An investigation of binding ability of Ixodes persulcatus Schulze Salp15 with Lyme disease spirochetes

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cg.authorship.typesNot CGIAR developing country instituteen
cg.contributor.affiliationHokkaido Universityen
cg.contributor.affiliationHokkaido Institute of Public Healthen
cg.contributor.affiliationYamaguchi Universityen
cg.contributor.affiliationNational Institute of Infectious Diseases, Japanen
cg.contributor.donorMinistry of Health, Labor and Welfare, Japanen
cg.contributor.donorJapan Society for the Promotion of Scienceen
cg.creator.identifierNaftaly Githaka: 0000-0003-4530-7164
cg.howPublishedFormally Publisheden
cg.identifier.doihttps://doi.org/10.1016/j.ibmb.2015.01.010en
cg.issn0965-1748en
cg.journalInsect Biochemistry and Molecular Biologyen
cg.subject.ilriANIMAL DISEASESen
cg.subject.ilriANIMAL HEALTHen
cg.subject.ilriCATTLEen
cg.volume60en
dc.contributor.authorMurase, Y.en
dc.contributor.authorKonnai, S.en
dc.contributor.authorYamada, S.en
dc.contributor.authorGithaka, Naftaly W.en
dc.contributor.authorIsezaki, M.en
dc.contributor.authorIto, T.en
dc.contributor.authorTakano, A.en
dc.contributor.authorAndo, S.en
dc.contributor.authorKawabata, H.en
dc.contributor.authorMurata, S.en
dc.contributor.authorOhashi, K.en
dc.date.accessioned2017-04-05T10:33:14Zen
dc.date.available2017-04-05T10:33:14Zen
dc.identifier.urihttps://hdl.handle.net/10568/80666
dc.titleAn investigation of binding ability of Ixodes persulcatus Schulze Salp15 with Lyme disease spirochetesen
dcterms.abstractSalp15, a 15-kDa tick salivary gland protein, has several suppressive modes of activity against host immunity and plays a critical role in the transmission of Lyme disease spirochetes in Ixodes scapularis and Ixodes ricinus, major vectors of Lyme disease in North America and Western Europe. Salp15 adheres to Borrelia burgdorferi and specifically interacts with its outer surface protein C (OspC), protecting the spirochete from antibody-mediated cytotoxicity and facilitating infection in the mice. Recently, we identified two Salp15 homologues, IperSalp15-1 and IperSalp15-2, in Ixodes persulcatus, a vector for Lyme disease in Japan. Here we describe the function of IperSalp15 in the transmission of Lyme borreliosis. To investigate the function of IperSalp15, recombinant IperSalp15-1 and IperSalp15-2 were prepared in bacterial and insect cells. Both were identified in the sera of tick-immunized hamsters, indicating that these are secretory proteins in exposed host animals. Solid-phase overlay and indirect fluorescence assays showed that IperSalp15 binds to OspC from B. burgdorferi, Borrelia garinii, and Borrelia afzelii. Importantly, this binding likely protected the spirochete from antibody-mediated cytotoxicity in vitro. In addition, IperSalp15 tended to facilitate infection in mice. Thus, further characterization of tick molecules, including IperSalp15, could lead to the development of new strategies to prevent the transmission of tick-borne diseases.en
dcterms.accessRightsLimited Access
dcterms.audienceScientistsen
dcterms.bibliographicCitationMurase, Y., Konnai, S., Yamada, S., Githaka, N., Isezaki, M., Ito, T., Takano, A., Ando, S., Kawabata, H., Murata, S. and Ohashi, K. 2015. An investigation of binding ability of Ixodes persulcatus Schulze Salp15 with Lyme disease spirochetes. Insect Biochemistry and Molecular Biology 60: 59–67.en
dcterms.extent59-67en
dcterms.issued2015-05
dcterms.languageen
dcterms.licenseCopyrighted; all rights reserved
dcterms.publisherElsevieren
dcterms.subjectanimal healthen
dcterms.subjectcattleen
dcterms.subjectantibodiesen
dcterms.subjectborrelia burgdorferien
dcterms.subjectborreliosisen
dcterms.subjectimmunityen
dcterms.subjectanimal diseasesen
dcterms.typeJournal Article

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