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However, the requirements for their proper surface display remained undefined. In previous studies, we showed that localization of\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Borrelia burgdorferi<\/jats:named-content>\n            monomeric surface lipoprotein OspA was dependent on residues in the N-terminal \u201ctether\u201d peptide. Here, site-directed mutagenesis of the\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">B. burgdorferi<\/jats:named-content>\n            OspC tether revealed two distinct regions affecting either release from the inner membrane or translocation through the outer membrane. Determinants of both of these steps appear consolidated within a single region of the\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Borrelia turicatae<\/jats:named-content>\n            Vsp1 tether. Periplasmic OspC mutants still were able to form dimers. Their localization defect could be rescued by the addition of an apparently structure-destabilizing C-terminal epitope tag but not by coexpression with wild-type OspC. Furthermore, disruption of intermolecular Vsp1 salt bridges blocked dimerization but not surface localization of the resulting Vsp1 monomers. Together, these results suggest that\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Borrelia<\/jats:named-content>\n            OspC\/Vsp1 surface lipoproteins traverse the periplasm and the outer membrane as unfolded monomeric intermediates and assemble into their functional multimeric folds only upon reaching the spirochetal surface.\n          <\/jats:p>","DOI":"10.1128\/jb.00015-11","type":"journal-article","created":{"date-parts":[[2011,3,27]],"date-time":"2011-03-27T00:13:53Z","timestamp":1301184833000},"page":"2814-2825","update-policy":"http:\/\/dx.doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":38,"title":["Surface Localization Determinants of Borrelia OspC\/Vsp Family Lipoproteins"],"prefix":"10.1128","volume":"193","author":[{"given":"Ozan S.","family":"Kumru","sequence":"first","affiliation":[{"name":"Department of Microbiology, Molecular Genetics and Immunology, University of Kansas Medical Center, 3901 Rainbow Boulevard, Kansas City, Kansas 66160"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ryan J.","family":"Schulze","sequence":"additional","affiliation":[{"name":"Department of Microbiology, Molecular Genetics and Immunology, University of Kansas Medical Center, 3901 Rainbow Boulevard, Kansas City, Kansas 66160"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Mykola V.","family":"Rodnin","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Biology, University of Kansas Medical Center, 3901 Rainbow Boulevard, Kansas City, Kansas 66160"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Alexey S.","family":"Ladokhin","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Biology, University of Kansas Medical Center, 3901 Rainbow Boulevard, Kansas City, Kansas 66160"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Wolfram R.","family":"Z\u00fcckert","sequence":"additional","affiliation":[{"name":"Department of Microbiology, Molecular Genetics and Immunology, University of Kansas Medical Center, 3901 Rainbow Boulevard, Kansas City, Kansas 66160"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"crossref","first-page":"1526","DOI":"10.1128\/IAI.67.3.1526-1532.1999","article-title":"Molecular and evolutionary analysis of Borrelia burgdorferi 297 circular plasmid-encoded lipoproteins with OspE- and OspF-like leader peptides","volume":"67","author":"Akins D. 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