{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,4]],"date-time":"2026-10-04T07:59:45Z","timestamp":1791100785496,"version":"4.1.0"},"reference-count":60,"publisher":"The Company of Biologists","issue":"18","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2002,9,15]]},"abstract":"<jats:title>SUMMARY<\/jats:title>\n               <jats:p>To attempt description of the set of mRNA and protein (sialome) expressed in the salivary glands of the tick Ixodes scapularis, we randomly sequenced 735 clones of a full-length salivary gland cDNA library of this arthropod and performed Edman degradation of protein bands from salivary gland homogenates (SGH) and saliva separated by SDS-PAGE. The sequences were grouped into 410 clusters, of which 383 are not associated with known I. scapularis sequences. 15- and 17-protein bands from PAGE yielded amino-terminal information on the saliva and salivary gland gels,respectively. We attributed 19 of these sequences to translation products of the cDNA library. Full-length sequences were obtained for 87 clones. Among these protein sequences are several protease inhibitors of distinct classes,metalloproteases, novel proteins with histamine-binding domains, and several peptide families of unknown function displaying different conserved cysteine residues, many of which contain single Kunitz domains. This work provides information into the diversity of messages expressed in the salivary glands of I. scapularis, describes novel sequences that may be responsible for known biological activites, indicates further biological activities that may be present in I. scapularis saliva and identifies novel vaccine targets that may be used in Lyme disease prevention.<\/jats:p>","DOI":"10.1242\/jeb.205.18.2843","type":"journal-article","created":{"date-parts":[[2021,4,25]],"date-time":"2021-04-25T05:02:32Z","timestamp":1619326952000},"page":"2843-2864","source":"Crossref","is-referenced-by-count":250,"title":["Exploring the sialome of the tick <i>Ixodes scapularis<\/i>"],"prefix":"10.1242","volume":"205","author":[{"given":"Jesus G.","family":"Valenzuela","sequence":"first","affiliation":[{"name":"Medical Entomology Section, Laboratory of Parasitic Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health,Bethesda Maryland, 20892-0425, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ivo M. B.","family":"Francischetti","sequence":"additional","affiliation":[{"name":"Medical Entomology Section, Laboratory of Parasitic Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health,Bethesda Maryland, 20892-0425, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Van My","family":"Pham","sequence":"additional","affiliation":[{"name":"Medical Entomology Section, Laboratory of Parasitic Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health,Bethesda Maryland, 20892-0425, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mark K.","family":"Garfield","sequence":"additional","affiliation":[{"name":"Research Technologies Branch, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Thomas N.","family":"Mather","sequence":"additional","affiliation":[{"name":"Center for Vector-Borne Disease, University of Rhode Island, Kingston 02881-0804, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jose\u0301 M. C.","family":"Ribeiro","sequence":"additional","affiliation":[{"name":"Medical Entomology Section, Laboratory of Parasitic Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health,Bethesda Maryland, 20892-0425, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"237","reference":[{"key":"2021042504581432800_REF1","doi-asserted-by":"crossref","unstructured":"Altschul, S. F., Gish, W., Miller, W., Myers, E. W. and Lipman,D. J. (1990). Basic local alignment search tool. J. Mol. Biol.215,403-410.","DOI":"10.1016\/S0022-2836(05)80360-2"},{"key":"2021042504581432800_REF2","doi-asserted-by":"crossref","unstructured":"Altschul, S. F., Madden, T. L., Schaffer, A. A., Zhang, J.,Zhang, Z., Miller, W. and Lipman, D. J. (1997). Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res.25,3389-3402.","DOI":"10.1093\/nar\/25.17.3389"},{"key":"2021042504581432800_REF3","doi-asserted-by":"crossref","unstructured":"Armstrong, P. B. and Quigley, J. P. (1999). Alpha2-macroglobulin: an evolutionarily conserved arm of the innate immune system. Dev. Comp. Immunol.23,375-390.","DOI":"10.1016\/S0145-305X(99)00018-X"},{"key":"2021042504581432800_REF4","unstructured":"Aumuller, G., Wilhelm, B. and Seitz, J. (1999). Apocrine secretion \u2014 fact or artifact? Anat. Anz.181,437-446."},{"key":"2021042504581432800_REF5","doi-asserted-by":"crossref","unstructured":"Bateman, A., Birney, E., Durbin, R., Eddy, S. R., Howe, K. L. and Sonnhammer, E. L. (2000). The Pfam protein families database. Nucleic Acids Res.28,263-266.","DOI":"10.1093\/nar\/28.1.263"},{"key":"2021042504581432800_REF6","doi-asserted-by":"crossref","unstructured":"Borth, W. (1992). Alpha 2-macroglobulin, a multifunctional binding protein with targeting characteristics. FASEB J.6,3345-3353.","DOI":"10.1096\/fasebj.6.15.1281457"},{"key":"2021042504581432800_REF7","doi-asserted-by":"crossref","unstructured":"Champagne, D. E., Smartt, C. T., Ribeiro, J. M. and James, A. A. (1995). The salivary gland-specific apyrase of the mosquito Aedes aegypti is a member of the 5\u2032-nucleotidase family. Proc. Natl. Acad. Sci. USA92,694-698.","DOI":"10.1073\/pnas.92.3.694"},{"key":"2021042504581432800_REF8","doi-asserted-by":"crossref","unstructured":"Charlab, R., Valenzuela, J. G., Rowton, E. D. and Ribeiro, J. M. (1999). Toward an understanding of the biochemical and pharmacological complexity of the saliva of a hematophagous sand fly Lutzomyia longipalpis.Proc. Natl. Acad. Sci. USA96,15155-15160.","DOI":"10.1073\/pnas.96.26.15155"},{"key":"2021042504581432800_REF9","doi-asserted-by":"crossref","unstructured":"Charpentier, S., Amiche, M., Mester, J., Vouille, V., Le Caer,J. P., Nicolas, P. and Delfour, A. (1998). Structure,synthesis, and molecular cloning of dermaseptins B, a family of skin peptide antibiotics. J. Biol. Chem.273,14690-14697.","DOI":"10.1074\/jbc.273.24.14690"},{"key":"2021042504581432800_REF10","doi-asserted-by":"crossref","unstructured":"Dainichi, T., Maekawa, Y., Ishii, K., Zhang, T., Nashed, B. F.,Sakai, T., Takashima, M. and Himeno, K. (2001). Nippocystatin, a cysteine protease inhibitor from Nippostrongylus brasiliensis, inhibits antigen processing and modulates antigen-specific immune response. Infect. Immun.69,7380-7386.","DOI":"10.1128\/IAI.69.12.7380-7386.2001"},{"key":"2021042504581432800_REF11","doi-asserted-by":"crossref","unstructured":"Das, S., Banerjee, G., DePonte, K., Marcantonio, N., Kantor, F. S. and Fikrig, E. (2001). Salp25D, an Ixodes scapularis antioxidant, is 1 of 14 immunodominant antigens in engorged tick salivary glands. J. Infect. Dis.184,1056-1064.","DOI":"10.1086\/323351"},{"key":"2021042504581432800_REF12","doi-asserted-by":"crossref","unstructured":"Das, S., Marcantonio, N., Deponte, K., Telford, S. R., 3rd,Anderson, J. F., Kantor, F. S. and Fikrig, E. (2000). SALP16,a gene induced in Ixodes scapularis salivary glands during tick feeding. Am. J. Trop. Med. Hyg.62, 99-105.","DOI":"10.4269\/ajtmh.2000.62.99"},{"key":"2021042504581432800_REF13","unstructured":"Dennis, M. S. and Lazarus, R. A. (1994). Kunitz domain inhibitors of tissue factor-factor VIIa. I. Potent inhibitors selected from libraries by phage display. J. Biol. Chem.269,22129-22136."},{"key":"2021042504581432800_REF14","doi-asserted-by":"crossref","unstructured":"Dickinson, R. G., O'Hagan, J. E., Shotz, M., Binnington, K. C. and Hegarty, M. P. (1976). Prostaglandin in the saliva of the cattle tick Boophilus microplus.Aust. J. Exp. Biol. Med. Sci.54,475-486.","DOI":"10.1038\/icb.1976.48"},{"key":"2021042504581432800_REF15","doi-asserted-by":"crossref","unstructured":"Fogaca, A. C., da Silva, P. I., Jr, Miranda, M. T., Bianchi, A. G., Miranda, A., Ribolla, P. E. and Daffre, S. (1999). Antimicrobial activity of a bovine hemoglobin fragment in the tick Boophilus microplus.J. Biol. Chem.274,25330-25334.","DOI":"10.1074\/jbc.274.36.25330"},{"key":"2021042504581432800_REF16","doi-asserted-by":"crossref","unstructured":"Francischetti, I. M., Valenzuela, J. G., Andersen, J. F.,Mather, T. N. and Ribeiro, J. M. C. (2002). Ixolaris, a novel recombinant tissue factor pathway inhibitor (TFPI) from the salivary glands of the tick, Ixodes scapularis: identification of factor X and factor Xa as scaffolds for the inhibition of factor VIIa\/tissue factor complex. Blood99,3602-3612.","DOI":"10.1182\/blood-2001-12-0237"},{"key":"2021042504581432800_REF17","doi-asserted-by":"crossref","unstructured":"Gillespie, R. D., Dolan, M. C., Piesman, J. and Titus, R. G.(2001). Identification of an IL-2 binding protein in the saliva of the Lyme disease vector tick, Ixodes scapularis.J. Immunol.166,4319-4326.","DOI":"10.4049\/jimmunol.166.7.4319"},{"key":"2021042504581432800_REF18","doi-asserted-by":"crossref","unstructured":"Girard, T. J., Warren, L. A., Novotny, W. F., Likert, K. M.,Brown, S. G., Miletich, J. P. and Broze, G. J., Jr (1989). Functional significance of the Kunitz-type inhibitory domains of lipoprotein-associated coagulation inhibitor. Nature338,518-520.","DOI":"10.1038\/338518a0"},{"key":"2021042504581432800_REF19","doi-asserted-by":"crossref","unstructured":"Hartmann, S., Kyewski, B., Sonnenburg, B. and Lucius, R.(1997). A filarial cysteine protease inhibitor down-regulates T cell proliferation and enhances interleukin-10 production. Eur. J. Immunol.27,2253-2260.","DOI":"10.1002\/eji.1830270920"},{"key":"2021042504581432800_REF20","doi-asserted-by":"crossref","unstructured":"Harvey, A. L. (2001). Twenty years of dendrotoxins. Toxicon39, 15-26.","DOI":"10.1016\/S0041-0101(00)00162-8"},{"key":"2021042504581432800_REF21","doi-asserted-by":"crossref","unstructured":"Higgs, G. A., Vane, J. R., Hart, R. J., Porter, C. and Wilson,R. G. (1976). Prostaglandins in the saliva of the cattle tick, Boophilus microplus (Canestrini) (Acarina, Ixodidae). Bull. Ent. Res.66,665-670.","DOI":"10.1017\/S0007485300010725"},{"key":"2021042504581432800_REF22","doi-asserted-by":"crossref","unstructured":"Hooper, N. M. (1994). Families of zinc metalloproteases. FEBS Lett.354, 1-6.","DOI":"10.1016\/0014-5793(94)01079-X"},{"key":"2021042504581432800_REF23","doi-asserted-by":"crossref","unstructured":"Jeanmougin, F., Thompson, J. D., Gouy, M., Higgins, D. G. and Gibson, T. J. (1998). Multiple sequence alignment with Clustal X. Trends Biochem. Sci.23,403-405.","DOI":"10.1016\/S0968-0004(98)01285-7"},{"key":"2021042504581432800_REF24","doi-asserted-by":"crossref","unstructured":"Jia, L. G., Shimokawa, K., Bjarnason, J. B. and Fox, J. W.(1996). Snake venom metalloproteinases: structure, function and relationship to the ADAMs family of proteins. Toxicon34,1269-1276.","DOI":"10.1016\/S0041-0101(96)00108-0"},{"key":"2021042504581432800_REF25","doi-asserted-by":"crossref","unstructured":"Jones, L. D., Davies, C. R., Steele, G. M. and Nuttall, P. A. (1987). A novel mode of arbovirus transmission involving a nonviremic host. Science237,775-777.","DOI":"10.1126\/science.3616608"},{"key":"2021042504581432800_REF26","doi-asserted-by":"crossref","unstructured":"Jones, L. D., Davies, C. R., Williams, T., Cory, J. and Nuttall,P. A. (1990). Non-viraemic transmission of Thogoto virus:vector efficiency of Rhipicephalus appendiculatus and Amblyomma variegatum.Trans. R. Soc. Trop. Med. Hyg.84,846-948.","DOI":"10.1016\/0035-9203(90)90104-M"},{"key":"2021042504581432800_REF27","doi-asserted-by":"crossref","unstructured":"Leonardi, A., Aragon-Ortiz, F., Gubensek, F. and Krizaj, I.(1999). Partial primary structure of a fibrinogenase from the venom of the snake Lachesis stenophrys. J. Chromatogr. A852,237-243.","DOI":"10.1016\/S0021-9673(99)00260-5"},{"key":"2021042504581432800_REF28","doi-asserted-by":"crossref","unstructured":"Lundwall, A. and Lazure, C. (1995). A novel gene family encoding proteins with highly differing structure because of a rapidly evolving exon. FEBS Lett.374, 53-56.","DOI":"10.1016\/0014-5793(95)01076-Q"},{"key":"2021042504581432800_REF29","doi-asserted-by":"crossref","unstructured":"Manoury, B., Gregory, W. F., Maizels, R. M. and Watts, C.(2001). Bm-CPI-2, a cystatin homolog secreted by the filarial parasite Brugia malayi, inhibits class II MHC-restricted antigen processing. Curr. Biol.11,447-451.","DOI":"10.1016\/S0960-9822(01)00118-X"},{"key":"2021042504581432800_REF30","doi-asserted-by":"crossref","unstructured":"Milstone, A. M., Harrison, L. M., Bungiro, R. D., Kuzmic, P. and Cappello, M. (2000). A broad spectrum Kunitz type serine protease inhibitor secreted by the hookworm Ancylostoma ceylanicum.J. Biol. Chem.275,29391-29399.","DOI":"10.1074\/jbc.M002715200"},{"key":"2021042504581432800_REF31","unstructured":"Mulenga, A., Sugimoto, C. and Onuma, M. (1999). Characterization of proteolytic enzymes expressed in the midgut of Haemaphysalis longicornis.Jpn. J. Vet. Res.46,179-184."},{"key":"2021042504581432800_REF32","doi-asserted-by":"crossref","unstructured":"Nash, P. D., Opas, M. and Michalak, M. (1994). Calreticulin: not just another calcium-binding protein. Mol. Cell. Biochem.135,71-78.","DOI":"10.1007\/BF00925962"},{"key":"2021042504581432800_REF33","doi-asserted-by":"crossref","unstructured":"Nielsen, H., Engelbrecht, J., Brunak, S. and von Heijne, G.(1997). Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites. Protein Eng.10,1-6.","DOI":"10.1093\/protein\/10.1.1"},{"key":"2021042504581432800_REF34","unstructured":"Nuttall, P. A., Paesen, G. C., Lawrie, C. H. and Wang, H.(2000). Vector-host interactions in disease transmission. J. Mol. Microbiol. Biotechnol.2, 381-386."},{"key":"2021042504581432800_REF35","doi-asserted-by":"crossref","unstructured":"Nyberg, F., Sanderson, K. and Glamsta, E. L.(1997). The hemorphins: a new class of opioid peptides derived from the blood protein hemoglobin. Biopolymers43,147-156.","DOI":"10.1002\/(SICI)1097-0282(1997)43:2<147::AID-BIP8>3.0.CO;2-V"},{"key":"2021042504581432800_REF36","doi-asserted-by":"crossref","unstructured":"Ogata, S., Hayashi, Y., Misumi, Y. and Ikehara, Y.(1990). Membrane-anchoring domain of rat liver 5\u2032-nucleotidase: identification of the COOH-terminal serine-523 covalently attached with a glycolipid. Biochemistry29,7923-7927.","DOI":"10.1021\/bi00486a021"},{"key":"2021042504581432800_REF37","doi-asserted-by":"crossref","unstructured":"Pitt-Rivers, R. and Impiombato, F. S. A.(1968). The binding of sodium dodecyl sulphate to various proteins. Biochem. J.109,825-830.","DOI":"10.1042\/bj1090825"},{"key":"2021042504581432800_REF38","doi-asserted-by":"crossref","unstructured":"Petersen, L. C., Bjorn, S. E., Olsen, O. H., Nordfang, O.,Norris, F. and Norris, K. (1996). Inhibitory properties of separate recombinant Kunitz-type-protease-inhibitor domains from tissue-factor-pathway inhibitor. Eur. J. Biochem.235,310-316.","DOI":"10.1111\/j.1432-1033.1996.0310f.x"},{"key":"2021042504581432800_REF39","unstructured":"Regoli, D. A. and Barabe, J. (1980). Pharmacology of bradykinin and related kinins. Pharmacol. Rev.32,1-46."},{"key":"2021042504581432800_REF40","doi-asserted-by":"crossref","unstructured":"Ribeiro, J. M. and Mather, T. N. (1998). Ixodes scapularis: salivary kininase activity is a metallo dipeptidyl carboxypeptidase. Exp. Parasitol.89,213-221.","DOI":"10.1006\/expr.1998.4296"},{"key":"2021042504581432800_REF41","doi-asserted-by":"crossref","unstructured":"Ribeiro, J. M. C. (1987). Ixodes dammini: Salivary anticomplement activity. Exp. Parasitol.64,347-353.","DOI":"10.1016\/0014-4894(87)90046-4"},{"key":"2021042504581432800_REF42","doi-asserted-by":"crossref","unstructured":"Ribeiro, J. M. C. (1989). Role of saliva in tick\/host associations. Exp. Appl. Acarol.7, 15-20.","DOI":"10.1007\/BF01200449"},{"key":"2021042504581432800_REF43","unstructured":"Ribeiro, J. M. C. (1995). Blood-feeding arthropods: Live syringes or invertebrate pharmacologists? Infect. Agents Dis.4,143-152."},{"key":"2021042504581432800_REF44","doi-asserted-by":"crossref","unstructured":"Ribeiro, J. M. C., Evans, P. M., MacSwain, J. L. and Sauer,J. (1992). Amblyomma americanum: Characterization of salivary prostaglandins E2 and F2alpha by RP-HPLC\/bioassay and gas chromatography-mass spectrometry. Exp. Parasitol.74,112-116.","DOI":"10.1016\/0014-4894(92)90145-Z"},{"key":"2021042504581432800_REF45","doi-asserted-by":"crossref","unstructured":"Ribeiro, J. M. C., Makoul, G., Levine, J., Robinson, D. and Spielman, A. (1985). Antihemostatic, antiinflammatory and immunosuppressive properties of the saliva of a tick, Ixodes dammini.J. Exp. Med.161,332-344.","DOI":"10.1084\/jem.161.2.332"},{"key":"2021042504581432800_REF46","doi-asserted-by":"crossref","unstructured":"Ribeiro, J. M. C., Makoul, G. and Robinson, D.(1988). Ixodes dammini: Evidence for salivary prostacyclin secretion. J. Parasitol.74,1068-1069.","DOI":"10.2307\/3282240"},{"key":"2021042504581432800_REF47","doi-asserted-by":"crossref","unstructured":"Ribeiro, J. M. C. and Spielman, A. (1986). Ixodes dammini: Salivary anaphylatoxin-inactivating activity. Exp. Parasitol.62,292-297.","DOI":"10.1016\/0014-4894(86)90034-2"},{"key":"2021042504581432800_REF48","doi-asserted-by":"crossref","unstructured":"Ribeiro, J. M. C., Weis, J. J. and Telford, S. R., III.(1990). Saliva of the tick Ixodes dammini inhibits neutrophil function. Exp. Parasitol.70,382-388.","DOI":"10.1016\/0014-4894(90)90121-R"},{"key":"2021042504581432800_REF49","doi-asserted-by":"crossref","unstructured":"Roberts, D. D. (1996). Regulation of tumor growth and metastasis by thrombospondin-1. FASEB J.10,1183-1191.","DOI":"10.1096\/fasebj.10.10.8751720"},{"key":"2021042504581432800_REF50","doi-asserted-by":"crossref","unstructured":"Schultz, J., Copley, R. R., Doerks, T., Ponting, C. P. and Bork,P. (2000). SMART: a web-based tool for the study of genetically mobile domains. Nucleic Acids Res.28,231-234.","DOI":"10.1093\/nar\/28.1.231"},{"key":"2021042504581432800_REF51","doi-asserted-by":"crossref","unstructured":"Tortorella, M. D., Pratta, M. A., Fox, J. W. and Arner, E. C. (1998). The interglobular domain of cartilage aggrecan is cleaved by hemorrhagic metalloproteinase HT-d (atrolysin C) at the matrix metalloproteinase and aggrecanase sites. J. Biol. Chem.273,5846-5850.","DOI":"10.1074\/jbc.273.10.5846"},{"key":"2021042504581432800_REF52","doi-asserted-by":"crossref","unstructured":"Valenzuela, J. G., Belkaid, Y., Garfield, M. K., Mendez, S.,Kamhawi, S., Rowton, E. D., Sacks, D. L. and Ribeiro, J. M.(2001). Toward a defined anti-Leishmania vaccine targeting vector antigens: characterization of a protective salivary protein. J. Exp. Med.194,331-342.","DOI":"10.1084\/jem.194.3.331"},{"key":"2021042504581432800_REF53","doi-asserted-by":"crossref","unstructured":"Valenzuela, J. G., Charlab, R., Mather, T. N. and Ribeiro, J. M. (2000). Purification, cloning, and expression of a novel salivary anticomplement protein from the tick, Ixodes scapularis.J. Biol. Chem.275,18717-18723.","DOI":"10.1074\/jbc.M001486200"},{"key":"2021042504581432800_REF54","doi-asserted-by":"crossref","unstructured":"Valenzuela, J. G., Pham, V. M., Garfield, M. K., Francischetti,I. M. and Ribeiro, J. M. C. (2002). Toward a description of the sialome of the adult female mosquito Aedes aegypti.Insect Biochem. Mol. Biol., in press.","DOI":"10.1016\/S0965-1748(02)00047-4"},{"key":"2021042504581432800_REF55","doi-asserted-by":"crossref","unstructured":"Wang, H. and Nuttall, P. A. (1995a). Immunoglobulin G binding proteins in male Rhipicephalus appendiculatus ticks. Parasite Immunol.17,517-524.","DOI":"10.1111\/j.1365-3024.1995.tb00882.x"},{"key":"2021042504581432800_REF56","doi-asserted-by":"crossref","unstructured":"Wang, H. and Nuttall, P. A. (1995b). Immunoglobulin-G binding proteins in the ixodid ticks, Rhipicephalus appendiculatus, Amblyomma variegatum and Ixodes hexagonus.Parasitology111,161-165.","DOI":"10.1017\/S0031182000064908"},{"key":"2021042504581432800_REF57","doi-asserted-by":"crossref","unstructured":"Wang, H. and Nuttall, P. A. (1999). Immunoglobulin-binding proteins in ticks: new target for vaccine development against a blood-feeding parasite. Cell. Mol. Life Sci.56,286-295.","DOI":"10.1007\/s000180050430"},{"key":"2021042504581432800_REF58","doi-asserted-by":"crossref","unstructured":"Wang, H., Kaufman, W. R. and Nuttall, P. A.(1999). Molecular individuality: polumorphism of salivary gland proteins in three species of ixodid tick. Exp. Appl. Acarol.23,969-975.","DOI":"10.1023\/A:1006362929841"},{"key":"2021042504581432800_REF59","doi-asserted-by":"crossref","unstructured":"Wikel, S., Ramachandra, R. N. and Bergman, D. K.(1994). Tick-induced modulation of the host immune response. Int. J. Parasitol.24,59-66.","DOI":"10.1016\/0020-7519(94)90059-0"},{"key":"2021042504581432800_REF60","doi-asserted-by":"crossref","unstructured":"Wikel, S. K. (1996). Host immunity to ticks. Ann. Rev. Entomol.41,1-22.","DOI":"10.1146\/annurev.en.41.010196.000245"}],"container-title":["Journal of Experimental Biology"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/journals.biologists.com\/jeb\/article-pdf\/205\/18\/2843\/1242791\/2843.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"http:\/\/journals.biologists.com\/jeb\/article-pdf\/205\/18\/2843\/1242791\/2843.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,4,25]],"date-time":"2021-04-25T05:03:21Z","timestamp":1619327001000},"score":1,"resource":{"primary":{"URL":"https:\/\/journals.biologists.com\/jeb\/article\/205\/18\/2843\/9088\/Exploring-the-sialome-of-the-tick-Ixodes"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2002,9,15]]},"references-count":60,"journal-issue":{"issue":"18","published-print":{"date-parts":[[2002,9,15]]}},"URL":"https:\/\/doi.org\/10.1242\/jeb.205.18.2843","relation":{},"ISSN":["1477-9145","0022-0949"],"issn-type":[{"value":"1477-9145","type":"electronic"},{"value":"0022-0949","type":"print"}],"subject":[],"published":{"date-parts":[[2002,9,15]]}}}