(2):886\u201395.","journal-title":"Inflammation."},{"issue":"5","key":"7429_CR82","first-page":"876","volume":"112","author":"AR Rezaie","year":"2014","unstructured":"Rezaie AR. Protease-activated receptor signalling by coagulation proteases in endothelial cells. Thromb Haemost. 2014;112(5):876\u201382.","journal-title":"Thromb Haemost"},{"issue":"5","key":"7429_CR83","doi-asserted-by":"publisher","first-page":"349","DOI":"10.1111\/j.1399-0039.2006.00585.x","volume":"67","author":"T Zava\u0161nik-Bergant","year":"2006","unstructured":"Zava\u0161nik-Bergant T, Turk B. Cysteine cathepsins in the immune response. Tissue Antigens. 2006;67(5):349\u201355.","journal-title":"Tissue Antigens"},{"issue":"11","key":"7429_CR84","doi-asserted-by":"publisher","first-page":"2955","DOI":"10.1002\/eji.200939650","volume":"39","author":"JD Colbert","year":"2009","unstructured":"Colbert JD, Matthews SP, Miller G, Watts C. Diverse regulatory roles for lysosomal proteases in the immune response. Eur J Immunol. 2009;39(11):2955\u201365.","journal-title":"Eur J Immunol"},{"issue":"8","key":"7429_CR85","doi-asserted-by":"publisher","first-page":"e0006512","DOI":"10.1371\/journal.pntd.0006512","volume":"12","author":"JL Siqueira-Neto","year":"2018","unstructured":"Siqueira-Neto JL, Debnath A, McCall LI, Bernatchez JA, Ndao M, Reed SL, et al. Cysteine proteases in protozoan parasites. PLoS Negl Trop Dis. 2018;12(8):e0006512.","journal-title":"PLoS Negl Trop Dis"},{"issue":"8","key":"7429_CR86","doi-asserted-by":"publisher","first-page":"e0005919","DOI":"10.1371\/journal.pntd.0005919","volume":"12","author":"A Grote","year":"2018","unstructured":"Grote A, Caffrey CR, Rebello KM, Smith D, Dalton JP, Lustigman S. Cysteine proteases during larval migration and development of helminths in their final host. PLoS Negl Trop Dis. 2018;12(8):e0005919.","journal-title":"PLoS Negl Trop Dis"},{"key":"7429_CR87","doi-asserted-by":"publisher","first-page":"49","DOI":"10.1016\/j.pharmthera.2017.06.004","volume":"180","author":"LG Ferreira","year":"2017","unstructured":"Ferreira LG, Andricopulo AD. Targeting cysteine proteases in trypanosomatid disease drug discovery. Pharm Ther. 2017;180:49\u201361.","journal-title":"Pharm Ther"},{"issue":"4","key":"7429_CR88","doi-asserted-by":"publisher","first-page":"392","DOI":"10.1016\/j.cbpb.2008.08.008","volume":"151","author":"PC Pohl","year":"2008","unstructured":"Pohl PC, Sorgine MH, Leal AT, et al. An extraovarian aspartic protease accumulated in tick oocytes with vitellin-degradation activity. Comp Biochem Physiol B Biochem Mol Biol. 2008;151(4):392\u20139.","journal-title":"Comp Biochem Physiol B Biochem Mol Biol"},{"issue":"11","key":"7429_CR89","doi-asserted-by":"publisher","first-page":"e2525","DOI":"10.1371\/journal.pntd.0002525","volume":"7","author":"W Mahmood","year":"2013","unstructured":"Mahmood W, Viberg LT, Fischer K, Walton SF, Holt DC. An Aspartic Protease of the Scabies Mite Sarcoptes scabiei Is Involved in the Digestion of Host Skin and Blood Macromolecules. PLoS Negl Trop Dis. 2013;7(11):e2525.","journal-title":"PLoS Negl Trop Dis"},{"issue":"4","key":"7429_CR90","doi-asserted-by":"publisher","first-page":"353","DOI":"10.1042\/CBI20090115","volume":"34","author":"AK Pathak","year":"2010","unstructured":"Pathak AK, Helm BA. Proteomic identification and characterization of secreted N-glycosylated NPC2 following cross-linking of the high-affinity receptor for IgE on mast cells. Cell Biol Int. 2010;34(4):353\u20139.","journal-title":"Cell Biol Int"},{"issue":"10","key":"7429_CR91","doi-asserted-by":"publisher","first-page":"2772","DOI":"10.1016\/j.molimm.2008.02.006","volume":"45","author":"JQ Ao","year":"2008","unstructured":"Ao JQ, Ling E, Rao XJ, Yu XQ. A novel ML protein from Manduca sexta may function as a key accessory protein for lipopolysaccharide signaling. Mol Immunol. 2008;45(10):2772\u201381.","journal-title":"Mol Immunol"},{"issue":"36","key":"7429_CR92","doi-asserted-by":"publisher","first-page":"10079","DOI":"10.1073\/pnas.1611956113","volume":"113","author":"X Li","year":"2016","unstructured":"Li X, Saha P, Lib J, Blobel G, Pfeffer SR. Clues to the mechanism of cholesterol transfer from the structure of NPC1 middle lumenal domain bound to NPC2. Proc Nat Acad USA. 2016;113(36):10079\u201384.","journal-title":"Proc Nat Acad USA"},{"issue":"2","key":"7429_CR93","doi-asserted-by":"publisher","first-page":"137","DOI":"10.1006\/geno.2000.6151","volume":"65","author":"JP Davies","year":"2000","unstructured":"Davies JP, Levy B, Ioannou YA. Evidence for a niemann-pick C (NPC) gene family: Identification and characterization of NPC1L1. Genomics. 2000;65(2):137\u201345.","journal-title":"Genomics."},{"issue":"3","key":"7429_CR94","doi-asserted-by":"publisher","first-page":"567","DOI":"10.1007\/s10482-010-9526-1","volume":"99","author":"P Vijayaraj","year":"2011","unstructured":"Vijayaraj P, Sabarirajan J, Nachiappan V. Enhanced phospholipase B activity and alteration of phospholipids and neutral lipids in Saccharomyces cerevisiae exposed to N-nitrosonornicotine. Antonie Van Leeuwenhoek. 2011;99(3):567\u201377.","journal-title":"Antonie Van Leeuwenhoek"},{"issue":"32","key":"7429_CR95","doi-asserted-by":"publisher","first-page":"29792","DOI":"10.1074\/jbc.M301859200","volume":"278","author":"J Mima","year":"2003","unstructured":"Mima J, Narita Y, Chiba H, Hayashi R. The multiple site binding of carboxypeptidase Y inhibitor (IC) to the cognate proteinase. Implications for the biological roles of the phosphatidylethanolamine-binding protein. J Biol Chem. 2003;278(32):29792\u20138.","journal-title":"J Biol Chem"},{"key":"7429_CR96","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1016\/j.ibmb.2019.03.011","volume":"110","author":"M Tang","year":"2019","unstructured":"Tang M, Dong Z, Guo P, et al. Functional analysis and characterization of antimicrobial phosphatidylethanolamine-binding protein BmPEBP in the silkworm Bombyx mori. Insect Biochem Mol Biol. 2019;110:1\u20139.","journal-title":"Insect Biochem Mol Biol"},{"issue":"10","key":"7429_CR97","doi-asserted-by":"publisher","first-page":"1875","DOI":"10.1242\/jcs.01171","volume":"117","author":"MK Dougherty","year":"2004","unstructured":"Dougherty MK, Morrison DK. Unlocking the code of 14-3-3. J Cell Sci. 2004;117(10):1875\u201384.","journal-title":"J Cell Sci"},{"issue":"6","key":"7429_CR98","doi-asserted-by":"publisher","first-page":"e64984","DOI":"10.1371\/journal.pone.0064984","volume":"8","author":"J Liu","year":"2013","unstructured":"Liu J, Dyer D, Wang J, Wang S, Du X, Xu B, et al. 3-Oxoacyl-ACP Reductase from Schistosoma japonicum: Integrated In Silico-In Vitro Strategy for Discovering Antischistosomal Lead Compounds. PLoS One. 2013;8(6):e64984.","journal-title":"PLoS One"},{"issue":"2","key":"7429_CR99","doi-asserted-by":"publisher","first-page":"447","DOI":"10.1042\/BJ20050832","volume":"393","author":"SR Wickramasinghe","year":"2006","unstructured":"Wickramasinghe SR, Inglis KA, Urch JE, M\u00fcller S, van Aalten DMF, Fairlamb AH. Kinetic, inhibition and structural studies on 3-oxoacyl-ACP reductase from Plasmodium falciparum, a key enzyme in fatty acid biosynthesis. Biochem J. 2006;393(2):447\u201357.","journal-title":"Biochem J"},{"issue":"1","key":"7429_CR100","doi-asserted-by":"publisher","first-page":"e1003109","DOI":"10.1371\/journal.ppat.1003109","volume":"9","author":"JT Crowley","year":"2013","unstructured":"Crowley JT, Toledo AM, LaRocca TJ, Coleman JL, London E, Benach JL. Lipid Exchange between Borrelia burgdorferi and Host Cells. PLoS Pathog. 2013;9(1):e1003109.","journal-title":"PLoS Pathog"},{"issue":"17","key":"7429_CR101","doi-asserted-by":"publisher","first-page":"5491","DOI":"10.1073\/pnas.1502561112","volume":"112","author":"A Toledo","year":"2015","unstructured":"Toledo A, Monz\u00f3n JD, Coleman JL, Garcia-Monco JC, Benach JL. Hypercholesterolemia and ApoE deficiency result in severe infection with Lyme disease and relapsing-fever Borrelia. Proc Natl Acad Sci U S A. 2015;112(17):5491\u20136.","journal-title":"Proc Natl Acad Sci U S A"},{"issue":"1\u20132","key":"7429_CR102","doi-asserted-by":"publisher","first-page":"9","DOI":"10.1016\/S0167-4838(00)00148-5","volume":"1482","author":"DR Flower","year":"2000","unstructured":"Flower DR, North AC, Sansom CE. The lipocalin protein family: structural and sequence overview. Biochim Biophys Acta. 2000;1482(1\u20132):9\u201324.","journal-title":"Biochim Biophys Acta"},{"issue":"5","key":"7429_CR103","doi-asserted-by":"publisher","first-page":"661","DOI":"10.1016\/S1097-2765(00)80359-7","volume":"3","author":"GC Paesen","year":"1999","unstructured":"Paesen GC, Adams PL, Harlos K, Nuttall PA, Stuart DI. Tick histamine-binding proteins: isolation, cloning, and three-dimensional structure. Mol Cell. 1999;3(5):661\u201371.","journal-title":"Mol Cell"},{"issue":"1\u20132","key":"7429_CR104","doi-asserted-by":"publisher","first-page":"92","DOI":"10.1016\/S0167-4838(00)00168-0","volume":"1482","author":"GC Paesen","year":"2000","unstructured":"Paesen GC, Adams PL, Nuttall PA, Stuart DL. Tick histamine-binding proteins: lipocalins with a second binding cavity. Biochim Biophys Acta. 2000;1482(1\u20132):92\u2013101.","journal-title":"Biochim Biophys Acta"},{"issue":"3","key":"7429_CR105","doi-asserted-by":"publisher","first-page":"487","DOI":"10.1017\/S0031182000000950","volume":"80","author":"D Kemp","year":"1980","unstructured":"Kemp D, Bourne A. Boophilus microplus: The effect of histamine on the attachment of cattle-tick larvae\u2013studies in vivo and in vitro. Parasitology. 1980;80(3):487\u201396.","journal-title":"Parasitology."},{"issue":"7","key":"7429_CR106","doi-asserted-by":"publisher","first-page":"992","DOI":"10.1099\/mic.0.000495","volume":"163","author":"M Nakano","year":"2017","unstructured":"Nakano M, Oda K, Mukaihara T. Ralstonia solanacearum novel E3 ubiquitin ligase (NEL) effectors RipAW and RipAR suppress pattern-triggered immunity in plants. Microbiology. 2017;163(7):992\u20131002.","journal-title":"Microbiology."},{"issue":"3","key":"7429_CR107","doi-asserted-by":"publisher","first-page":"544","DOI":"10.1128\/MMBR.00015-14","volume":"78","author":"CM \u00dcnal","year":"2014","unstructured":"\u00dcnal CM, Steinert M. Microbial peptidyl-prolyl cis\/trans isomerases (PPIases): virulence factors and potential alternative drug targets. Microbiol Mol Biol Rev. 2014;78(3):544\u201371.","journal-title":"Microbiol Mol Biol Rev"},{"key":"7429_CR108","first-page":"967","volume-title":"Parasite annexins - New molecules with potential for drug and vaccine development","author":"A Hofmann","year":"2010","unstructured":"Hofmann A, Osman A, Leow CY, Driguez P, McManus DP, Jones MK. Parasite annexins - New molecules with potential for drug and vaccine development. Hoboken: BioEssays; 2010. p. 967\u201376."},{"issue":"40","key":"7429_CR109","doi-asserted-by":"publisher","first-page":"33733","DOI":"10.1074\/jbc.M112.341339","volume":"287","author":"M Martin","year":"2012","unstructured":"Martin M, Leffler J, Blom AM. Annexin A2 and A5 serve as new ligands for C1q on apoptotic cells. J Biol Chem. 2012;287(40):33733\u201344.","journal-title":"J Biol Chem"},{"issue":"3","key":"7429_CR110","doi-asserted-by":"publisher","first-page":"1355","DOI":"10.4049\/jimmunol.1500793","volume":"196","author":"B Renner","year":"2016","unstructured":"Renner B, Tong HH, Laskowski J, et al. Annexin A2 Enhances Complement Activation by Inhibiting Factor H. J Immunol. 2016;196(3):1355\u201365.","journal-title":"J Immunol"},{"key":"7429_CR111","doi-asserted-by":"publisher","first-page":"959","DOI":"10.3389\/fimmu.2018.00959","volume":"9","author":"H Zhi","year":"2018","unstructured":"Zhi H, Xie J, Skare JT. The Classical Complement Pathway Is Required to Control Borrelia burgdorferi Levels During Experimental Infection. Front Immunol. 2018;9:959.","journal-title":"Front Immunol"},{"issue":"3\u20134","key":"7429_CR112","doi-asserted-by":"publisher","first-page":"277","DOI":"10.1016\/j.cytogfr.2008.04.013","volume":"19","author":"C de Trez","year":"2008","unstructured":"de Trez C, Ware CF. The TNF receptor and Ig superfamily members form an integrated signaling circuit controlling dendritic cell homeostasis. Cytokine Growth Factor Rev. 2008;19(3\u20134):277\u201384.","journal-title":"Cytokine Growth Factor Rev"},{"key":"7429_CR113","doi-asserted-by":"publisher","first-page":"282","DOI":"10.1016\/j.virol.2015.12.015","volume":"489","author":"J DeBoer","year":"2016","unstructured":"DeBoer J, Madson CJ, Belshan M. Cyclophilin B enhances HIV-1 infection. Virology. 2016;489:282\u201391.","journal-title":"Virology."},{"issue":"1","key":"7429_CR114","doi-asserted-by":"publisher","first-page":"114","DOI":"10.1186\/s12985-017-0781-x","volume":"14","author":"K Zhao","year":"2017","unstructured":"Zhao K, Li J, He W, Song D, Zhang X, Zhang D, et al. Cyclophilin B facilitates the replication of Orf virus. Virol J. 2017;14(1):114.","journal-title":"Virol J"},{"key":"7429_CR115","first-page":"1","volume":"21","author":"FU Dawar","year":"2017","unstructured":"Dawar FU, Tu J, Khattak MNK, Mei J, Lin L. Cyclophilin a: A key factor in virus replication and potential target for anti-viral therapy. Curr Issues Mol Biol. 2017;21:1\u201320.","journal-title":"Curr Issues Mol Biol"},{"issue":"12","key":"7429_CR116","doi-asserted-by":"publisher","first-page":"1255","DOI":"10.1016\/j.dci.2007.03.012","volume":"31","author":"C Lesch","year":"2007","unstructured":"Lesch C, Goto A, Lindgren M, Bidla G, Dushay MS, Theopold U. A role for Hemolectin in coagulation and immunity in Drosophila melanogaster. Dev Comp Immunol. 2007;31(12):1255\u201363.","journal-title":"Dev Comp Immunol"},{"issue":"1","key":"7429_CR117","doi-asserted-by":"publisher","first-page":"99","DOI":"10.1042\/bj3590099","volume":"359","author":"A Goto","year":"2001","unstructured":"Goto A, Kumagai T, Kumagai C, Hirose J, Narita H, Mori H, et al. A Drosophila haemocyte-specific protein, hemolectin, similar to human von Willebrand factor. Biochem J. 2001;359(1):99\u2013108.","journal-title":"Biochem J"},{"issue":"3","key":"7429_CR118","doi-asserted-by":"publisher","first-page":"255","DOI":"10.1038\/s41590-018-0052-z","volume":"19","author":"M Akkaya","year":"2018","unstructured":"Akkaya M, Akkaya B, Kim AS, et al. Toll-like receptor 9 antagonizes antibody affinity maturation. Nat Immunol. 2018;19(3):255\u201366.","journal-title":"Nat Immunol"},{"key":"7429_CR119","doi-asserted-by":"publisher","first-page":"103997","DOI":"10.1016\/j.cellimm.2019.103997","volume":"346","author":"SN Ashley","year":"2019","unstructured":"Ashley SN, Somanathan S, Giles AR, Wilson JM. TLR9 signaling mediates adaptive immunity following systemic AAV gene therapy. Cell Immunol. 2019;346:103997.","journal-title":"Cell Immunol"},{"issue":"3\u20134","key":"7429_CR120","doi-asserted-by":"publisher","first-page":"211","DOI":"10.1016\/j.ijpara.2017.08.018","volume":"48","author":"T Hollmann","year":"2018","unstructured":"Hollmann T, Kim TK, Tirloni L, Radulovi\u0107 \u017dM, Pinto AFM, Diedrich JK, et al. Identification and characterization of proteins in the Amblyomma americanum tick cement cone. Int J Parasitol. 2018;48(3\u20134):211\u201324.","journal-title":"Int J Parasitol"},{"issue":"19","key":"7429_CR121","doi-asserted-by":"publisher","first-page":"18803","DOI":"10.1074\/jbc.M501731200","volume":"280","author":"S Raibaud","year":"2005","unstructured":"Raibaud S, Schwarz-Linek U, Kim JH, et al. Borrelia burgdorferi binds fibronectin through a tandem beta-zipper, a common mechanism of fibronectin binding in staphylococci, streptococci, and spirochetes. J Biol Chem. 2005;280(19):18803\u20139.","journal-title":"J Biol Chem"},{"issue":"17","key":"7429_CR122","doi-asserted-by":"publisher","first-page":"E3490","DOI":"10.1073\/pnas.1615007114","volume":"114","author":"AF Niddam","year":"2017","unstructured":"Niddam AF, Ebady R, Bansal A, Koehler A, Hinz B, Moriarty TJ. Plasma fibronectin stabilizes Borrelia burgdorferi-endothelial interactions under vascular shear stress by a catch-bond mechanism. Proc Natl Acad Sci U S A. 2017;114(17):E3490\u20138.","journal-title":"Proc Natl Acad Sci U S A"},{"issue":"8","key":"7429_CR123","doi-asserted-by":"publisher","first-page":"3184","DOI":"10.1128\/IAI.00349-15","volume":"83","author":"JA Caine","year":"2015","unstructured":"Caine JA, Coburn J. A short-term Borrelia burgdorferi infection model identifies tissue tropisms and bloodstream survival conferred by adhesion proteins. Infect Immun. 2015;83(8):3184\u201394.","journal-title":"Infect Immun"},{"issue":"23","key":"7429_CR124","doi-asserted-by":"publisher","first-page":"7482","DOI":"10.1128\/AEM.02483-13","volume":"79","author":"T Itoh","year":"2013","unstructured":"Itoh T, Hibi T, Fujii Y, Sugimoto I, Fujiwara A, Suzuki F, et al. Cooperative degradation of chitin by extracellular and cell surface-expressed chitinases from Paenibacillus sp. strain FPU7. Appl Environ Microbiol. 2013;79(23):7482\u201390.","journal-title":"Appl Environ Microbiol"},{"key":"7429_CR125","doi-asserted-by":"publisher","first-page":"201","DOI":"10.1007\/s00018-009-0161-9","volume":"67","author":"Y Arakane","year":"2010","unstructured":"Arakane Y, Muthukrishnan S. Insect chitinase and chitinase-like proteins. Cell Mol Life Sci. 2010;67:201\u201316.","journal-title":"Cell Mol Life Sci"},{"issue":"19","key":"7429_CR126","first-page":"3493","volume":"217","author":"TK Kim","year":"2014","unstructured":"Kim TK, Curran J, Mulenga A. Dual silencing of long and short Amblyomma Americanum acidic chitinase forms weakens the tick cement cone stability. J Exp Biol. 2014;217(19):3493\u2013503.","journal-title":"J Exp Biol"},{"issue":"12","key":"7429_CR127","doi-asserted-by":"publisher","first-page":"e0144507","DOI":"10.1371\/journal.pone.0144507","volume":"10","author":"F Almeida","year":"2015","unstructured":"Almeida F, Sardinha-Silva A, da Silva TA, Pessoni AM, Pinzan CF, Alegre-Maller ACP, et al. Toxoplasma gondii chitinase induces macrophage activation. PLoS One. 2015;10(12):e0144507.","journal-title":"PLoS One"},{"issue":"4","key":"7429_CR128","doi-asserted-by":"publisher","first-page":"373","DOI":"10.1007\/s00418-015-1400-9","volume":"145","author":"I Krist\u00f3","year":"2016","unstructured":"Krist\u00f3 I, Bajusz I, Bajusz C, Bork\u00fati P, Vilmos P. Actin, actin-binding proteins, and actin-related proteins in the nucleus. Histochem Cell Biol. 2016;145(4):373\u201388.","journal-title":"Histochem Cell Biol"},{"issue":"5","key":"7429_CR129","doi-asserted-by":"publisher","first-page":"1683","DOI":"10.1128\/IAI.01411-12","volume":"81","author":"X Naj","year":"2013","unstructured":"Naj X, Hoffmann AK, Himmel M, Linder S. The formins FMNL1 and mDia1 regulate coiling phagocytosis of Borrelia burgdorferi by primary human macrophages. Infect Immun. 2013;81(5):1683\u201395.","journal-title":"Infect Immun"},{"issue":"3-5","key":"7429_CR130","first-page":"221","volume":"11","author":"CW Wolgemuth","year":"2006","unstructured":"Wolgemuth CW, Charon NW, Goldstein SF, Goldstein RE. The flagellar cytoskeleton of the spirochetes. J Mol Microbiol Biotechnol. 2006;11(3-5):221\u20137.","journal-title":"J Mol Microbiol Biotechnol"},{"issue":"6","key":"7429_CR131","doi-asserted-by":"publisher","first-page":"1344","DOI":"10.1111\/j.1365-2958.2009.06951.x","volume":"74","author":"JA Hyde","year":"2009","unstructured":"Hyde JA, Shaw DK, Smith R, Trzeciakowski JP, Skare JT. The BosR regulatory protein of Borrelia burgdorferi interfaces with the RpoS regulatory pathway and modulates both the oxidative stress response and pathogenic properties of the Lyme disease spirochete. Mol Microbiol. 2009;74(6):1344\u201355.","journal-title":"Mol Microbiol"},{"issue":"11","key":"7429_CR132","doi-asserted-by":"publisher","first-page":"3141","DOI":"10.1128\/IAI.00430-16","volume":"84","author":"AC Showman","year":"2016","unstructured":"Showman AC, Aranjuez G, Adams PP, Jewett MW. Gene bb0318 is critical for the oxidative stress response and infectivity of Borrelia burgdorferi. Infect Immun. 2016;84(11):3141\u201351.","journal-title":"Infect Immun"},{"key":"7429_CR133","doi-asserted-by":"publisher","first-page":"301","DOI":"10.3389\/fpls.2016.00301","volume":"7","author":"II Ozyigit","year":"2016","unstructured":"Ozyigit II, Filiz E, Vatansever R, Kurtoglu KY, Koc I, \u00d6zt\u00fcrk MX, et al. Identification and comparative analysis of H2O2-scavenging enzymes (ascorbate peroxidase and glutathione peroxidase) in selected plants employing bioinformatics approaches. Front Plant Sci. 2016;7:301.","journal-title":"Front Plant Sci"},{"issue":"1","key":"7429_CR134","doi-asserted-by":"publisher","first-page":"41","DOI":"10.1089\/152308604771978336","volume":"6","author":"A-K Rundl\u00f6f","year":"2004","unstructured":"Rundl\u00f6f A-K, Arn\u00e9r ESJ. Regulation of the mammalian selenoprotein thioredoxin reductase 1 in relation to cellular phenotype, growth, and signaling events. Antioxid Redox Signal. 2004;6(1):41\u201352.","journal-title":"Antioxid Redox Signal"},{"key":"7429_CR135","doi-asserted-by":"publisher","first-page":"51","DOI":"10.1146\/annurev.pharmtox.45.120403.095857","volume":"45","author":"JD Hayes","year":"2005","unstructured":"Hayes JD, Flanagan JU, Jowsey IR. Glutathione transferases. Annu Rev Pharmacol Toxicol. 2005;45:51\u201388.","journal-title":"Annu Rev Pharmacol Toxicol"},{"key":"7429_CR136","doi-asserted-by":"publisher","first-page":"6049","DOI":"10.1016\/S0021-9258(18)63504-5","volume":"244","author":"JM McCord","year":"1969","unstructured":"McCord JM, Fridovich I. Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein). J Biol Chem. 1969;244:6049\u201355.","journal-title":"J Biol Chem"},{"issue":"6660","key":"7429_CR137","doi-asserted-by":"publisher","first-page":"580","DOI":"10.1038\/37551","volume":"390","author":"CM Fraser","year":"1997","unstructured":"Fraser CM, Casjens S, Huang WM, Sutton GG, Clayton R, Lathigra R, et al. Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi. Nature. 1997;390(6660):580\u20136.","journal-title":"Nature"},{"issue":"20","key":"7429_CR138","doi-asserted-by":"publisher","first-page":"11684","DOI":"10.1073\/pnas.2032956100","volume":"100","author":"JA Boylan","year":"2003","unstructured":"Boylan JA, Posey JE, Gherardini FC. Borrelia oxidative stress response regulator, BosR: a distinctive Zn-dependent transcriptional activator. Proc Natl Acad Sci USA. 2003;100(20):11684\u20139.","journal-title":"Proc Natl Acad Sci USA"},{"key":"7429_CR139","doi-asserted-by":"publisher","first-page":"1734","DOI":"10.3389\/fmicb.2017.01734","volume":"8","author":"DP Dulebohn","year":"2017","unstructured":"Dulebohn DP, Richards CL, Su H, Lawrence KA, Gherardini FC. Weak Organic Acids Decrease Borrelia burgdorferi Cytoplasmic pH, Eliciting an Acid Stress Response and Impacting RpoN- and RpoS-Dependent Gene Expression. Front Microbiol. 2017;8:1734.","journal-title":"Front Microbiol"},{"issue":"1","key":"7429_CR140","doi-asserted-by":"publisher","first-page":"57","DOI":"10.1111\/j.1600-0463.2004.apm1120110.x","volume":"112","author":"R Murgia","year":"2004","unstructured":"Murgia R, Cinco M. Induction of cystic forms by different stress conditions in Borrelia burgdorferi. APMIS. 2004;112(1):57\u201362.","journal-title":"APMIS."},{"issue":"5","key":"7429_CR141","doi-asserted-by":"publisher","first-page":"1352","DOI":"10.1111\/j.1365-2958.2004.04352.x","volume":"54","author":"J Seshu","year":"2004","unstructured":"Seshu J, Boylan JA, Hyde JA, Swingle KL, Gherardini FC, Skare JT. A conservative amino acid change alters the function of BosR, the redox regulator of Borrelia burgdorferi. Mol Microbiol. 2004;54(5):1352\u201363.","journal-title":"Mol Microbiol"},{"issue":"1","key":"7429_CR142","doi-asserted-by":"publisher","first-page":"265","DOI":"10.1128\/IAI.01018-09","volume":"78","author":"JA Hyde","year":"2010","unstructured":"Hyde JA, Shaw DK, Smith R 3rd, Trzeciakowski JP, Skare JT. Characterization of a conditional bosR mutant in Borrelia burgdorferi. Infect Immun. 2010;78(1):265\u201374.","journal-title":"Infect Immun"},{"issue":"3","key":"7429_CR143","doi-asserted-by":"publisher","first-page":"786","DOI":"10.1111\/j.1365-2958.2008.06204.x","volume":"68","author":"JA Boylan","year":"2008","unstructured":"Boylan JA, Lawrence KA, Downey JS, Gherardini FC. Borrelia burgdorferi membranes are the primary targets of reactive oxygen species. Mol Microbiol. 2008;68(3):786\u201399.","journal-title":"Mol Microbiol"},{"key":"7429_CR144","doi-asserted-by":"publisher","first-page":"881","DOI":"10.1146\/annurev.micro.54.1.881","volume":"54","author":"C Ratledge","year":"2000","unstructured":"Ratledge C, Dover LG. Iron metabolism in pathogenic bacteria. Annu Rev Microbiol. 2000;54:881\u2013941.","journal-title":"Annu Rev Microbiol"},{"issue":"2","key":"7429_CR145","doi-asserted-by":"publisher","first-page":"10.1128","DOI":"10.1128\/microbiolspec.VMBF-0010-2015","volume":"4","author":"JR Sheldon","year":"2016","unstructured":"Sheldon JR, Laakso HA, Heinrichs DE. Iron Acquisition Strategies of Bacterial Pathogens. Microbiol Spectrum. 2016;4(2):10.1128.","journal-title":"Microbiol Spectrum"},{"issue":"5471","key":"7429_CR146","doi-asserted-by":"publisher","first-page":"1651","DOI":"10.1126\/science.288.5471.1651","volume":"288","author":"JE Posey","year":"2000","unstructured":"Posey JE, Gherardini FC. Lack of a role for iron in the Lyme disease pathogen. Science. 2000;288(5471):1651\u20133.","journal-title":"Science."},{"issue":"1","key":"7429_CR147","doi-asserted-by":"publisher","first-page":"67","DOI":"10.1111\/j.1574-6968.1991.tb04714.x","volume":"65","author":"V Sambri","year":"1991","unstructured":"Sambri V, Cevenini R, la Placa M. Susceptibility of iron-loaded Borrelia burgdorferi to killing by hydrogen peroxide and human polymorphonuclear leucocytes. FEMS Microbiol Lett. 1991;65(1):67\u201371.","journal-title":"FEMS Microbiol Lett"},{"issue":"6","key":"7429_CR148","doi-asserted-by":"publisher","first-page":"414","DOI":"10.1002\/iub.1621","volume":"69","author":"P Arosio","year":"2017","unstructured":"Arosio P, Elia L, Poli M. Ferritin, cellular iron storage and regulation. IUBMB Life. 2017;69(6):414\u201322.","journal-title":"IUBMB Life"},{"issue":"3","key":"7429_CR149","doi-asserted-by":"publisher","first-page":"437","DOI":"10.1007\/s11302-012-9309-4","volume":"8","author":"H Zimmermann","year":"2012","unstructured":"Zimmermann H, Zebisch M, Str\u00e4ter N. Cellular function and molecular structure of ectonucleotidases. Purinergic Signal. 2012;8(3):437\u2013502.","journal-title":"Purinergic Signal"},{"issue":"47","key":"7429_CR150","doi-asserted-by":"publisher","first-page":"46195","DOI":"10.1074\/jbc.R300032200","volume":"278","author":"V Bianchi","year":"2003","unstructured":"Bianchi V, Spychala J. Mammalian 5\u2019-nucleotidases. J Biol Chem. 2003;278(47):46195\u20138.","journal-title":"J Biol Chem"},{"key":"7429_CR151","doi-asserted-by":"publisher","first-page":"15","DOI":"10.3390\/molecules24152778","volume":"24","author":"O P\u00e9terfi","year":"2019","unstructured":"P\u00e9terfi O, Boda F, Szab\u00f3 Z, Ferencz E, B\u00e1ba L. Hypotensive Snake Venom Components-A Mini-Review. Molecules. 2019;24:15.","journal-title":"Molecules."},{"issue":"8","key":"7429_CR152","doi-asserted-by":"publisher","first-page":"1477","DOI":"10.1161\/ATVBAHA.108.169219","volume":"28","author":"ML Hart","year":"2008","unstructured":"Hart ML, K\u00f6hler D, Eckle T, Kloor D, Stahl GL, Eltzschig HK. Direct treatment of mouse or human blood with soluble 5\u2019-nucleotidase inhibits platelet aggregation. Arterioscler Thromb Vasc Biol. 2008;28(8):1477\u201383.","journal-title":"Arterioscler Thromb Vasc Biol"},{"issue":"4","key":"7429_CR153","first-page":"563","volume":"94","author":"GJ Johnson","year":"1979","unstructured":"Johnson GJ, Schwartz BS, Leis LA. In vivo platelet retention in human bleeding-time wounds. I. Normal subjects and patients with platelet dysfunction. J Lab Clin Med. 1979;94(4):563.","journal-title":"J Lab Clin Med"},{"issue":"4","key":"7429_CR154","first-page":"574","volume":"94","author":"BS Schwartz","year":"1979","unstructured":"Schwartz BS, Leis LA, Johnson GJ. In vivo platelet retention in human bleeding-time wounds. II. Effect of aspirin ingestion. J Lab Clin Med. 1979;94(4):574\u201384.","journal-title":"J Lab Clin Med"},{"issue":"3","key":"7429_CR155","doi-asserted-by":"publisher","first-page":"141","DOI":"10.1038\/nrm.2016.159","volume":"18","author":"CM Hammond","year":"2017","unstructured":"Hammond CM, Str\u00f8mme CB, Huang H, Patel DJ, Groth A. Histone chaperone networks shaping chromatin function. Nat Rev Mol Cell Biol. 2017;18(3):141\u201358.","journal-title":"Nat Rev Mol Cell Biol"},{"issue":"6","key":"7429_CR156","doi-asserted-by":"publisher","first-page":"1753","DOI":"10.1681\/ASN.2016080925","volume":"28","author":"D Nakazawa","year":"2017","unstructured":"Nakazawa D, Kumar SV, Marschner J, Desai J, Holderied A, Rath L, et al. Histones and Neutrophil Extracellular Traps Enhance Tubular Necrosis and Remote Organ Injury in Ischemic AKI. J Am Soc Nephrol. 2017;28(6):1753\u201368.","journal-title":"J Am Soc Nephrol"},{"issue":"3","key":"7429_CR157","doi-asserted-by":"publisher","first-page":"441","DOI":"10.2217\/fmb.15.151","volume":"11","author":"M Hoeksema","year":"2016","unstructured":"Hoeksema M, van Eijk M, Haagsman HP, Hartshorn KL. Histones as mediators of host defense, inflammation and thrombosis. Future Microbiol. 2016;11(3):441\u201353.","journal-title":"Future Microbiol"},{"issue":"11","key":"7429_CR158","doi-asserted-by":"publisher","first-page":"5393","DOI":"10.4049\/jimmunol.1103771","volume":"189","author":"C Menten-Dedoyart","year":"2012","unstructured":"Menten-Dedoyart C, Faccinetto C, Golovchenko M, Dupiereux I, van Lerberghe P-B, Dubois S, et al. Neutrophil extracellular traps entrap and kill Borrelia burgdorferi sensu stricto spirochetes and are not affected by Ixodes ricinus tick saliva. J Immunol. 2012;189(11):5393\u2013401.","journal-title":"J Immunol"},{"issue":"11","key":"7429_CR159","doi-asserted-by":"publisher","first-page":"4755","DOI":"10.1074\/jbc.M116.764787","volume":"292","author":"L Li","year":"2017","unstructured":"Li L, Zhang Q, Yang H, Zou Q, Lai C, Jiang F, et al. Fumarylacetoacetate Hydrolase Knock-out Rabbit Model for Hereditary Tyrosinemia Type 1. J Biol Chem. 2017;292(11):4755\u201363.","journal-title":"J Biol Chem"},{"issue":"13","key":"7429_CR160","doi-asserted-by":"publisher","first-page":"6080","DOI":"10.1073\/pnas.89.13.6080","volume":"89","author":"KI Varughese","year":"1992","unstructured":"Varughese KI, Skinner MM, Whiteley JM, Matthews DA, Xuong NH. Crystal structure of rat liver dihydropteridine reductase. Proc Natl Acad Sci U S A. 1992;89(13):6080\u20134.","journal-title":"Proc Natl Acad Sci U S A"},{"issue":"2","key":"7429_CR161","doi-asserted-by":"publisher","first-page":"154","DOI":"10.1136\/adc.63.2.154","volume":"63","author":"A Ponzone","year":"1988","unstructured":"Ponzone A, Guardamagna O, Ferraris S, Bracco G, Niederwieser A, Cotton RG. Two mutations of dihydropteridine reductase deficiency. Arch Dis Child. 1988;63(2):154\u20137.","journal-title":"Arch Dis Child"},{"issue":"3","key":"7429_CR162","doi-asserted-by":"publisher","first-page":"689","DOI":"10.1042\/bj2320689","volume":"232","author":"PN Lowe","year":"1985","unstructured":"Lowe PN, Rowe AF. Aspartate: 2-oxoglutarate aminotransferase from trichomonas vaginalis. Identity of aspartate aminotransferase and aromatic amino acid aminotransferase. Biochem J. 1985;232(3):689\u201395.","journal-title":"Biochem J"},{"key":"7429_CR163","doi-asserted-by":"publisher","first-page":"110","DOI":"10.3389\/fmolb.2018.00110","volume":"5","author":"GA Grant","year":"2018","unstructured":"Grant GA. D-3-Phosphoglycerate Dehydrogenase. Front Mol Biosci. 2018;5:110.","journal-title":"Front Mol Biosci"},{"issue":"7","key":"7429_CR164","doi-asserted-by":"publisher","first-page":"e1002102","DOI":"10.1371\/journal.ppat.1002102","volume":"7","author":"CJ Pappas","year":"2011","unstructured":"Pappas CJ, Iyer R, Petzke MM, Caimano MJ, Radolf JD, Schwartz I. Borrelia burgdorferi requires glycerol for maximum fitness during the tick phase of the enzootic cycle. PLoS Pathog. 2011;7(7):e1002102.","journal-title":"PLoS Pathog"},{"issue":"2","key":"7429_CR165","doi-asserted-by":"publisher","first-page":"157","DOI":"10.1111\/j.1574-695X.2012.00996.x","volume":"66","author":"LL Hoon-Hanks","year":"2012","unstructured":"Hoon-Hanks LL, Morton EA, Lybecker MC, Battisti JM, Samuels DS, Drecktrah D. Borrelia burgdorferi malQ mutants utilize disaccharides and traverse the enzootic cycle. FEMS Immunol Med Microbiol. 2012;66(2):157\u201365.","journal-title":"FEMS Immunol Med Microbiol"},{"key":"7429_CR166","doi-asserted-by":"publisher","first-page":"3","DOI":"10.1128\/microbiolspec.MBP-0011-2014","volume":"3","author":"A Corona","year":"2015","unstructured":"Corona A, Schwartz I. Borrelia burgdorferi: Carbon Metabolism and the Tick-Mammal Enzootic Cycle. Microbiol Spectr. 2015;3:3.","journal-title":"Microbiol Spectr"},{"issue":"6","key":"7429_CR167","doi-asserted-by":"publisher","first-page":"822","DOI":"10.1016\/j.chom.2016.10.006","volume":"20","author":"M Oosting","year":"2016","unstructured":"Oosting M, Kerstholt M, Ter Horst R, et al. Functional and Genomic Architecture of Borrelia burgdorferi-Induced Cytokine Responses in Humans. Cell Host Microbe. 2016;20(6):822\u201333.","journal-title":"Cell Host Microbe"},{"issue":"24","key":"7429_CR168","doi-asserted-by":"publisher","first-page":"9629","DOI":"10.1073\/pnas.1307485110","volume":"110","author":"AI Stettner","year":"2013","unstructured":"Stettner AI, Segr\u00e8 D. The cost of efficiency in energy metabolism. Proc Natl Acad Sci USA. 2013;110(24):9629\u201330.","journal-title":"Proc Natl Acad Sci USA"},{"issue":"18","key":"7429_CR169","doi-asserted-by":"publisher","first-page":"12189","DOI":"10.1074\/jbc.R114.557314","volume":"289","author":"S Lenzen","year":"2014","unstructured":"Lenzen S. A fresh view of glycolysis and glucokinase regulation: history and current status. J Biol Chem. 2014;289(18):12189\u201394.","journal-title":"J Biol Chem"},{"key":"7429_CR170","doi-asserted-by":"publisher","first-page":"36","DOI":"10.1186\/s12896-015-0160-x","volume":"15","author":"E Bene\u0161ov\u00e1","year":"2015","unstructured":"Bene\u0161ov\u00e1 E, Lipovov\u00e1 P, Krejzov\u00e1 J, Kova\u013eov\u00e1 T, Buchtov\u00e1 P, Spiwok V, et al. Alpha-L-fucosidase isoenzyme iso2 from Paenibacillus thiaminolyticus. BMC Biotechnol. 2015;15:36.","journal-title":"BMC Biotechnol"},{"key":"7429_CR171","unstructured":"Melkonian EA, Asuka E, Schury MP. Physiology, Gluconeogenesis. In:  StatPearls. Treasure Island: StatPearls Publishing; 2020."},{"key":"7429_CR172","doi-asserted-by":"publisher","first-page":"e84625","DOI":"10.1371\/journal.pone.0084625","volume":"9","author":"B Troxell","year":"2014","unstructured":"Troxell B, Zhang JJ, Bourret TJ, Zeng MY, Blum J, Gherardini F, Hassan HM, Yang XF. Pyruvate protects pathogenic spirochetes from H2O2 killing. PLoS One. 2014;9:e84625.","journal-title":"PLoS One"},{"key":"7429_CR173","doi-asserted-by":"publisher","first-page":"43","DOI":"10.1016\/j.semcdb.2015.08.004","volume":"43","author":"WJ Israelsen","year":"2015","unstructured":"Israelsen WJ, Vander Heiden MG. Pyruvate kinase: Function, regulation and role in cancer. Semin Cell Dev Biol. 2015;43:43\u201351.","journal-title":"Semin Cell Dev Biol"},{"issue":"2","key":"7429_CR174","doi-asserted-by":"publisher","first-page":"75","DOI":"10.1016\/j.molbiopara.2014.02.005","volume":"193","author":"A G\u00f3mez-Arreaza","year":"2014","unstructured":"G\u00f3mez-Arreaza A, Acosta H, Qui\u00f1ones W, Concepci\u00f3n JL, Michels PAM, Avil\u00e1n L. Extracellular functions of glycolytic enzymes of parasites: unpredicted use of ancient proteins. Mol Biochem Parasitol. 2014;193(2):75\u201381.","journal-title":"Mol Biochem Parasitol"},{"issue":"4","key":"7429_CR175","doi-asserted-by":"publisher","first-page":"239","DOI":"10.1097\/SHK.0b013e3182a185ab","volume":"40","author":"A de Maio","year":"2013","unstructured":"de Maio A, Vazquez D. Extracellular heat shock proteins: a new location, a new function. Shock. 2013;40(4):239\u201346.","journal-title":"Shock"},{"issue":"7","key":"7429_CR176","doi-asserted-by":"publisher","first-page":"2186","DOI":"10.1128\/iai.58.7.2186-2191.1990","volume":"58","author":"MM Carreiro","year":"1990","unstructured":"Carreiro MM, Laux DC, Nelson DR. Characterization of the heat shock response and identification of heat shock protein antigens of Borrelia burgdorferi. Infect Immun. 1990;58(7):2186\u201391.","journal-title":"Infect Immun"},{"issue":"5","key":"7429_CR177","doi-asserted-by":"publisher","first-page":"1736","DOI":"10.1128\/iai.64.5.1736-1743.1996","volume":"64","author":"RG Cluss","year":"1996","unstructured":"Cluss RG, Goel AS, Rehm HL, Schoenecker JG, Boothby JT. Coordinate synthesis and turnover of heat shock proteins in Borrelia burgdorferi: degradation of DnaK during recovery from heat shock. Infect Immun. 1996;64(5):1736\u201343.","journal-title":"Infect Immun"},{"key":"7429_CR178","doi-asserted-by":"publisher","first-page":"15","DOI":"10.1189\/jlb.0306167","volume":"81","author":"E Schmitt","year":"2007","unstructured":"Schmitt E, Gehrmann M, Brunet M, Multhoff G, Garrido C. Intracellular and extracellular functions of heat shock proteins: repercussions in cancer therapy. J Leukoc Biol. 2007;81:15\u201327.","journal-title":"J Leukoc Biol"},{"issue":"1","key":"7429_CR179","doi-asserted-by":"publisher","first-page":"92","DOI":"10.1111\/j.1365-2915.2011.00973.x","volume":"26","author":"AT Busby","year":"2012","unstructured":"Busby AT, Ayllon N, Kocan KM, Blouin EF, de la Fuente G, Galindo RC, et al. Expression of heat shock proteins and subolesin affects stress responses, Anaplasma phagocytophilum infection and questing behaviour in the tick, Ixodes scapularis. Med Vet Entomol. 2012;26(1):92\u2013102.","journal-title":"Med Vet Entomol"},{"key":"7429_CR180","doi-asserted-by":"publisher","first-page":"307","DOI":"10.3389\/fcimb.2017.00307","volume":"7","author":"M Contreras","year":"2017","unstructured":"Contreras M, Alberdi P, Mateos-Hernandez L, Fernandez de Mera IG, Garcia-Perez AL, Vancova M, et al. Anaplasma phagocytophilum MSP4 and HSP70 Proteins Are Involved in Interactions with Host Cells during Pathogen Infection. Front Cell Infect Microbiol. 2017;7:307.","journal-title":"Front Cell Infect Microbiol"},{"key":"7429_CR181","doi-asserted-by":"publisher","first-page":"136","DOI":"10.1196\/annals.1428.073","volume":"1149","author":"R Vichido","year":"2008","unstructured":"Vichido R, Falcon A, Ramos JA, Alvarez A, Figueroa JV, Norimine J, et al. Expression analysis of heat shock protein 20 and rhoptry-associated protein 1a in sexual stages and kinetes of Babesia bigemina. Ann N Y Acad Sci. 2008;1149:136\u201340.","journal-title":"Ann N Y Acad Sci"},{"key":"7429_CR182","doi-asserted-by":"publisher","first-page":"44593","DOI":"10.1038\/srep44593","volume":"7","author":"A Vora","year":"2017","unstructured":"Vora A, Taank V, Dutta SM, Anderson JF, Fish D, Sonenshine DE, et al. Ticks elicit variable fibrinogenolytic activities upon feeding on hosts with different immune backgrounds. Sci Rep. 2017;7:44593.","journal-title":"Sci Rep"},{"issue":"20","key":"7429_CR183","doi-asserted-by":"publisher","first-page":"9305","DOI":"10.1128\/JVI.00661-16","volume":"90","author":"R Surtees","year":"2016","unstructured":"Surtees R, Dowall SD, Shaw A, Armstrong S, Hewson R, Carroll MW, et al. Heat Shock Protein 70 Family Members Interact with Crimean-Congo Hemorrhagic Fever Virus and Hazara Virus Nucleocapsid Proteins and Perform a Functional Role in the Nairovirus Replication Cycle. J Virol. 2016;90(20):9305\u201316.","journal-title":"J Virol"},{"key":"7429_CR184","doi-asserted-by":"publisher","first-page":"96","DOI":"10.3389\/fcell.2017.00096","volume":"5","author":"L Varricchio","year":"2017","unstructured":"Varricchio L, Falchi M, Dall\u2019Ora M, de Benedittis C, Ruggeri A, Uversky VN, et al. Calreticulin: Challenges Posed by the Intrinsically Disordered Nature of Calreticulin to the Study of Its Function. Front Cell Dev Biol. 2017;5:96.","journal-title":"Front Cell Dev Biol"},{"issue":"11","key":"7429_CR185","doi-asserted-by":"publisher","first-page":"1217","DOI":"10.1128\/CVI.00201-06","volume":"13","author":"F Alarcon-Chaidez","year":"2006","unstructured":"Alarcon-Chaidez F, Ryan R, Wikel S, Dardick K, Lawler C, Foppa IM, et al. Confirmation of tick bite by detection of antibody to Ixodes calreticulin salivary protein. Clin Vaccine Immunol. 2006;13(11):1217\u201322.","journal-title":"Clin Vaccine Immunol"},{"issue":"2","key":"7429_CR186","doi-asserted-by":"publisher","first-page":"279","DOI":"10.4269\/ajtmh.1998.59.279","volume":"59","author":"ML Sanders","year":"1998","unstructured":"Sanders ML, Jaworski DC, Sanchez JL, DeFraites RF, Glass GE, Scott AL, et al. Antibody to a cDNA-derived calreticulin protein from Amblyomma americanum as a biomarker of tick exposure in humans. Am J Trop Med Hyg. 1998;59(2):279\u201385.","journal-title":"Am J Trop Med Hyg"},{"issue":"8","key":"7429_CR187","doi-asserted-by":"publisher","first-page":"777","DOI":"10.1093\/oxfordjournals.aje.a009887","volume":"149","author":"ML Sanders","year":"1999","unstructured":"Sanders ML, Glass GE, Nadelman RB, Wormser GP, Scott AL, Raha S, et al. Antibody levels to recombinant tick calreticulin increase in humans after exposure to Ixodes scapularis (Say) and are correlated with tick engorgement indices. Am J Epidemiol. 1999;149(8):777\u201384.","journal-title":"Am J Epidemiol"},{"key":"7429_CR188","doi-asserted-by":"publisher","first-page":"318","DOI":"10.3389\/fphys.2019.00318","volume":"10","author":"S Antunes","year":"2019","unstructured":"Antunes S, Couto J, Ferrolho J, Sanches GS, Merino Charrez JO, De la Cruz Hernandez N, Mazuz M, Villar M, Shkap V, de la Fuente J, Domingos A. Transcriptome and Proteome Response of Rhipicephalus annulatus Tick Vector to Babesia bigemina Infection. Front Physiol. 2019;10:318.","journal-title":"Front Physiol"},{"issue":"1","key":"7429_CR189","doi-asserted-by":"publisher","first-page":"91","DOI":"10.1016\/j.ttbdis.2014.10.002","volume":"6","author":"TK Kim","year":"2015","unstructured":"Kim TK, Ibelli AMG, Mulenga A. Amblyomma americanum tick calreticulin binds C1q but does not inhibit activation of the classical complement cascade. Ticks Tick Borne Dis. 2015;6(1):91\u2013101.","journal-title":"Ticks Tick Borne Dis"},{"issue":"6","key":"7429_CR190","first-page":"761","volume":"20","author":"V Hwa","year":"1999","unstructured":"Hwa V, Oh Y, Rosenfeld RG. The insulin-like growth factor-binding protein (IGFBP) superfamily. Endocr Rev. 1999;20(6):761\u201387.","journal-title":"Endocr Rev"},{"key":"7429_CR191","doi-asserted-by":"publisher","first-page":"5","DOI":"10.1111\/imb.12180","volume":"24","author":"ZM Radulovic","year":"2015","unstructured":"Radulovic ZM, Porter LM, Kim TK, Bakshi M, Mulenga A. Amblyomma americanum tick saliva insulin-like growth factor binding protein-related protein 1 binds insulin but not insulin-like growth factors. Insect Mol Biol. 2015;24:5.","journal-title":"Insect Mol Biol"},{"issue":"11","key":"7429_CR192","doi-asserted-by":"publisher","first-page":"e1008128","DOI":"10.1371\/journal.ppat.1008128","volume":"15","author":"M Bakshi","year":"2019","unstructured":"Bakshi M, Kim TK, Porter L, Mwangi W, Mulenga A. Amblyomma americanum ticks utilizes countervailing pro and anti-inflammatory proteins to evade host defense. PLoS Pathog. 2019;15(11):e1008128.","journal-title":"PLoS Pathog"},{"issue":"Pt 7","key":"7429_CR193","doi-asserted-by":"publisher","first-page":"1153","DOI":"10.1242\/jeb.035204","volume":"213","author":"A Mulenga","year":"2010","unstructured":"Mulenga A, Khumthong R. Silencing of three Amblyomma americanum (L.) insulin-like growth factor binding protein-related proteins prevents ticks from feeding to repletion. J Exp Biol. 2010;213(Pt 7):1153\u201361.","journal-title":"J Exp Biol"},{"key":"7429_CR194","doi-asserted-by":"publisher","first-page":"267","DOI":"10.1007\/s10493-007-9064-3","volume":"41","author":"A Mulenga","year":"2007","unstructured":"Mulenga A, Blandon M, Khumthong R. The molecular basis of the Amblyomma americanum tick attachment phase. Exp Appl Acarol. 2007;41:267\u201387.","journal-title":"Exp Appl Acarol"},{"issue":"6","key":"7429_CR195","doi-asserted-by":"publisher","first-page":"439","DOI":"10.1016\/j.ijpara.2012.12.012","volume":"43","author":"A Mulenga","year":"2013","unstructured":"Mulenga A, Kim TK, Ibelli AMG. Deorphanization and target validation of cross-tick species conserved novel Amblyomma americanum tick saliva protein. Int J Parasitol. 2013;43(6):439\u201351.","journal-title":"Int J Parasitol"},{"issue":"12","key":"7429_CR196","doi-asserted-by":"publisher","first-page":"2415","DOI":"10.1111\/febs.14810","volume":"286","author":"P Bierwagen","year":"2019","unstructured":"Bierwagen P, Szpotkowski K, Jaskolski M, Urbanowicz A. Borrelia outer surface protein C is capable of human fibrinogen binding. FEBS J. 2019;286(12):2415\u201328 https:\/\/doi.org\/10.1111\/febs.14810.","journal-title":"FEBS J"},{"issue":"2","key":"7429_CR197","doi-asserted-by":"publisher","first-page":"220","DOI":"10.1172\/JCI200419894","volume":"113","author":"U Pal","year":"2004","unstructured":"Pal U, Yang X, Chen M, et al. OspC facilitates Borrelia burgdorferi invasion of Ixodes scapularis salivary glands. J Clin Invest. 2004;113(2):220\u201330 https:\/\/doi.org\/10.1172\/JCI19894.","journal-title":"J Clin Invest"},{"key":"7429_CR198","doi-asserted-by":"publisher","first-page":"e1006764","DOI":"10.1371\/journal.ppat.1006764","volume":"14","author":"W Zhou","year":"2018","unstructured":"Zhou W, Woodson M, Neupane B, Bai F, Sherman MB, Choi KH, Neelakanta G, Sultana H. Exosomes serve as novel modes of tick-borne flavivirus transmission from arthropod to human cells and facilitates dissemination of viral RNA and proteins to the vertebrate neuronal cells. PLoS Pathog. 2018;14:e1006764.","journal-title":"PLoS Pathog"},{"key":"7429_CR199","doi-asserted-by":"publisher","first-page":"e0148073","DOI":"10.1371\/journal.pone.0148073","volume":"11","author":"YN Zhang","year":"2016","unstructured":"Zhang YN, Vernooij F, Ibrahim I, Ooi S, Gijsberts CM, Schoneveld AH, Sen KW, den Ruijter HM, Timmers L, Richards AM, Jong CT, Mazlan I, Wang JW, Lam CS, de Kleijn DP. Extracellular Vesicle Proteins Associated with Systemic Vascular Events Correlate with Heart Failure: An Observational Study in a Dyspnoea Cohort. PLoS One. 2016;11:e0148073.","journal-title":"PLoS One"},{"key":"7429_CR200","doi-asserted-by":"publisher","first-page":"450","DOI":"10.1165\/rcmb.2016-0033OC","volume":"55","author":"A Vargas","year":"2016","unstructured":"Vargas A, Roux-Dalvai F, Droit A, Lavoie JP. Neutrophil-Derived Exosomes: A New Mechanism Contributing to Airway Smooth Muscle Remodeling. Am J Respir Cell Mol Biol. 2016;55:450\u201361.","journal-title":"Am J Respir Cell Mol Biol"},{"key":"7429_CR201","doi-asserted-by":"publisher","first-page":"3258","DOI":"10.1074\/mcp.M115.053934","volume":"14","author":"K Cwiklinski","year":"2015","unstructured":"Cwiklinski K, de la Torre-Escudero E, Trelis M, Bernal D, Dufresne PJ, Brennan GP, O'Neill S, Tort J, Paterson S, Marcilla A, Dalton JP, Robinson MW. The Extracellular Vesicles of the Helminth Pathogen, Fasciola hepatica: Biogenesis Pathways and Cargo Molecules Involved in Parasite Pathogenesis. Mol Cell Proteomics. 2015;14:3258\u201373.","journal-title":"Mol Cell Proteomics"},{"key":"7429_CR202","doi-asserted-by":"publisher","first-page":"e45974","DOI":"10.1371\/journal.pone.0045974","volume":"7","author":"A Marcilla","year":"2012","unstructured":"Marcilla A, Trelis M, Cortes A, Sotillo J, Cantalapiedra F, Minguez MT, Valero ML, Sanchez del Pino MM, Munoz-Antoli C, Toledo R, Bernal D. Extracellular vesicles from parasitic helminths contain specific excretory\/secretory proteins and are internalized in intestinal host cells. PLoS One. 2012;7:e45974.","journal-title":"PLoS One"},{"key":"7429_CR203","doi-asserted-by":"publisher","first-page":"e0006438","DOI":"10.1371\/journal.pntd.0006438","volume":"12","author":"H Harischandra","year":"2018","unstructured":"Harischandra H, Yuan W, Loghry HJ, Zamanian M, Kimber MJ. Profiling extracellular vesicle release by the filarial nematode Brugia malayi reveals sex-specific differences in cargo and a sensitivity to ivermectin. PLoS Negl Trop Dis. 2018;12:e0006438.","journal-title":"PLoS Negl Trop Dis"},{"key":"7429_CR204","doi-asserted-by":"publisher","first-page":"4608","DOI":"10.1128\/IAI.71.8.4608-4613.2003","volume":"71","author":"M Labandeira-Rey","year":"2003","unstructured":"Labandeira-Rey M, Seshu J, Skare JT. The absence of linear plasmid 25 or 28-1 of Borrelia burgdorferi dramatically alters the kinetics of experimental infection via distinct mechanisms. Infect Immun. 2003;71:4608\u201313.","journal-title":"Infect Immun"},{"issue":"4","key":"7429_CR205","doi-asserted-by":"publisher","first-page":"2139","DOI":"10.1128\/IAI.70.4.2139-2150.2002","volume":"70","author":"AF Elias","year":"2002","unstructured":"Elias AF, Stewart PE, Grimm D, Caimano MJ, Eggers CH, Tilly K, Bono JL, Akins DR, Radolf JD, Schwan TG, Rosa P. Clonal polymorphism of Borrelia burgdorferi strain B31 MI: 2002. implications for mutagenesis in an infectious strain background. Infect Immun. 2002;70(4):2139\u201350 https:\/\/doi.org\/10.1128\/iai.70.4.2139-2150.","journal-title":"Infect Immun"},{"key":"7429_CR206","doi-asserted-by":"publisher","first-page":"730","DOI":"10.4269\/ajtmh.1992.47.730","volume":"47","author":"BJ Johnson","year":"1992","unstructured":"Johnson BJ, Happ CM, Mayer LW, Piesman J. Detection of Borrelia burgdorferi in ticks by species-specific amplification of the flagellin gene. Am J Trop Med Hyg. 1992;47:730\u201341.","journal-title":"Am J Trop Med Hyg"},{"issue":"18","key":"7429_CR207","doi-asserted-by":"publisher","first-page":"2162","DOI":"10.1002\/rcm.1603","volume":"18","author":"WH McDonald","year":"2004","unstructured":"McDonald WH, Tabb DL, Sadygov RG, MacCoss MJ, Venable J, Graumann J, et al. MS1, MS2, and SQT-three unified, compact, and easily parsed file formats for the storage of shotgun proteomic spectra and identifications. Rapid Commun Mass Spectrom. 2004;18(18):2162\u20138.","journal-title":"Rapid Commun Mass Spectrom"},{"key":"7429_CR208","doi-asserted-by":"publisher","first-page":"16","DOI":"10.1016\/j.jprot.2015.07.001","volume":"129","author":"T Xu","year":"2015","unstructured":"Xu T, Park SK, Venable JD, Wohlschlegel JA, Diedrich JK, Cociorva D, et al. ProLuCID: An improved SEQUEST-like algorithm with enhanced sensitivity and specificity. J Proteome. 2015;129:16\u201324.","journal-title":"J Proteome"},{"issue":"5","key":"7429_CR209","doi-asserted-by":"publisher","first-page":"680","DOI":"10.1093\/bioinformatics\/btq003","volume":"26","author":"Y Huang","year":"2010","unstructured":"Huang Y, Niu B, Gao Y, Fu L, Li W. CD-HIT Suite: a web server for clustering and comparing biological sequences. Bioinformatics. 2010;26(5):680\u20132.","journal-title":"Bioinformatics."},{"issue":"Database issue","key":"7429_CR210","doi-asserted-by":"publisher","first-page":"D115","DOI":"10.1093\/nar\/gkh131","volume":"32","author":"R Apweiler","year":"2004","unstructured":"Apweiler R, Bairoch A, Wu CH, et al. UniProt: the Universal Protein knowledgebase. Nucleic Acids Res. 2004;32(Database issue):D115\u20139.","journal-title":"Nucleic Acids Res"},{"issue":"W1","key":"7429_CR211","doi-asserted-by":"publisher","first-page":"W296","DOI":"10.1093\/nar\/gky427","volume":"46","author":"A Waterhouse","year":"2018","unstructured":"Waterhouse A, Bertoni M, Bienert S, et al. SWISS-MODEL: homology modelling of protein structures and complexes. Nucleic Acids Res. 2018;46(W1):W296\u2013303.","journal-title":"Nucleic Acids Res"},{"issue":"12","key":"7429_CR212","doi-asserted-by":"publisher","first-page":"e28525","DOI":"10.1371\/journal.pone.0028525","volume":"6","author":"S Karim","year":"2011","unstructured":"Karim S, Singh P, Ribeiro JMC. A deep insight into the sialotranscriptome of the gulf coast tick, Amblyomma maculatum. PLoS One. 2011;6(12):e28525.","journal-title":"PLoS One"}],"container-title":["BMC Genomics"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1186\/s12864-021-07429-0.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/article\/10.1186\/s12864-021-07429-0\/fulltext.html","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1186\/s12864-021-07429-0.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,1,29]],"date-time":"2023-01-29T20:04:54Z","timestamp":1675022694000},"score":1,"resource":{"primary":{"URL":"https:\/\/bmcgenomics.biomedcentral.com\/articles\/10.1186\/s12864-021-07429-0"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2021,3,4]]},"references-count":212,"journal-issue":{"issue":"1","published-online":{"date-parts":[[2021,12]]}},"alternative-id":["7429"],"URL":"https:\/\/doi.org\/10.1186\/s12864-021-07429-0","relation":{},"ISSN":["1471-2164"],"issn-type":[{"value":"1471-2164","type":"electronic"}],"subject":[],"published":{"date-parts":[[2021,3,4]]},"assertion":[{"value":"7 September 2020","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"8 February 2021","order":2,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"4 March 2021","order":3,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"All experiments were done according to the animal use protocol approved by Texas A&M University Institutional Animal Care and Use Committee (IACUC) (AUP 2017-0068 and 2018-0001) that meets all federal requirements, as defined in the Animal Welfare Act (AWA), the Public Health Service Policy (PHS), and the Humane Care and Use of Laboratory Animals. Rabbits used in this study were commercially purchased through Comparative Medicine Program at Texas A&M from Harlan Sprague Dawley Inc. (Indianapolis, IN, USA).","order":1,"name":"Ethics","group":{"name":"EthicsHeading","label":"Ethics approval and consent to participate"}},{"value":"Not applicable.","order":2,"name":"Ethics","group":{"name":"EthicsHeading","label":"Consent for publication"}},{"value":"The authors declare that they have no competing interest.","order":3,"name":"Ethics","group":{"name":"EthicsHeading","label":"Competing interests"}}],"article-number":"152"}}