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Volumn 4, Issue AUG, 2014, Pages

Immunity-related genes in Ixodes scapularis-perspectives from genome information

Author keywords

Borrelia burgdorferi; Genomics; Immunity related genes; Innate response; Ixodes scapularis; Ticks

Indexed keywords

LEUCINE RICH REPEAT KINASE 2; PEPTIDOGLYCAN RECOGNITION PROTEIN; POLYPEPTIDE ANTIBIOTIC AGENT; PROTEINASE; STAT PROTEIN; SUPEROXIDE DISMUTASE; ANTIMICROBIAL CATIONIC PEPTIDE; REACTIVE OXYGEN METABOLITE;

EID: 84925883866     PISSN: None     EISSN: 22352988     Source Type: Journal    
DOI: 10.3389/fcimb.2014.00116     Document Type: Article
Times cited : (64)

References (135)
  • 1
    • 0028960959 scopus 로고
    • Properties of a blood-mealinduced midgut lectin from the tsetse fly Glossina morsitans
    • doi: 10.1007/BF00931529
    • Abubakar, L., Osir, E. O., and Imbuga, M. O. (1995). Properties of a blood-mealinduced midgut lectin from the tsetse fly Glossina morsitans. Parasitol. Res. 81, 271-275. doi: 10.1007/BF00931529.
    • (1995) Parasitol. Res. , vol.81 , pp. 271-275
    • Abubakar, L.1    Osir, E.O.2    Imbuga, M.O.3
  • 2
    • 33645068436 scopus 로고    scopus 로고
    • Molecular characterization of a tsetse fly midgut proteolytic lectin that mediates differentiation of African trypanosomes
    • doi: 10.1016/j.ibmb.2006.01.010
    • Abubakar, L. U., Bulimo, W. D., Mulaa, F. J., and Osir, E. O. (2006). Molecular characterization of a tsetse fly midgut proteolytic lectin that mediates differentiation of African trypanosomes. Insect Biochem. Mol. Biol. 36, 344-352. doi: 10.1016/j.ibmb.2006.01.010.
    • (2006) Insect Biochem. Mol. Biol. , vol.36 , pp. 344-352
    • Abubakar, L.U.1    Bulimo, W.D.2    Mulaa, F.J.3    Osir, E.O.4
  • 3
    • 0025815472 scopus 로고
    • Epizootiology of Lyme borreliosis
    • Anderson, J. (1991). Epizootiology of Lyme borreliosis. Scan. J. Infect. Dis. Suppl. 77, 23-24.
    • (1991) Scan. J. Infect. Dis. Suppl. , vol.77 , pp. 23-24
    • Anderson, J.1
  • 4
    • 77954623743 scopus 로고    scopus 로고
    • Dual oxidase in mucosal immunity and host-microbe homeostasis
    • doi: 10.1016/j.it.2010.05.003
    • Bae, Y. S., Choi, M. K., and Lee, W. J. (2010). Dual oxidase in mucosal immunity and host-microbe homeostasis. Trends Immunol. 31, 278-287. doi: 10.1016/j.it.2010.05.003.
    • (2010) Trends Immunol. , vol.31 , pp. 278-287
    • Bae, Y.S.1    Choi, M.K.2    Lee, W.J.3
  • 5
    • 0029593345 scopus 로고
    • Plasmodium gallinaceum: sporozoite invasion of Aedes aegypti salivary glands is inhibited by anti-gland antibodies and by lectins
    • doi: 10.1006/expr.1995.1124
    • Barreau, C., Touray, M., Pimenta, P. F., Miller, L. H., and Vernick, K. D. (1995). Plasmodium gallinaceum: sporozoite invasion of Aedes aegypti salivary glands is inhibited by anti-gland antibodies and by lectins. Exp. Parasitol. 81, 332-343. doi: 10.1006/expr.1995.1124.
    • (1995) Exp. Parasitol. , vol.81 , pp. 332-343
    • Barreau, C.1    Touray, M.2    Pimenta, P.F.3    Miller, L.H.4    Vernick, K.D.5
  • 6
    • 78049297909 scopus 로고    scopus 로고
    • A heterodimeric complex of the LRR proteins LRIM1 and APL1C regulates complement-like immunity in Anopheles gambiae
    • doi: 10.1073/pnas.10105 75107
    • Baxter, R. H., Steinert, S., Chelliah, Y., Volohonsky, G., Levashina, E. A., and Deisenhofer, J. (2010). A heterodimeric complex of the LRR proteins LRIM1 and APL1C regulates complement-like immunity in Anopheles gambiae. Proc. Natl. Acad. Sci. U.S.A. 107, 16817-16822. doi: 10.1073/pnas.10105 75107.
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 16817-16822
    • Baxter, R.H.1    Steinert, S.2    Chelliah, Y.3    Volohonsky, G.4    Levashina, E.A.5    Deisenhofer, J.6
  • 7
    • 0141559415 scopus 로고    scopus 로고
    • Leucine-rich repeats and pathogen recognition in Toll-like receptors
    • doi: 10.1016/S1471-4906(03)00242-4
    • Bell, J. K., Mullen, G. E., Leifer, C. A., Mazzoni, A., Davies, D. R., and Segal, D. M. (2003). Leucine-rich repeats and pathogen recognition in Toll-like receptors. Trends Immunol. 24, 528-533. doi: 10.1016/S1471-4906(03)00242-4.
    • (2003) Trends Immunol. , vol.24 , pp. 528-533
    • Bell, J.K.1    Mullen, G.E.2    Leifer, C.A.3    Mazzoni, A.4    Davies, D.R.5    Segal, D.M.6
  • 8
    • 0029730738 scopus 로고    scopus 로고
    • A conserved signaling pathway: the Drosophila toll-dorsal pathway
    • doi: 10.1146/annurev.cellbi o.12.1.393
    • Belvin, M. P., and Anderson, K. V. (1996). A conserved signaling pathway: the Drosophila toll-dorsal pathway. Annu. Rev. Cell Dev. Biol. 12, 393-416. doi: 10.1146/annurev.cellbi o.12.1.393.
    • (1996) Annu. Rev. Cell Dev. Biol. , vol.12 , pp. 393-416
    • Belvin, M.P.1    Anderson, K.V.2
  • 9
    • 14744299030 scopus 로고    scopus 로고
    • Regulation of innate immunity by Rho GTPases
    • doi: 10.1016/j.tcb.2005.01.002
    • Bokoch, G. M. (2005). Regulation of innate immunity by Rho GTPases. Trends Cell Biol. 15, 163-171. doi: 10.1016/j.tcb.2005.01.002.
    • (2005) Trends Cell Biol. , vol.15 , pp. 163-171
    • Bokoch, G.M.1
  • 10
    • 0001564983 scopus 로고
    • Cell-free immunity in insects
    • doi: 10.1146/annurev.mi.41.100187.000535
    • Boman, H. G., and Hultmark, D. (1981). Cell-free immunity in insects. Trends Biochem. Sci. 6, 3. doi: 10.1146/annurev.mi.41.100187.000535.
    • (1981) Trends Biochem. Sci. , vol.6 , pp. 3
    • Boman, H.G.1    Hultmark, D.2
  • 11
    • 33750471197 scopus 로고    scopus 로고
    • Mutual cross-talk between reactive oxygen species and nuclear factor-kappa B: molecular basis and biological significance
    • doi: 10.1038/sj.onc. 1209936
    • Bubici, C., Papa, S., Dean, K., and Franzoso, G. (2006). Mutual cross-talk between reactive oxygen species and nuclear factor-kappa B: molecular basis and biological significance. Oncogene 25, 6731-6748. doi: 10.1038/sj.onc. 1209936.
    • (2006) Oncogene , vol.25 , pp. 6731-6748
    • Bubici, C.1    Papa, S.2    Dean, K.3    Franzoso, G.4
  • 12
    • 84882709450 scopus 로고    scopus 로고
    • Gut homeostasis in a microbial world: insights from Drosophila melanogaster
    • doi: 10.1038/nrmicro3074
    • Buchon, N., Broderick, N. A., and Lemaitre, B. (2013). Gut homeostasis in a microbial world: insights from Drosophila melanogaster. Nat. Rev. Microbiol. 11, 615-626. doi: 10.1038/nrmicro3074.
    • (2013) Nat. Rev. Microbiol. , vol.11 , pp. 615-626
    • Buchon, N.1    Broderick, N.A.2    Lemaitre, B.3
  • 13
    • 60649091298 scopus 로고    scopus 로고
    • Drosophila intestinal response to bacterial infection: activation of host defense and stem cell proliferation
    • doi: 10.1016/j.chom.2009.01.003
    • Buchon, N., Broderick, N. A., Poidevin, M., Pradervand, S., and Lemaitre, B. (2009). Drosophila intestinal response to bacterial infection: activation of host defense and stem cell proliferation. Cell Host Microbe 5, 200-211. doi: 10.1016/j.chom.2009.01.003.
    • (2009) Cell Host Microbe , vol.5 , pp. 200-211
    • Buchon, N.1    Broderick, N.A.2    Poidevin, M.3    Pradervand, S.4    Lemaitre, B.5
  • 14
    • 0033022730 scopus 로고    scopus 로고
    • Antimicrobial peptides in insects; structure and function
    • doi: 10.1016/S0145-305X(99)00015-4
    • Bulet, P., Hetru, C., Dimarcq, J. L., and Hoffmann, D. (1999). Antimicrobial peptides in insects; structure and function. Dev. Comp. Immunol. 23, 329-344. doi: 10.1016/S0145-305X(99)00015-4.
    • (1999) Dev. Comp. Immunol. , vol.23 , pp. 329-344
    • Bulet, P.1    Hetru, C.2    Dimarcq, J.L.3    Hoffmann, D.4
  • 16
    • 80054052509 scopus 로고    scopus 로고
    • Metagenomic profile of the bacterial communities associated with Ixodes ricinus ticks
    • doi: 10.1371/journal.pone.0025604.
    • Carpi, G., Cagnacci, F., Wittekindt, N. E., Zhao, F., Qi, J., Tomsho, L. P., et al. (2011). Metagenomic profile of the bacterial communities associated with Ixodes ricinus ticks. PLoS ONE 6:e25604. doi: 10.1371/journal.pone.0025604.
    • (2011) PLoS ONE , vol.6
    • Carpi, G.1    Cagnacci, F.2    Wittekindt, N.E.3    Zhao, F.4    Qi, J.5    Tomsho, L.P.6
  • 17
    • 78751512204 scopus 로고    scopus 로고
    • A tick salivary protein targets cathepsin G and chymase and inhibits host inflammation and platelet aggregation
    • doi: 10.1182/blood-2010-06-293241
    • Chmelar, J., Oliveira, C. J., Rezacova, P., Francischetti, I. M., Kovarova, Z., Pejler, G., et al. (2011). A tick salivary protein targets cathepsin G and chymase and inhibits host inflammation and platelet aggregation. Blood 117, 736-744. doi: 10.1182/blood-2010-06-293241.
    • (2011) Blood , vol.117 , pp. 736-744
    • Chmelar, J.1    Oliveira, C.J.2    Rezacova, P.3    Francischetti, I.M.4    Kovarova, Z.5    Pejler, G.6
  • 18
    • 0037020201 scopus 로고    scopus 로고
    • Immunity-related genes and gene families in Anopheles gambiae.
    • doi: 10.1126/science.1077136.
    • Christophides, G. K., Zdobnov, E., Barillas-Mury, C., Birney, E., Blandin, S., Blass, C., et al. (2002). Immunity-related genes and gene families in Anopheles gambiae. Science298, 159-165. doi: 10.1126/science.1077136.
    • (2002) Science , vol.298 , pp. 159-165
    • Christophides, G.K.1    Zdobnov, E.2    Barillas-Mury, C.3    Birney, E.4    Blandin, S.5    Blass, C.6
  • 19
    • 52649155001 scopus 로고    scopus 로고
    • Microbial communities and interactions in the lone star tick, Amblyomma americanum
    • doi: 10.1111/j.1365-294X.2008. 03914.x
    • Clay, K., Klyachko, O., Grindle, N., Civitello, D., Oleske, D., and Fuqua, C. (2008). Microbial communities and interactions in the lone star tick, Amblyomma americanum. Mol. Ecol. 17, 4371-4381. doi: 10.1111/j.1365-294X.2008. 03914.x.
    • (2008) Mol. Ecol. , vol.17 , pp. 4371-4381
    • Clay, K.1    Klyachko, O.2    Grindle, N.3    Civitello, D.4    Oleske, D.5    Fuqua, C.6
  • 20
    • 84940249780 scopus 로고    scopus 로고
    • "The coagulation cascade and its regulation
    • J. X. J. Yuan, C. A. Hales, S. L. Archer, J. G. N. Garcia, S. Rich, and J. B. West (New York, NY: Springer)
    • Crawley, J., Gonzalez-Porras, J. R., and Lane, D. A. (2011). "The coagulation cascade and its regulation," in Textbook of Pulmonary Vascular Disease, eds J. X. J. Yuan, C. A. Hales, S. L. Archer, J. G. N. Garcia, S. Rich, and J. B. West (New York, NY: Springer), 357-370.
    • (2011) Textbook of Pulmonary Vascular Disease , pp. 357-370
    • Crawley, J.1    Gonzalez-Porras, J.R.2    Lane, D.A.3
  • 21
    • 79251473364 scopus 로고    scopus 로고
    • Tick histamine release factor is critical for Ixodes scapularis engorgement and transmission of the lyme disease agent.
    • doi: 10.1371/journal.ppat.1001205.
    • Dai, J., Narasimhan, S., Zhang, L., Liu, L., Wang, P., and Fikrig, E. (2010). Tick histamine release factor is critical for Ixodes scapularis engorgement and transmission of the lyme disease agent. PLoS Pathog. 6:e1001205. doi: 10.1371/journal.ppat.1001205.
    • (2010) PLoS Pathog , vol.6
    • Dai, J.1    Narasimhan, S.2    Zhang, L.3    Liu, L.4    Wang, P.5    Fikrig, E.6
  • 22
    • 77949890193 scopus 로고    scopus 로고
    • Lectins as pattern recognition molecules: the effects of epitope density in innate immunity
    • doi: 10.1093/glycob/cwp186
    • Dam, T. K., and Brewer, C. F. (2010). Lectins as pattern recognition molecules: the effects of epitope density in innate immunity. Glycobiology 20, 270-279. doi: 10.1093/glycob/cwp186.
    • (2010) Glycobiology , vol.20 , pp. 270-279
    • Dam, T.K.1    Brewer, C.F.2
  • 23
    • 0035887953 scopus 로고    scopus 로고
    • Salp25D, an Ixodes scapularis antioxidant, is 1 of 14 immunodominant antigens in engorged tick salivary glands
    • doi: 10.1086/323351
    • Das, S., Banerjee, G., Deponte, K., Marcantonio, N., Kantor, E 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.
    • (2001) J. Infect. Dis. , vol.184 , pp. 1056-1064
    • Das, S.1    Banerjee, G.2    Deponte, K.3    Marcantonio, N.4    Kantor, E.S.5    Fikrig, E.6
  • 24
    • 0033763267 scopus 로고    scopus 로고
    • Nitric oxide signalling in insects
    • doi: 10.1016/S0965-1748(00)00118-1
    • Davies, S. (2000). Nitric oxide signalling in insects. Insect Biochem. Mol. Biol. 30, 1123-1138. doi: 10.1016/S0965-1748(00)00118-1.
    • (2000) Insect Biochem. Mol. Biol. , vol.30 , pp. 1123-1138
    • Davies, S.1
  • 25
    • 0037013856 scopus 로고    scopus 로고
    • The Toll and IMD pathways are the major regulators of the immune response in Drosophila
    • doi: 10.1093/emboj/21.11.2568
    • De Gregorio, E., Spellman, P. T., Tzou, P., Rubin, G. M., and Lemaitre, B. (2002). The Toll and IMD pathways are the major regulators of the immune response in Drosophila. EMBO J. 21, 2568-2579. doi: 10.1093/emboj/21.11.2568.
    • (2002) EMBO J. , vol.21 , pp. 2568-2579
    • De Gregorio, E.1    Spellman, P.T.2    Tzou, P.3    Rubin, G.M.4    Lemaitre, B.5
  • 26
    • 84901036297 scopus 로고    scopus 로고
    • Roles of DUOXmediated hydrogen peroxide in metabolism, host defense, and signaling.
    • doi: 10.1089/ars.2013.5602.
    • Deken, X. D., Corvilain, B., Dumont, J. E., and Miot, F. (2013). Roles of DUOXmediated hydrogen peroxide in metabolism, host defense, and signaling. Antioxid. RedoxSignal. 20, 2776-2793. doi: 10.1089/ars.2013.5602.
    • (2013) Antioxid. RedoxSignal. , vol.20 , pp. 2776-2793
    • Deken, X.D.1    Corvilain, B.2    Dumont, J.E.3    Miot, F.4
  • 27
    • 84894312920 scopus 로고    scopus 로고
    • Ovarian dual oxidase (Duox) activity is essential for insect eggshell hardening and waterproofing
    • doi: 10.1074/jbc.M113.522201
    • Dias, F. A., Gandara, A. C., Queiroz-Barros, F. G., Oliveira, R. L., Sorgine, M. H., Braz, G. R., et al. (2013). Ovarian dual oxidase (Duox) activity is essential for insect eggshell hardening and waterproofing. J. Biol. Chem. 288, 35058-35067. doi: 10.1074/jbc.M113.522201.
    • (2013) J. Biol. Chem. , vol.288 , pp. 35058-35067
    • Dias, F.A.1    Gandara, A.C.2    Queiroz-Barros, F.G.3    Oliveira, R.L.4    Sorgine, M.H.5    Braz, G.R.6
  • 28
    • 1042302949 scopus 로고    scopus 로고
    • The gut bacteria of insects: nonpathogenic interactions
    • doi: 10.1146/annurev.ento.49. 061802.123416
    • Dillon, R. J., and Dillon, V. M. (2004). The gut bacteria of insects: nonpathogenic interactions. Annu. Rev. Entomol. 49, 71-92. doi: 10.1146/annurev.ento.49. 061802.123416.
    • (2004) Annu. Rev. Entomol. , vol.49 , pp. 71-92
    • Dillon, R.J.1    Dillon, V.M.2
  • 29
    • 12944263712 scopus 로고    scopus 로고
    • Anopheles gambiae pilot gene discovery project: identification of mosquito innate immunity genes from expressed sequence tags generated from immune-competent cell lines
    • doi: 10.1073/pnas.97.12.6619
    • Dimopoulos, G., Casavant, T. L., Chang, S., Scheetz, T., Roberts, C., Donohue, M., et al. (2000). Anopheles gambiae pilot gene discovery project: identification of mosquito innate immunity genes from expressed sequence tags generated from immune-competent cell lines. Proc. Natl. Acad. Sci. U.S.A. 97, 6619-6624. doi: 10.1073/pnas.97.12.6619.
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 6619-6624
    • Dimopoulos, G.1    Casavant, T.L.2    Chang, S.3    Scheetz, T.4    Roberts, C.5    Donohue, M.6
  • 30
    • 0032476592 scopus 로고    scopus 로고
    • Malaria infection of the mosquito Anopheles gambiae activates immune-responsive genes during critical transition stages of the parasite life cycle
    • doi: 10.1093/emboj/17.21.6115
    • Dimopoulos, G., Seeley, D., Wolf, A., and Kafatos, F. C. (1998). Malaria infection of the mosquito Anopheles gambiae activates immune-responsive genes during critical transition stages of the parasite life cycle. EMBO J. 17, 6115-6123. doi: 10.1093/emboj/17.21.6115.
    • (1998) EMBO J. , vol.17 , pp. 6115-6123
    • Dimopoulos, G.1    Seeley, D.2    Wolf, A.3    Kafatos, F.C.4
  • 31
    • 33745684283 scopus 로고    scopus 로고
    • Anopheles gambiae immune responses to human and rodent Plasmodium parasite species.
    • doi: 10.1371/journal.ppat.0020052.
    • Dong, Y., Aguilar, R., Xi, Z., Warr, E., Mongin, E., and Dimopoulos, G. (2006). Anopheles gambiae immune responses to human and rodent Plasmodium parasite species. PLoS Pathog. 2:e52. doi: 10.1371/journal.ppat.0020052.
    • (2006) PLoS Pathog. , vol.2
    • Dong, Y.1    Aguilar, R.2    Xi, Z.3    Warr, E.4    Mongin, E.5    Dimopoulos, G.6
  • 32
    • 0035921417 scopus 로고    scopus 로고
    • Tyrosine cross-linking of extracellular matrix is catalyzed by Duox, a multidomain oxidase/peroxidase with homology to the phagocyte oxidase subunitgp91phox.J
    • doi: 10.1083/jcb.200103132
    • Edens, W A., Sharling, L., Cheng, G., Shapira, R., Kinkade, J. M., Lee, T., et al. (2001). Tyrosine cross-linking of extracellular matrix is catalyzed by Duox, a multidomain oxidase/peroxidase with homology to the phagocyte oxidase subunitgp91phox.J. Cell Biol. 154, 879-891. doi: 10.1083/jcb.200103132.
    • (2001) Cell Biol. , vol.154 , pp. 879-891
    • Edens, W.A.1    Sharling, L.2    Cheng, G.3    Shapira, R.4    Kinkade, J.M.5    Lee, T.6
  • 33
    • 0034729655 scopus 로고    scopus 로고
    • Interactions between the cellular and humoral immune responses in Drosophila
    • doi: 10.1016/S0960-9822(00)00569-8
    • Elrod-Erickson, M., Mishra, S., and Schneider, D. (2000). Interactions between the cellular and humoral immune responses in Drosophila. Curr. Biol. 10, 781-784. doi: 10.1016/S0960-9822(00)00569-8.
    • (2000) Curr. Biol. , vol.10 , pp. 781-784
    • Elrod-Erickson, M.1    Mishra, S.2    Schneider, D.3
  • 34
    • 1042291215 scopus 로고    scopus 로고
    • Structural principles of leucine-rich repeat (LRR) proteins
    • doi: 10.1002/prot. 10605
    • Enkhbayar, P., Kamiya, M., Osaki, M., Matsumoto, T., and Matsushima, N. (2004). Structural principles of leucine-rich repeat (LRR) proteins. Proteins 54, 394-403. doi: 10.1002/prot. 10605.
    • (2004) Proteins , vol.54 , pp. 394-403
    • Enkhbayar, P.1    Kamiya, M.2    Osaki, M.3    Matsumoto, T.4    Matsushima, N.5
  • 35
    • 0037069690 scopus 로고    scopus 로고
    • Rho GTPases in cell biology
    • doi: 10.1038/nature01148
    • Etienne-Manneville, S., and Hall, A. (2002). Rho GTPases in cell biology. Nature 420, 629-635. doi: 10.1038/nature01148.
    • (2002) Nature , vol.420 , pp. 629-635
    • Etienne-Manneville, S.1    Hall, A.2
  • 36
    • 35549006674 scopus 로고    scopus 로고
    • The Drosophila systemic immune response: sensing and signalling during bacterial and fungal infections
    • doi: 10.1038/nri2194
    • Ferrandon, D., Imler, J. L., Hetru, C., and Hoffmann, J. A. (2007). The Drosophila systemic immune response: sensing and signalling during bacterial and fungal infections. Nat. Rev. Immunol. 7, 862-874. doi: 10.1038/nri2194.
    • (2007) Nat. Rev. Immunol. , vol.7 , pp. 862-874
    • Ferrandon, D.1    Imler, J.L.2    Hetru, C.3    Hoffmann, J.A.4
  • 37
    • 61849177493 scopus 로고    scopus 로고
    • Two mosquito LRR proteins function as complement control factors in the TEP1-mediated killing of Plasmodium
    • doi: 10.1016/j.chom.2009.01.005
    • Fraiture, M., Baxter, R. H., Steinert, S., Chelliah, Y., Frolet, C., Quispe-Tintaya, W., et al. (2009). Two mosquito LRR proteins function as complement control factors in the TEP1-mediated killing of Plasmodium. Cell Host Microbe 5, 273-284. doi: 10.1016/j.chom.2009.01.005.
    • (2009) Cell Host Microbe , vol.5 , pp. 273-284
    • Fraiture, M.1    Baxter, R.H.2    Steinert, S.3    Chelliah, Y.4    Frolet, C.5    Quispe-Tintaya, W.6
  • 38
    • 0031470826 scopus 로고    scopus 로고
    • Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi
    • doi: 10.1038/37551
    • Fraser, C. M., Casjens, S., Huang, W. M., Sutton, G. G., Clayton, R., Lathigra, R., et al. (1997). Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi. Nature 390, 580-586. doi: 10.1038/37551.
    • (1997) Nature , vol.390 , pp. 580-586
    • Fraser, C.M.1    Casjens, S.2    Huang, W.M.3    Sutton, G.G.4    Clayton, R.5    Lathigra, R.6
  • 39
    • 0036584407 scopus 로고    scopus 로고
    • Evolution of the lectin-complement pathway and its role in innate immunity
    • doi: 10.1038/nri800
    • Fujita, T. (2002). Evolution of the lectin-complement pathway and its role in innate immunity. Nat. Rev. Immunol. 2, 346-353. doi: 10.1038/nri800.
    • (2002) Nat. Rev. Immunol. , vol.2 , pp. 346-353
    • Fujita, T.1
  • 40
    • 10644262971 scopus 로고    scopus 로고
    • The Nox family of NAD(P)H oxidases: host defense and beyond
    • doi: 10.1074/jbc.R400024200
    • Geiszt, M., and Leto, T. L. (2004). The Nox family of NAD(P)H oxidases: host defense and beyond. J. Biol. Chem. 279, 51715-51718. doi: 10.1074/jbc.R400024200.
    • (2004) J. Biol. Chem. , vol.279 , pp. 51715-51718
    • Geiszt, M.1    Leto, T.L.2
  • 41
    • 0035313541 scopus 로고    scopus 로고
    • Identification of an IL-2 binding protein in the saliva of the Lyme disease vector tick, Ixodes scapularis
    • doi: 10.4049/jimmunol.166.7.4319
    • 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.
    • (2001) J. Immunol. , vol.166 , pp. 4319-4326
    • Gillespie, R.D.1    Dolan, M.C.2    Piesman, J.3    Titus, R.G.4
  • 42
    • 0035118609 scopus 로고    scopus 로고
    • Serine proteases as mediators of mosquito immune responses
    • doi: 10.1016/S0965-1748(00)00145-4
    • Gorman, M. J., and Paskewitz, S. M. (2001). Serine proteases as mediators of mosquito immune responses. Insect Biochem. Mol. Biol. 31, 257-262. doi: 10.1016/S0965-1748(00)00145-4.
    • (2001) Insect Biochem. Mol. Biol. , vol.31 , pp. 257-262
    • Gorman, M.J.1    Paskewitz, S.M.2
  • 43
    • 19344365944 scopus 로고    scopus 로고
    • Innate immunity in fruit flies: a textbook example of genomic recycling
    • doi: 10.1371/journal. pbio.0020276.
    • Govind, S., and Nehm, R. H. (2004). Innate immunity in fruit flies: a textbook example of genomic recycling. PLoS Biol. 2:E276. doi: 10.1371/journal. pbio.0020276.
    • (2004) PLoS Biol , vol.2
    • Govind, S.1    Nehm, R.H.2
  • 45
    • 0031219599 scopus 로고    scopus 로고
    • Lectins (hemagglutinins) in the gut of the important disease vectors
    • Grubhoffer, L., Hypsa, V., and Volf, P. (1997). Lectins (hemagglutinins) in the gut of the important disease vectors. Parasite 4, 203-216.
    • (1997) Parasite , vol.4 , pp. 203-216
    • Grubhoffer, L.1    Hypsa, V.2    Volf, P.3
  • 46
    • 0031890488 scopus 로고    scopus 로고
    • Lectins and tick-pathogen interactions: a minireview
    • Grubhoffer, L., and Jindrak, L. (1998). Lectins and tick-pathogen interactions: a minireview. Folia Parasitol. (Praha) 45, 9-13.
    • (1998) Folia Parasitol. (Praha) , vol.45 , pp. 9-13
    • Grubhoffer, L.1    Jindrak, L.2
  • 47
    • 20344386959 scopus 로고    scopus 로고
    • Tick lectins: structural and functional properties
    • doi: 10.1017/S0031182004004858
    • Grubhoffer, L., Kovar, V., and Rudenko, N. (2004). Tick lectins: structural and functional properties. Parasitology 129(Suppl.), S113-S125. doi: 10.1017/S0031182004004858.
    • (2004) Parasitology , vol.129 , Issue.SUPPL
    • Grubhoffer, L.1    Kovar, V.2    Rudenko, N.3
  • 48
    • 84873566911 scopus 로고    scopus 로고
    • The roles of serpins in mosquito immunology and physiology
    • doi: 10.1016/j.jinsphys.2012.08.015
    • Gulley, M. M., Zhang, X., and Michel, K. (2013). The roles of serpins in mosquito immunology and physiology. J. Insect Physiol. 59, 138-147. doi: 10.1016/j.jinsphys.2012.08.015.
    • (2013) J. Insect Physiol. , vol.59 , pp. 138-147
    • Gulley, M.M.1    Zhang, X.2    Michel, K.3
  • 49
    • 65549140168 scopus 로고    scopus 로고
    • The STAT pathway mediates late-phase immunity against Plasmodium in the mosquito Anopheles gambiae
    • doi: 10.1016/j.chom.2009.04.003
    • Gupta, L., Molina-Cruz, A., Kumar, S., Rodrigues, J., Dixit, R., Zamora, R. E., et al. (2009). The STAT pathway mediates late-phase immunity against Plasmodium in the mosquito Anopheles gambiae. Cell Host Microbe 5, 498-507. doi: 10.1016/j.chom.2009.04.003.
    • (2009) Cell Host Microbe , vol.5 , pp. 498-507
    • Gupta, L.1    Molina-Cruz, A.2    Kumar, S.3    Rodrigues, J.4    Dixit, R.5    Zamora, R.E.6
  • 51
    • 0038010577 scopus 로고    scopus 로고
    • Drosophila melanogaster antimicrobial defense
    • doi: 10.1086/ 374758
    • Hetru, C., Troxler, L., and Hoffmann, J. A. (2003). Drosophila melanogaster antimicrobial defense. J. Infect. Dis. 187(Suppl. 2), S327-S334. doi: 10.1086/ 374758.
    • (2003) J. Infect. Dis. , vol.187 , Issue.SUPPL. 2
    • Hetru, C.1    Troxler, L.2    Hoffmann, J.A.3
  • 52
    • 15044342339 scopus 로고    scopus 로고
    • The Ixodes scapularis Genome Project: an opportunity for advancing tick research
    • doi: 10.1016/j.pt.2005.02.004
    • Hill, C. A., and Wikel, S. K. (2005). The Ixodes scapularis Genome Project: an opportunity for advancing tick research. Trends Parasitol. 21, 151-153. doi: 10.1016/j.pt.2005.02.004.
    • (2005) Trends Parasitol. , vol.21 , pp. 151-153
    • Hill, C.A.1    Wikel, S.K.2
  • 53
    • 0033591428 scopus 로고    scopus 로고
    • Phylogenetic perspectives in innate immunity
    • doi: 10.1126/science.284.5418.1313
    • Hoffmann, J. A., Kafatos, E C., Janeway, C. A., and Ezekowitz, R. A. (1999). Phylogenetic perspectives in innate immunity. Science 284, 1313-1318. doi: 10.1126/science.284.5418.1313.
    • (1999) Science , vol.284 , pp. 1313-1318
    • Hoffmann, J.A.1    Kafatos, E.C.2    Janeway, C.A.3    Ezekowitz, R.A.4
  • 54
    • 0036167107 scopus 로고    scopus 로고
    • Drosophila innate immunity: an evolutionary perspective
    • doi: 10.1038/ni0202-121
    • Hoffmann, J. A., and Reichhart, J. M. (2002). Drosophila innate immunity: an evolutionary perspective. Nat. Immunol. 3, 121-126. doi: 10.1038/ni0202-121.
    • (2002) Nat. Immunol. , vol.3 , pp. 121-126
    • Hoffmann, J.A.1    Reichhart, J.M.2
  • 55
    • 84861980130 scopus 로고    scopus 로고
    • Interactions between the microbiota and the immune system
    • doi: 10.1126/science.1223490
    • Hooper, L. V., Littman, D. R., and Macpherson, A. J. (2012). Interactions between the microbiota and the immune system. Science 336, 1268-1273. doi: 10.1126/science.1223490.
    • (2012) Science , vol.336 , pp. 1268-1273
    • Hooper, L.V.1    Littman, D.R.2    Macpherson, A.J.3
  • 56
    • 39849098637 scopus 로고    scopus 로고
    • Salivating for knowledge: potential pharmacological agents in tick saliva
    • doi: 10.1371/journal. pmed.0050043.
    • Hovius, J. W., Levi, M., and Fikrig, E. (2008). Salivating for knowledge: potential pharmacological agents in tick saliva. PLoS Med. 5:e43. doi: 10.1371/journal. pmed.0050043.
    • (2008) PLoS Med , vol.5
    • Hovius, J.W.1    Levi, M.2    Fikrig, E.3
  • 57
    • 29144478261 scopus 로고    scopus 로고
    • A defensin-like gene expressed in the black-legged tick, Ixodes scapularis
    • doi: 10.1111/j.1365-2915.2005.00579.x
    • Hynes, W. L., Ceraul, S. M., Todd, S. M., Seguin, K. C., and Sonenshine, D. E. (2005). A defensin-like gene expressed in the black-legged tick, Ixodes scapularis. Med. Vet. Entomol. 19, 339-344. doi: 10.1111/j.1365-2915.2005.00579.x.
    • (2005) Med. Vet. Entomol. , vol.19 , pp. 339-344
    • Hynes, W.L.1    Ceraul, S.M.2    Todd, S.M.3    Seguin, K.C.4    Sonenshine, D.E.5
  • 58
    • 21344463378 scopus 로고    scopus 로고
    • Antimicrobial peptides in Drosophila: structures, activities and gene regulation
    • doi: 10.1159/000086648
    • Imler, J. L., and Bulet, P. (2005). Antimicrobial peptides in Drosophila: structures, activities and gene regulation. Chem. Immunol. Allergy 86, 1-21. doi: 10.1159/000086648.
    • (2005) Chem. Immunol. Allergy , vol.86 , pp. 121
    • Imler, J.L.1    Bulet, P.2
  • 59
    • 0035406485 scopus 로고    scopus 로고
    • Characterization of phagocytic hemocytes in Ornithodoros moubata (Acari: Ixodidae)
    • doi: 10.1603/0022-2585- 38.4.514
    • Inoue, N., Hanada, K., Tsuji, N., Igarashi, I., Nagasawa, H., Mikami, T., et al. (2001). Characterization of phagocytic hemocytes in Ornithodoros moubata (Acari: Ixodidae). J. Med. Entomol. 38, 514-519. doi: 10.1603/0022-2585- 38.4.514.
    • (2001) J. Med. Entomol. , vol.38 , pp. 514-519
    • Inoue, N.1    Hanada, K.2    Tsuji, N.3    Igarashi, I.4    Nagasawa, H.5    Mikami, T.6
  • 61
    • 0242658682 scopus 로고    scopus 로고
    • Blocking malaria parasite invasion of mosquito salivary glands
    • doi: 10.1242/jeb.00616
    • James, A. A. (2003). Blocking malaria parasite invasion of mosquito salivary glands. J. Exp. Biol. 206, 3817-3821. doi: 10.1242/jeb.00616.
    • (2003) J. Exp. Biol. , vol.206 , pp. 3817-3821
    • James, A.A.1
  • 62
    • 0028853663 scopus 로고
    • Role of nitric oxide in parasitic infections
    • James, S. L. (1995). Role of nitric oxide in parasitic infections. Microbiol. Rev. 59, 533-547.
    • (1995) Microbiol. Rev. , vol.59 , pp. 533-547
    • James, S.L.1
  • 63
    • 0036212849 scopus 로고    scopus 로고
    • Innate immune recognition
    • doi: 10.1146/annurev.immunol.20.083001. 084359
    • Janeway, C. A. Jr., and Medzhitov, R. (2002). Innate immune recognition. Annu. Rev. Immunol. 20, 197-216. doi: 10.1146/annurev.immunol.20.083001. 084359.
    • (2002) Annu. Rev. Immunol. , vol.20 , pp. 197-216
    • Janeway Jr., C.A.1    Medzhitov, R.2
  • 64
    • 77956563695 scopus 로고    scopus 로고
    • Pyrosequencing and characterization of immune response genes from the American dog tick, Dermacen tor variabilis (L.)
    • doi: 10.1111/j.1365-2583.2010.01037.x
    • Jaworski, D. C., Zou, Z., Bowen, C. J., Wasala, N. B., Madden, R., Wang, Y., et al. (2010). Pyrosequencing and characterization of immune response genes from the American dog tick, Dermacen tor variabilis (L.). Insect Mol. Biol. 19, 617-630. doi: 10.1111/j.1365-2583.2010.01037.x.
    • (2010) Insect Mol. Biol. , vol.19 , pp. 617-630
    • Jaworski, D.C.1    Zou, Z.2    Bowen, C.J.3    Wasala, N.B.4    Madden, R.5    Wang, Y.6
  • 65
    • 33646495280 scopus 로고    scopus 로고
    • Cell-mediated immunity in arthropods: hematopoiesis, coagulation, melanization and opsonization.
    • doi: 10.1016/j.imbio.2005.10.015.
    • Jiravanichpaisal, P., Lee, B. L., and Soderhall, K. (2006). Cell-mediated immunity in arthropods: hematopoiesis, coagulation, melanization and opsonization. Immunobiology 211,213-236. doi: 10.1016/j.imbio.2005.10.015.
    • (2006) Immunobiology , vol.211 , pp. 213-236
    • Jiravanichpaisal, P.1    Lee, B.L.2    Soderhall, K.3
  • 66
    • 0035228020 scopus 로고    scopus 로고
    • Contrasts in tick innate immune responses to Borrelia burgdorferi challenge: immunotolerance in Ixodes scapularis versus immunocompetence in Dermacentor variabilis (Acari: Ixodidae)
    • doi: 10.1603/0022-2585-38.1.99
    • Johns, R., Ohnishi, J., Broadwater, A., Sonenshine, D. E., De Silva, A. M., and Hynes, W. L. (2001). Contrasts in tick innate immune responses to Borrelia burgdorferi challenge: immunotolerance in Ixodes scapularis versus immunocompetence in Dermacentor variabilis (Acari: Ixodidae). J. Med. Entomol. 38, 99-107. doi: 10.1603/0022-2585-38.1.99.
    • (2001) J. Med. Entomol. , vol.38 , pp. 99-107
    • Johns, R.1    Ohnishi, J.2    Broadwater, A.3    Sonenshine, D.E.4    De Silva, A.M.5    Hynes, W.L.6
  • 67
    • 16844371922 scopus 로고    scopus 로고
    • The global importance of ticks
    • doi: 10.1017/S0031182004005967.
    • Jongejan, F., and Uilenberg, G. (2004). The global importance of ticks. Parasitology 129 (Suppl.),S3-S14. doi: 10.1017/S0031182004005967.
    • (2004) Parasitology , vol.129 , Issue.SUPPL
    • Jongejan, F.1    Uilenberg, G.2
  • 68
    • 0036020351 scopus 로고    scopus 로고
    • Existence of phenol oxidase in the argasid tick Ornithodoros moubata
    • doi: 10.1007/s00436-002-0664-x
    • Kadota, K., Satoh, E., Ochiai, M., Inoue, N., Tsuji, N., Igarashi, I., et al. (2002). Existence of phenol oxidase in the argasid tick Ornithodoros moubata. Parasitol. Res. 88, 781-784. doi: 10.1007/s00436-002-0664-x.
    • (2002) Parasitol. Res. , vol.88 , pp. 781-784
    • Kadota, K.1    Satoh, E.2    Ochiai, M.3    Inoue, N.4    Tsuji, N.5    Igarashi, I.6
  • 69
    • 84876913132 scopus 로고    scopus 로고
    • Role of the gut microbiota in immunity and inflammatory disease
    • doi: 10.1038/nri3430
    • Kamada, N., Seo, S. U., Chen, G. Y., and Nunez, G. (2013). Role of the gut microbiota in immunity and inflammatory disease. Nat. Rev. Immunol. 13, 321-335. doi: 10.1038/nri3430.
    • (2013) Nat. Rev. Immunol. , vol.13 , pp. 321-335
    • Kamada, N.1    Seo, S.U.2    Chen, G.Y.3    Nunez, G.4
  • 70
    • 15944420868 scopus 로고    scopus 로고
    • Bacterial recognition and signalling by the Drosophila IMD pathway
    • doi: 10.1111/j.1462- 5822.2005.00504.x
    • Kaneko, T., and Silverman, N. (2005). Bacterial recognition and signalling by the Drosophila IMD pathway. Cell. Microbiol. 7, 461-469. doi: 10.1111/j.1462- 5822.2005.00504.x.
    • (2005) Cell. Microbiol. , vol.7 , pp. 461-469
    • Kaneko, T.1    Silverman, N.2
  • 71
    • 0032992544 scopus 로고    scopus 로고
    • Serine proteinase inhibitors in arthropod immunity
    • doi: 10.1016/S0145-305X(99) 00012-9
    • Kanost, M. R. (1999). Serine proteinase inhibitors in arthropod immunity. Dev. Comp. Imunol. 23, 291-301. doi: 10.1016/S0145-305X(99) 00012-9.
    • (1999) Dev. Comp. Imunol. , vol.23 , pp. 291-301
    • Kanost, M.R.1
  • 72
    • 84940241235 scopus 로고    scopus 로고
    • Potential role of lectins in ticks: Rhipicephalus appendicula and Rhipicephaluspulchellus
    • Kibuka-Sebitosi, E. (2006). Potential role of lectins in ticks: Rhipicephalus appendicula and Rhipicephaluspulchellus. Syst. Appl. Acarol Publ. 21, 14.
    • (2006) Syst. Appl. Acarol Publ. , vol.21 , pp. 14
    • Kibuka-Sebitosi, E.1
  • 73
    • 84900537629 scopus 로고    scopus 로고
    • Role of DUOX in gut inflammation: lessons from model of gut-microbiota interactions.
    • doi: 10.3389/fcimb.2013.00116.
    • Kim, S. H., and Lee, W. J. (2014). Role of DUOX in gut inflammation: lessons from model of gut-microbiota interactions. Front. Cell. Infect. Microbiol. 3:116. doi: 10.3389/fcimb.2013.00116.
    • (2014) Front. Cell. Infect. Microbiol , vol.3 , pp. 116
    • Kim, S.H.1    Lee, W.J.2
  • 74
    • 0035692811 scopus 로고    scopus 로고
    • The leucine-rich repeat as a protein recognition motif
    • doi: 10.1016/S0959- 440X(01)00266-4
    • Kobe, B., and Kajava, A. V. (2001). The leucine-rich repeat as a protein recognition motif. Curr. Opin. Struct. Biol. 11, 725-732. doi: 10.1016/S0959- 440X(01)00266-4.
    • (2001) Curr. Opin. Struct. Biol. , vol.11 , pp. 725-732
    • Kobe, B.1    Kajava, A.V.2
  • 76
    • 0029882031 scopus 로고    scopus 로고
    • Ultrastructural localization of a sialic acid-specific hemolymph lectin in the hemocytes and other tissues of the hard tick Ixodes ricinus (Acari; Chelicerata)
    • doi: 10.1007/s004360050098
    • Kuhn, K. H., Uhlir, J., and Grubhoffer, L. (1996). Ultrastructural localization of a sialic acid-specific hemolymph lectin in the hemocytes and other tissues of the hard tick Ixodes ricinus (Acari; Chelicerata). Parasitol. Res. 82, 215-221. doi: 10.1007/s004360050098.
    • (1996) Parasitol. Res. , vol.82 , pp. 215-221
    • Kuhn, K.H.1    Uhlir, J.2    Grubhoffer, L.3
  • 77
    • 77950234253 scopus 로고    scopus 로고
    • A peroxidase/dual oxidase system modulates midgut epithelial immunity in Anopheles gambiae
    • doi: 10.1126/science. 1184008
    • Kumar, S., Molina-Cruz, A., Gupta, L., Rodrigues, J., and Barillas-Mury, C. (2010). A peroxidase/dual oxidase system modulates midgut epithelial immunity in Anopheles gambiae. Science 327, 1644-1648. doi: 10.1126/science. 1184008.
    • (2010) Science , vol.327 , pp. 1644-1648
    • Kumar, S.1    Molina-Cruz, A.2    Gupta, L.3    Rodrigues, J.4    Barillas-Mury, C.5
  • 78
    • 84871458941 scopus 로고    scopus 로고
    • Borrelia burgdorferi and tick proteins supporting pathogen persistence in the vector
    • doi: 10.2217/fmb.12.121
    • Kung, F., Anguita, J., and Pal, U. (2013). Borrelia burgdorferi and tick proteins supporting pathogen persistence in the vector. Future Microbiol. 8, 41-56. doi: 10.2217/fmb.12.121.
    • (2013) Future Microbiol. , vol.8 , pp. 41-56
    • Kung, F.1    Anguita, J.2    Pal, U.3
  • 79
    • 79953276805 scopus 로고    scopus 로고
    • Immunology
    • doi: 10.1126/science. 1200486
    • Lazzaro, B. P., and Rolff, J. (2011). Immunology. Danger, microbes, and homeostasis. Science 332, 43-44. doi: 10.1126/science. 1200486 Lemaitre, B. (2004). The road to Toll. Nat. Rev. Immunol. 4, 521-527. doi: 10.1038/nri1390.
    • (2011) Danger, microbes, and homeostasis. Science , vol.332 , pp. 43-44
    • Lazzaro, B.P.1    Rolff, J.2
  • 80
    • 3142691844 scopus 로고    scopus 로고
    • The road to Toll
    • doi: 10.1038/nri1390.
    • Lemaitre, B. (2004). The road to Toll. Nat. Rev. Immunol. 4, 521-527. doi: 10.1038/nri1390.
    • (2004) Nat. Rev. Immunol , vol.4 , pp. 521-527
    • Lemaitre, B.1
  • 81
    • 84866937631 scopus 로고    scopus 로고
    • Ixodes scapularis JAK-STAT pathway regulates tick antimicrobial peptides, thereby controlling the agent of human granulocytic anaplasmosis
    • doi: 10.1093/infdis/jis484
    • Liu, L., Dai, J., Zhao, Y. O., Narasimhan, S., Yang, Y., Zhang, L., et al. (2012). Ixodes scapularis JAK-STAT pathway regulates tick antimicrobial peptides, thereby controlling the agent of human granulocytic anaplasmosis. J. Infect. Dis. 206, 1233-1241. doi: 10.1093/infdis/jis484.
    • (2012) J. Infect. Dis. , vol.206 , pp. 1233-1241
    • Liu, L.1    Dai, J.2    Zhao, Y.O.3    Narasimhan, S.4    Yang, Y.5    Zhang, L.6
  • 82
    • 2942625911 scopus 로고    scopus 로고
    • Interactions between commensal intestinal bacteria and the immune system
    • doi: 10.1038/nri1373
    • Macpherson, A. J., and Harris, N. L. (2004). Interactions between commensal intestinal bacteria and the immune system. Nat. Rev. Immunol. 4, 478-485. doi: 10.1038/nri1373.
    • (2004) Nat. Rev. Immunol. , vol.4 , pp. 478-485
    • Macpherson, A.J.1    Harris, N.L.2
  • 83
    • 33750805449 scopus 로고    scopus 로고
    • Rel/NF-kappaB double mutants reveal that cellular immunity is central to Drosophila host defense
    • doi: 10.1073/pnas.0605721103.
    • Matova, N., and Anderson, K. V. (2006). Rel/NF-kappaB double mutants reveal that cellular immunity is central to Drosophila host defense. Proc. Natl. Acad.Sci. U.S.A. 103, 16424-16429. doi: 10.1073/pnas.0605721103.
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 16424-16429
    • Matova, N.1    Anderson, K.V.2
  • 84
    • 36849032928 scopus 로고    scopus 로고
    • Phagocytosis of the Lyme disease spirochete, Borrelia burgdorferi, by cells from the ticks, Ixodes scapularis and Dermacentor andersoni, infected with an endosymbiont, Rickettsiapeacockii
    • doi: 10.1673/031.007.5801
    • Mattila, J. T., Munderloh, U. G., and Kurtti, T. J. (2007). Phagocytosis of the Lyme disease spirochete, Borrelia burgdorferi, by cells from the ticks, Ixodes scapularis and Dermacentor andersoni, infected with an endosymbiont, Rickettsiapeacockii. I InsectSci. 7, 58. doi: 10.1673/031.007.5801.
    • (2007) I InsectSci. , vol.7 , pp. 58
    • Mattila, J.T.1    Munderloh, U.G.2    Kurtti, T.J.3
  • 85
    • 41249085856 scopus 로고    scopus 로고
    • Reactive oxygen species modulate Anopheles gambiae immunity against bacteria and Plasmodium
    • doi: 10.1074/jbc.M705873200
    • Molina-Cruz, A., Dejong, R. J., Charles, B., Gupta, L., Kumar, S., Jaramillo- Gutierrez, G., et al. (2008). Reactive oxygen species modulate Anopheles gambiae immunity against bacteria and Plasmodium. J. Biol. Chem. 283, 3217-3223. doi: 10.1074/jbc.M705873200.
    • (2008) J. Biol. Chem. , vol.283 , pp. 3217-3223
    • Molina-Cruz, A.1    Dejong, R.J.2    Charles, B.3    Gupta, L.4    Kumar, S.5    Jaramillo-Gutierrez, G.6
  • 86
    • 78650894319 scopus 로고    scopus 로고
    • Crosstalk of reactive oxygen species and NFkappaB signaling
    • doi: 10.1038/cr.2010.178
    • Morgan, M. J., and Liu, Z. G. (2011). Crosstalk of reactive oxygen species and NFkappaB signaling. CellRes. 21, 103-115. doi: 10.1038/cr.2010.178.
    • (2011) CellRes. , vol.21 , pp. 103-115
    • Morgan, M.J.1    Liu, Z.G.2
  • 87
    • 0035488012 scopus 로고    scopus 로고
    • Tick- Encoded serine proteinase inhibitors (serpins); potential target antigens for tick vaccine development
    • doi: 10.1292/jvms. 63.1063
    • Muleng, A., Sugino, M., Nakajim, M., Sugimoto, C., and Onuma, M. (2001). Tick- Encoded serine proteinase inhibitors (serpins); potential target antigens for tick vaccine development. J. Vet. Med. Sci. 63, 1063-1069. doi: 10.1292/jvms. 63.1063.
    • (2001) J. Vet. Med. Sci. , vol.63 , pp. 1063-1069
    • Muleng, A.1    Sugino, M.2    Nakajim, M.3    Sugimoto, C.4    Onuma, M.5
  • 88
    • 66749177735 scopus 로고    scopus 로고
    • Ixodes scapularis tick serine proteinase inhibitor (serpin) gene family; annotation and transcriptional analysis
    • doi: 10.1186/1471-2164-10-217.
    • Mulenga, A., Khumthong, R., and Chalaire, K. C. (2009). Ixodes scapularis tick serine proteinase inhibitor (serpin) gene family; annotation and transcriptional analysis. BMC Genomics 10:217. doi: 10.1186/1471-2164-10-217.
    • (2009) BMC Genomics , vol.10 , pp. 217
    • Mulenga, A.1    Khumthong, R.2    Chalaire, K.C.3
  • 89
    • 0036897706 scopus 로고    scopus 로고
    • Antibacterial peptide defensin is involved in midgut immunity of the soft tick, Ornithodoros moubata
    • doi: 10.1046/j.1365-2583.2002.00372.x
    • Nakajima, Y., van der Goes van Naters-Yasui, A., Taylor, D., and Yamakawa, M. (2002). Antibacterial peptide defensin is involved in midgut immunity of the soft tick, Ornithodoros moubata. Insect Mol. Biol. 11, 611-618. doi: 10.1046/j.1365-2583.2002.00372.x.
    • (2002) Insect Mol. Biol. , vol.11 , pp. 611-618
    • Nakajima, Y.1    van der Goes van, N.-Y.A.2    Taylor, D.3    Yamakawa, M.4
  • 90
    • 18744386088 scopus 로고    scopus 로고
    • A novel family of anticoagulants from the saliva of Ixodes scapularis
    • doi: 10.1046/j.1365-2583.2002. 00375.x
    • Narasimhan, S., Koski, R. A., Beaulieu, B., Anderson, J. F., Ramamoorthi, N., Kantor, F., et al. (2002). A novel family of anticoagulants from the saliva of Ixodes scapularis. Insect Mol. Biol. 11, 641-650. doi: 10.1046/j.1365-2583.2002. 00375.x.
    • (2002) Insect Mol. Biol. , vol.11 , pp. 641-650
    • Narasimhan, S.1    Koski, R.A.2    Beaulieu, B.3    Anderson, J.F.4    Ramamoorthi, N.5    Kantor, F.6
  • 92
    • 84892582368 scopus 로고    scopus 로고
    • Gut Microbiota of the tick vector Ixodes scapularis modulate colonization of the Lyme disease spirochete
    • doi: 10.1016/j.chom.2013.12.001
    • Narasimhan, S., Rajeevan, N., Liu, L., Zhao, Y. O., Heisig, J., Pan, J., et al. (2014). Gut Microbiota of the tick vector Ixodes scapularis modulate colonization of the Lyme disease spirochete. Cell Host Microbe 15, 58-71. doi: 10.1016/j.chom.2013.12.001.
    • (2014) Cell Host Microbe , vol.15 , pp. 58-71
    • Narasimhan, S.1    Rajeevan, N.2    Liu, L.3    Zhao, Y.O.4    Heisig, J.5    Pan, J.6
  • 93
    • 34347352122 scopus 로고    scopus 로고
    • A tick antioxidant facilitates the Lyme disease agent's successful migration from the mammalian host to the arthropod vector
    • doi: 10.1016/j.chom.2007.06.001
    • Narasimhan, S., Sukumaran, B., Bozdogan, U., Thomas, V., Liang, X., Deponte, K., et al. (2007). A tick antioxidant facilitates the Lyme disease agent's successful migration from the mammalian host to the arthropod vector. Cell Host Microbe 2, 7-18. doi: 10.1016/j.chom.2007.06.001.
    • (2007) Cell Host Microbe , vol.2 , pp. 7-18
    • Narasimhan, S.1    Sukumaran, B.2    Bozdogan, U.3    Thomas, V.4    Liang, X.5    Deponte, K.6
  • 94
    • 1642301073 scopus 로고    scopus 로고
    • Effects of mosquito genes on Plasmodium development
    • doi: 10.1126/science. 1091789
    • Osta, M. A., Christophides, G. K., and Kafatos, F. C. (2004). Effects of mosquito genes on Plasmodium development. Science 303, 2030-2032. doi: 10.1126/science. 1091789.
    • (2004) Science , vol.303 , pp. 2030-2032
    • Osta, M.A.1    Christophides, G.K.2    Kafatos, F.C.3
  • 95
    • 70349446465 scopus 로고    scopus 로고
    • Reactive oxygen species prime Drosophila haematopoietic progenitors for differentiation
    • doi: 10.1038/nature08313
    • Owusu-Ansah, E., and Banerjee, U. (2009). Reactive oxygen species prime Drosophila haematopoietic progenitors for differentiation. Nature 461, 537-541. doi: 10.1038/nature08313.
    • (2009) Nature , vol.461 , pp. 537-541
    • Owusu-Ansah, E.1    Banerjee, U.2
  • 97
  • 98
    • 84862909051 scopus 로고    scopus 로고
    • Wolbachia induces reactive oxygen species (ROS)-dependent activation of the Toll pathway to control dengue virus in the mosquito Aedes aegypti
    • doi: 10.1073/pnas.1116932108
    • Pan, X., Zhou, G., Wu, J., Bian, G., Lu, P., Raikhel, A. S., et al. (2012). Wolbachia induces reactive oxygen species (ROS)-dependent activation of the Toll pathway to control dengue virus in the mosquito Aedes aegypti. Proc. Natl. Acad. Sci. U.S.A. 109, E23-E31. doi: 10.1073/pnas.1116932108.
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109
    • Pan, X.1    Zhou, G.2    Wu, J.3    Bian, G.4    Lu, P.5    Raikhel, A.S.6
  • 99
    • 0035673073 scopus 로고    scopus 로고
    • Production of reactive oxygen species by hemocytes from the cattle tick Boophilus microplus
    • doi: 10.1006/expr.2001.4657
    • Pereira, L. S., Oliveira, P. L., Barja-Fidalgo, C., and Daffre, S. (2001). Production of reactive oxygen species by hemocytes from the cattle tick Boophilus microplus. Exp. Parasitol. 99, 66-72. doi: 10.1006/expr.2001.4657.
    • (2001) Exp. Parasitol. , vol.99 , pp. 66-72
    • Pereira, L.S.1    Oliveira, P.L.2    Barja-Fidalgo, C.3    Daffre, S.4
  • 100
    • 79955766238 scopus 로고    scopus 로고
    • Structure-function analysis of the Anopheles gambiae LRIM1/APL1C complex and its interaction with complement C3-like protein TEP1
    • doi: 10.1371/journal.ppat.1002023.
    • Povelones, M., Upton, L. M., Sala, K. A., and Christophides, G. K. (2011). Structure-function analysis of the Anopheles gambiae LRIM1/APL1C complex and its interaction with complement C3-like protein TEP1. PLoS Pathog. 7:e1002023. doi: 10.1371/journal.ppat.1002023.
    • (2011) PLoS Pathog. , vol.7
    • Povelones, M.1    Upton, L.M.2    Sala, K.A.3    Christophides, G.K.4
  • 101
    • 64849109588 scopus 로고    scopus 로고
    • Leucine-rich repeat protein complex activates mosquito complement in defense against Plasmodium parasites
    • doi: 10.1126/science. 1 171400
    • Povelones, M., Waterhouse, R. M., Kafatos, F. C., and Christophides, G. K. (2009). Leucine-rich repeat protein complex activates mosquito complement in defense against Plasmodium parasites. Science 324, 258-261. doi: 10.1126/science. 1 171400.
    • (2009) Science , vol.324 , pp. 258-261
    • Povelones, M.1    Waterhouse, R.M.2    Kafatos, F.C.3    Christophides, G.K.4
  • 102
    • 2342445635 scopus 로고    scopus 로고
    • The JAK/STAT signaling pathway.J
    • doi: 10.1242/jcs.00963
    • Rawlings, J. S., Rosler, K. M., and Harrison, D. A. (2004). The JAK/STAT signaling pathway.J. CellSci. 117, 1281-1283. doi: 10.1242/jcs.00963.
    • (2004) CellSci. , vol.117 , pp. 1281-1283
    • Rawlings, J.S.1    Rosler, K.M.2    Harrison, D.A.3
  • 103
    • 79959350886 scopus 로고    scopus 로고
    • The Drosophila serpins: multiple functions in immunity and morphogenesis
    • doi: 10.1016/B978-0-12-386471-0.00011-0
    • Reichhart, J. M., Gubb, D., and Leclerc, V. (2011). The Drosophila serpins: multiple functions in immunity and morphogenesis. Meth. Enzymol. 499, 205-225. doi: 10.1016/B978-0-12-386471-0.00011-0.
    • (2011) Meth. Enzymol. , vol.499 , pp. 205-225
    • Reichhart, J.M.1    Gubb, D.2    Leclerc, V.3
  • 104
    • 67349250428 scopus 로고    scopus 로고
    • The gut microbiota shapes intestinal immune responses during health and disease
    • doi: 10.1038/nri2515
    • Round, J. L., and Mazmanian, S. K. (2009). The gut microbiota shapes intestinal immune responses during health and disease. Nat. Rev. Immunol. 9, 313-323. doi: 10.1038/nri2515.
    • (2009) Nat. Rev. Immunol. , vol.9 , pp. 313-323
    • Round, J.L.1    Mazmanian, S.K.2
  • 105
    • 12844284086 scopus 로고    scopus 로고
    • Differential expression of Ixodes ricinus tick genes induced by blood feeding or Borrelia burgdorferi infection
    • doi: 10.1603/0022- 2585(2005)042[0036:DEOIRT]2.0.CO;2
    • Rudenko, N., Golovchenko, M., Edwards, M. J., and Grubhoffer, L. (2005). Differential expression of Ixodes ricinus tick genes induced by blood feeding or Borrelia burgdorferi infection. J. Med. Entomol. 42, 36-41. doi: 10.1603/0022- 2585(2005)042[0036:DEOIRT]2.0.CO;2.
    • (2005) J. Med. Entomol. , vol.42 , pp. 36-41
    • Rudenko, N.1    Golovchenko, M.2    Edwards, M.J.3    Grubhoffer, L.4
  • 106
    • 67651154295 scopus 로고    scopus 로고
    • Identification and characterization of antimicrobial peptide, defensin, in the taiga tick, Ixodes persulcatus
    • doi: 10.111 1/j.1365- 2583.2009.00897.x
    • Saito, Y., Konnai, S., Yamada, S., Imamura, S., Nishikado, H., Ito, T., et al. (2009). Identification and characterization of antimicrobial peptide, defensin, in the taiga tick, Ixodes persulcatus. Insect Mol. Biol. 18, 531-539. doi: 10.111 1/j.1365- 2583.2009.00897.x.
    • (2009) Insect Mol. Biol. , vol.18 , pp. 531-539
    • Saito, Y.1    Konnai, S.2    Yamada, S.3    Imamura, S.4    Nishikado, H.5    Ito, T.6
  • 107
    • 2442707636 scopus 로고    scopus 로고
    • The mosquito's innate sting
    • doi: 10.1038/nm0504-455
    • Saul, A. (2004). The mosquito's innate sting. Nat. Med. 10, 455-457. doi: 10.1038/nm0504-455.
    • (2004) Nat. Med. , vol.10 , pp. 455-457
    • Saul, A.1
  • 108
    • 0015462556 scopus 로고
    • Peptidoglycan types of bacterial cell walls and their taxonomic implications
    • Schleifer, K. H., and Kandler, O. (1972). Peptidoglycan types of bacterial cell walls and their taxonomic implications. Bacteriol. Rev. 36, 407-477.
    • (1972) Bacteriol. Rev. , vol.36 , pp. 407477
    • Schleifer, K.H.1    Kandler, O.2
  • 109
    • 80051863283 scopus 로고    scopus 로고
    • A tick mannose-binding lectin inhibitor interferes with the vertebrate complement cascade to enhance transmission of the lyme disease agent
    • doi: 10.1016/j.chom.2011. 06.010
    • Schuijt, T. J., Coumou, J., Narasimhan, S., Dai, J., Deponte, K., Wouters, D., et al. (2011). A tick mannose-binding lectin inhibitor interferes with the vertebrate complement cascade to enhance transmission of the lyme disease agent. Cell Host Microbe 10, 136-146. doi: 10.1016/j.chom.2011. 06.010.
    • (2011) Cell Host Microbe , vol.10 , pp. 136-146
    • Schuijt, T.J.1    Coumou, J.2    Narasimhan, S.3    Dai, J.4    Deponte, K.5    Wouters, D.6
  • 110
    • 84877148030 scopus 로고    scopus 로고
    • The intestinal microbiota and host immune interactions in the critically ill
    • doi: 10.1016/j.tim.2013.02.001
    • Schuijt, T. J., van der Poll, T., de Vos, W. M., and Wiersinga, W. J. (2013). The intestinal microbiota and host immune interactions in the critically ill. Trends Microbiol. 21, 221-229. doi: 10.1016/j.tim.2013.02.001.
    • (2013) Trends Microbiol. , vol.21 , pp. 221-229
    • Schuijt, T.J.1    van der Poll, T.2    de Vos, W.M.3    Wiersinga, W.J.4
  • 111
    • 1542619261 scopus 로고    scopus 로고
    • Antioxidant role of glutathione S-transferases: protection against oxidant toxicity and regulation of stress-mediated apoptosis
    • doi: 10.1089/152308604322899350
    • Sharma, R., Yang, Y., Sharma, A., Awasthi, S., and Awasthi, Y C. (2004). Antioxidant role of glutathione S-transferases: protection against oxidant toxicity and regulation of stress-mediated apoptosis. Antioxid. Redox Signal. 6, 289-300. doi: 10.1089/152308604322899350.
    • (2004) Antioxid. Redox Signal. , vol.6 , pp. 289-300
    • Sharma, R.1    Yang, Y.2    Sharma, A.3    Awasthi, S.4    Awasthi, Y.C.5
  • 112
    • 0027772891 scopus 로고
    • Polypeptide signalling to the nucleus through tyrosine phosphorylation of Jak and Stat proteins
    • doi: 10.1038/ 366580a0
    • Shuai, K., Ziemiecki, A., Wilks, A. F., Harpur, A. G., Sadowski, H. B., Gilman, M. Z., et al. (1993). Polypeptide signalling to the nucleus through tyrosine phosphorylation of Jak and Stat proteins. Nature 366, 580-583. doi: 10.1038/ 366580a0.
    • (1993) Nature , vol.366 , pp. 580-583
    • Shuai, K.1    Ziemiecki, A.2    Wilks, A.F.3    Harpur, A.G.4    Sadowski, H.B.5    Gilman, M.Z.6
  • 113
    • 39549117368 scopus 로고    scopus 로고
    • Innate immunity in insects: surface-associated dopa decarboxylasedependent pathways regulate phagocytosis, nodulation and melanization in medfly haemocytes
    • doi: 10.1111/j.1365- 2567.2007.02722.x
    • Sideri, M., Tsakas, S., Markoutsa, E., Lampropoulou, M., and Marmaras, V. J. (2008). Innate immunity in insects: surface-associated dopa decarboxylasedependent pathways regulate phagocytosis, nodulation and melanization in medfly haemocytes. Immunology 123, 528-537. doi: 10.1111/j.1365- 2567.2007.02722.x.
    • (2008) Immunology , vol.123 , pp. 528-537
    • Sideri, M.1    Tsakas, S.2    Markoutsa, E.3    Lampropoulou, M.4    Marmaras, V.J.5
  • 114
    • 80053297181 scopus 로고    scopus 로고
    • Cysteine proteases from bloodfeeding arthropod ectoparasites
    • doi: 10.1007/978-1-4419-8414-2_11
    • Sojka, D., Francischetti, I. M., Calvo, E., and Kotsyfakis, M. (2011). Cysteine proteases from bloodfeeding arthropod ectoparasites. Adv. Exp. Med. Biol. 712, 177-191. doi: 10.1007/978-1-4419-8414-2_11.
    • (2011) Adv. Exp. Med. Biol. , vol.712 , pp. 177-191
    • Sojka, D.1    Francischetti, I.M.2    Calvo, E.3    Kotsyfakis, M.4
  • 115
    • 84940276996 scopus 로고
    • New York, NY: Oxford University Press.
    • Sonenshine, D. E. (1993). Biology ofTicks. New York, NY: Oxford University Press.
    • (1993) Biology ofTicks
    • Sonenshine, D.E.1
  • 116
    • 0141457796 scopus 로고    scopus 로고
    • Expression of defensin-like peptides in tick hemolymph and midgut in response to challenge with Borrelia burgdorferi, Escherichia coli and Bacillus subtilis
    • doi: 10.1023/A:10253543 26877
    • Sonenshine, D. E., Ceraul, S. M., Hynes, W. E., Macaluso, K. R., and Azad, A. F. (2002). Expression of defensin-like peptides in tick hemolymph and midgut in response to challenge with Borrelia burgdorferi, Escherichia coli and Bacillus subtilis. Exp. Appl. Acarol. 28, 127-134. doi: 10.1023/A:10253543 26877.
    • (2002) Exp. Appl. Acarol. , vol.28 , pp. 127-134
    • Sonenshine, D.E.1    Ceraul, S.M.2    Hynes, W.E.3    Macaluso, K.R.4    Azad, A.F.5
  • 117
    • 23044477809 scopus 로고    scopus 로고
    • Host blood proteins and peptides in the midgut of the tick Dermacentor variabilis contribute to bacterial control
    • doi: 10.1007/s10493-005-2564-0
    • Sonenshine, D. E., Hynes, W. L., Ceraul, S. M., Mitchell, R., and Benzine, T. (2005). Host blood proteins and peptides in the midgut of the tick Dermacentor variabilis contribute to bacterial control. Exp. Appl. Acarol. 36, 207-223. doi: 10.1007/s10493-005-2564-0.
    • (2005) Exp. Appl. Acarol. , vol.36 , pp. 207-223
    • Sonenshine, D.E.1    Hynes, W.L.2    Ceraul, S.M.3    Mitchell, R.4    Benzine, T.5
  • 118
    • 70449577158 scopus 로고    scopus 로고
    • An evolutionary conserved function of the JAK-STAT pathway in anti-dengue defense
    • doi: 10.1073/pnas.0905006106
    • Souza-Neto, J. A., Sim, S., and Dimopoulos, G. (2009). An evolutionary conserved function of the JAK-STAT pathway in anti-dengue defense. Proc. Natl. Acad. Sci. U.S.A. 106, 17841-17846. doi: 10.1073/pnas.0905006106.
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 17841-17846
    • Souza-Neto, J.A.1    Sim, S.2    Dimopoulos, G.3
  • 119
    • 0023226512 scopus 로고
    • Absence of lipopolysaccharide in the Lyme disease spirochete, Borrelia burgdorferi
    • Takayama, K., Rothenberg, R. J., and Barbour, A. G. (1987). Absence of lipopolysaccharide in the Lyme disease spirochete, Borrelia burgdorferi. Infect. Immun. 55, 2311-2313.
    • (1987) Infect. Immun. , vol.55 , pp. 2311-2313
    • Takayama, K.1    Rothenberg, R.J.2    Barbour, A.G.3
  • 120
    • 34250221179 scopus 로고    scopus 로고
    • Toll and IMD pathways synergistically activate an innate immune response in Drosophila melanogaster
    • doi: 10.1128/MCB.01814-06
    • Tanji, T., Hu, X., Weber, A. N., and Ip, Y T. (2007). Toll and IMD pathways synergistically activate an innate immune response in Drosophila melanogaster. Mol. Cell. Biol. 27, 4578-4588. doi: 10.1128/MCB.01814-06.
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 4578-4588
    • Tanji, T.1    Hu, X.2    Weber, A.N.3    Ip, Y.T.4
  • 121
    • 20044396975 scopus 로고    scopus 로고
    • Regulators of the Toll and IMD pathways in the Drosophila innate immune response
    • doi: 10.1016/j.it.2005.02.006
    • Tanji, T., and Ip, Y T. (2005). Regulators of the Toll and IMD pathways in the Drosophila innate immune response. Trends Immunol. 26, 193-198. doi: 10.1016/j.it.2005.02.006.
    • (2005) Trends Immunol. , vol.26 , pp. 193-198
    • Tanji, T.1    Ip, Y.T.2
  • 123
    • 1842800032 scopus 로고    scopus 로고
    • Coagulation in arthropods: defence, wound closure and healing
    • doi: 10.1016/j.it.2004.03.004
    • Theopold, U., Schmidt, O., Soderhall, K., and Dushay, M. S. (2004). Coagulation in arthropods: defence, wound closure and healing. Trends Immunol. 25, 289-294. doi: 10.1016/j.it.2004.03.004.
    • (2004) Trends Immunol. , vol.25 , pp. 289-294
    • Theopold, U.1    Schmidt, O.2    Soderhall, K.3    Dushay, M.S.4
  • 124
    • 0023656119 scopus 로고
    • Lipopolysaccharide-sensitive serine-protease zymogen (factor C) of horseshoe crab hemocytes Identification and alignment of proteolytic fragments produced during the activation show that it is a novel type of serine protease
    • doi: 10.1111/j.1432-1033.1987. tb13352.x
    • Tokunaga, F., Miyata, T., Nakamura, T., Morita, T., Kuma, K., Miyata, T., et al. (1987). Lipopolysaccharide-sensitive serine-protease zymogen (factor C) of horseshoe crab hemocytes. Identification and alignment of proteolytic fragments produced during the activation show that it is a novel type of serine protease. Eur. J. Biochem. 167, 405-416. doi: 10.1111/j.1432-1033.1987. tb13352.x.
    • (1987) Eur. J. Biochem. , vol.167 , pp. 405-416
    • Tokunaga, F.1    Miyata, T.2    Nakamura, T.3    Morita, T.4    Kuma, K.5    Miyata, T.6
  • 125
    • 0030333524 scopus 로고    scopus 로고
    • Novel agglutinin in the midgut of the tick Ixodes ricinus
    • Uhlir, J., Grubhoffer, L., and Volf, P. (1996). Novel agglutinin in the midgut of the tick Ixodes ricinus. Folia Parasitol. (Praha) 43, 233-239.
    • (1996) Folia Parasitol. (Praha) , vol.43 , pp. 233-239
    • Uhlir, J.1    Grubhoffer, L.2    Volf, P.3
  • 126
    • 17444363029 scopus 로고    scopus 로고
    • Genome size and organization in the blacklegged tick, Ixodes scapularis and the Southern cattle tick, Boophilus microplus
    • doi: 10.1111/j.1365-2583.2005.00551.x
    • Ullmann, A. J., Lima, C. M., Guerrero, F. D., Piesman, J., and Black, W. C. T. (2005). Genome size and organization in the blacklegged tick, Ixodes scapularis and the Southern cattle tick, Boophilus microplus. Insect Mol. Biol. 14, 217-222. doi: 10.1111/j.1365-2583.2005.00551.x.
    • (2005) Insect Mol. Biol. , vol.14 , pp. 217-222
    • Ullmann, A.J.1    Lima, C.M.2    Guerrero, F.D.3    Piesman, J.4    Black, W.C.T.5
  • 127
    • 79251557500 scopus 로고    scopus 로고
    • The Drosophila Toll signaling pathway.J
    • doi: 10.4049/jimmunol.1002302
    • Valanne, S., Wang, J. H., and Ramet, M. (2011). The Drosophila Toll signaling pathway.J. Immunol. 186, 649-656. doi: 10.4049/jimmunol.1002302 Vilmos, P., and Kurucz, E. (1998). Insect immunity: evolutionary roots of the mammalian innate immune system. Immunol. Lett. 62, 59-66. doi: 10.1016/S0165- 2478(98)00023-6.
    • (2011) Immunol. , vol.186 , pp. 649-656
    • Valanne, S.1    Wang, J.H.2    Ramet, M.3
  • 128
    • 0031854424 scopus 로고    scopus 로고
    • Insect immunity: evolutionary roots of the mammalian innate immune system
    • doi: 10.1016/S0165- 2478(98)00023-6
    • Vilmos, P., and Kurucz, E. (1998). Insect immunity: evolutionary roots of the mammalian innate immune system. Immunol. Lett. 62, 59-66. doi: 10.1016/S0165- 2478(98)00023-6
    • (1998) Immunol. Lett. , vol.62 , pp. 59-66
    • Vilmos, P.1    Kurucz, E.2
  • 129
    • 0018010183 scopus 로고
    • Phagocytosis: a review
    • doi: 10.3109/10408447809081012. Wandurska-Nowak, E. (2004). [The role of nitric oxide (NO) in parasitic infections]. Wiad. Parazytol. 50, 665-678
    • Walters, M. N., and Papadimitriou, J. M. (1978). Phagocytosis: a review. CRC Crit. Rev. Toxicol. 5, 377-421. doi: 10.3109/10408447809081012. Wandurska-Nowak, E. (2004). [The role of nitric oxide (NO) in parasitic infections]. Wiad. Parazytol. 50, 665-678.
    • (1978) CRC Crit. Rev. Toxicol. , vol.5 , pp. 377-421
    • Walters, M.N.1    Papadimitriou, J.M.2
  • 130
    • 0030019155 scopus 로고    scopus 로고
    • Host immunity to ticks
    • doi: 10.1146/annurev.en.41.010196.000245
    • Wikel, S. K. (1996). Host immunity to ticks. Annu. Rev. Entomol. 41, 1-22. doi: 10.1146/annurev.en.41.010196.000245.
    • (1996) Annu. Rev. Entomol. , vol.41 , pp. 1-22
    • Wikel, S.K.1
  • 131
    • 48249112228 scopus 로고    scopus 로고
    • The Aedes aegypti toll pathway controls dengue virus infection.
    • doi: 10.1371/journal. ppat.1000098.
    • Xi, Z., Ramirez, J. L., and Dimopoulos, G. (2008). The Aedes aegypti toll pathway controls dengue virus infection. PLoS Pathog. 4:e1000098. doi: 10.1371/journal. ppat.1000098.
    • (2008) PLoS Pathog , vol.4
    • Xi, Z.1    Ramirez, J.L.2    Dimopoulos, G.3
  • 132
    • 77649219382 scopus 로고    scopus 로고
    • Anopheles gambiae innate immunity
    • doi: 10.1111/j.1462-5822.2009.01388.x
    • Yassine, H., and Osta, M. A. (2010). Anopheles gambiae innate immunity. Cell. Microbiol. 12, 1-9. doi: 10.1111/j.1462-5822.2009.01388.x.
    • (2010) Cell. Microbiol. , vol.12 , pp. 1-9
    • Yassine, H.1    Osta, M.A.2
  • 133
    • 18844411853 scopus 로고    scopus 로고
    • The Toll pathway is important for an antiviral response in Drosophila
    • doi: 10.1073/pnas.0409181102
    • Zambon, R. A., Nandakumar, M., Vakharia, V. N., and Wu, L. P. (2005). The Toll pathway is important for an antiviral response in Drosophila. Proc. Natl. Acad. Sci. U.S.A. 102, 7257-7262. doi: 10.1073/pnas.0409181102.
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 7257-7262
    • Zambon, R.A.1    Nandakumar, M.2    Vakharia, V.N.3    Wu, L.P.4
  • 134
    • 70349206320 scopus 로고    scopus 로고
    • Drosomycin, an essential component of antifungal defence in Drosophila
    • doi: 10.1111/j. 1365- 2583.2009.00907.x
    • Zhang, Z. T., and Zhu, S. Y. (2009). Drosomycin, an essential component of antifungal defence in Drosophila. Insect Mol. Biol. 18, 549-556. doi: 10.1111/j. 1365- 2583.2009.00907.x.
    • (2009) Insect Mol. Biol. , vol.18 , pp. 549-556
    • Zhang, Z.T.1    Zhu, S.Y.2
  • 135
    • 77957003068 scopus 로고    scopus 로고
    • Leureptin: a soluble, extracellular leucine-rich repeat protein from Manduca sexta that binds lipopolysaccharide
    • doi: 10.1016/j.ibmb.2010.07.002
    • Zhu, Y., Ragan, E. J., and Kanost, M. R. (2010). Leureptin: a soluble, extracellular leucine-rich repeat protein from Manduca sexta that binds lipopolysaccharide. Insect Biochem. Mol. Biol. 40, 713-722. doi: 10.1016/j.ibmb.2010.07.002.
    • (2010) Insect Biochem. Mol. Biol. , vol.40 , pp. 713-722
    • Zhu, Y.1    Ragan, E.J.2    Kanost, M.R.3


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