{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2023,9,14]],"date-time":"2023-09-14T14:10:10Z","timestamp":1694700610436},"reference-count":52,"publisher":"American Society for Microbiology","issue":"6","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Clin. Vaccine Immunol."],"published-print":{"date-parts":[[2011,6]]},"abstract":"<jats:title>ABSTRACT<\/jats:title><jats:p><jats:named-content content-type=\"genus-species\">Borrelia burgdorferi<\/jats:named-content>OspC is an outer membrane lipoprotein required for the establishment of infection in mammals. Due to its universal distribution among<jats:named-content content-type=\"genus-species\">B. burgdorferi<\/jats:named-content>sensu lato strains and high antigenicity, it is being explored for the development of a next-generation Lyme disease vaccine. An understanding of the surface presentation of OspC will facilitate efforts to maximize its potential as a vaccine candidate. OspC forms homodimers at the cell surface, and it has been hypothesized that it may also form oligomeric arrays. Here, we employ site-directed mutagenesis to test the hypothesis that interdimeric disulfide bonds at cysteine 130 (C130) mediate oligomerization.<jats:named-content content-type=\"genus-species\">B. burgdorferi<\/jats:named-content>B31<jats:named-content content-type=\"genus-species\">ospC<\/jats:named-content>was replaced with a C130A substitution mutant to yield strain B31::<jats:named-content content-type=\"genus-species\">ospC<\/jats:named-content>(<jats:named-content content-type=\"genus-species\">C130A<\/jats:named-content>). Recombinant protein was also generated. Disulfide-bond-dependent oligomer formation was demonstrated and determined to be dependent on C130. Oligomerization was not required for<jats:italic>in vivo<\/jats:italic>function, as B31::<jats:named-content content-type=\"genus-species\">ospC<\/jats:named-content>(<jats:named-content content-type=\"genus-species\">C130A<\/jats:named-content>) retained infectivity and disseminated normally. The total IgG response and the induced isotype pattern were similar between mice infected with untransformed B31 and those infected with the B31::<jats:named-content content-type=\"genus-species\">ospC<\/jats:named-content>(<jats:named-content content-type=\"genus-species\">C130A<\/jats:named-content>) strain. These data indicate that the immune response to OspC is not significantly altered by formation of OspC oligomers, a finding that has significant implications in Lyme disease vaccine design.<\/jats:p>","DOI":"10.1128\/cvi.05004-11","type":"journal-article","created":{"date-parts":[[2011,4,28]],"date-time":"2011-04-28T02:44:13Z","timestamp":1303958653000},"page":"901-906","source":"Crossref","is-referenced-by-count":10,"title":["Disulfide-Mediated Oligomer Formation in Borrelia burgdorferi Outer Surface Protein C, a Critical Virulence Factor and Potential Lyme Disease Vaccine Candidate"],"prefix":"10.1128","volume":"18","author":[{"given":"Christopher G.","family":"Earnhart","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"DeLacy V. L.","family":"Rhodes","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Richard T.","family":"Marconi","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"235","published-online":{"date-parts":[[2011,4,27]]},"reference":[{"key":"key20180919073517_B1","doi-asserted-by":"crossref","first-page":"849","DOI":"10.1016\/S1074-7613(02)00325-4","article-title":"Salp15, an Ixodes scapularis salivary protein, inhibits CD4(+) T cell activation","volume":"16","author":"Anguita","year":"2002","journal-title":"Immunity"},{"key":"key20180919073517_B2","first-page":"521","article-title":"Isolation and cultivation of Lyme disease spirochetes","volume":"57","author":"Barbour","year":"1984","journal-title":"Yale J. Biol. 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