{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,31]],"date-time":"2025-10-31T13:55:33Z","timestamp":1761918933913},"reference-count":48,"publisher":"American Society for Microbiology","issue":"5","license":[{"start":{"date-parts":[[2007,3,1]],"date-time":"2007-03-01T00:00:00Z","timestamp":1172707200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["J Bacteriol"],"published-print":{"date-parts":[[2007,3]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            The outer membrane of\n            <jats:italic>Borrelia burgdorferi<\/jats:italic>\n            , the causative agent of Lyme disease, contains very few integral membrane proteins, in contrast to other gram-negative bacteria. BBA74, a\n            <jats:italic>Borrelia burgdorferi<\/jats:italic>\n            plasmid-encoded protein, was proposed to be an integral outer membrane protein with putative porin function and designated as a 28-kDa outer membrane-spanning porin (Oms28). In this study, the biophysical properties of BBA74 and its subcellular localization were investigated. BBA74 is posttranslationally modified by signal peptidase I cleavage to a mature 25-kDa protein. The secondary structure of BBA74 as determined by circular dichroism spectroscopy consists of at least 78% \u03b1-helix with little \u03b2-sheet structure. BBA74 in intact\n            <jats:italic>B. burgdorferi<\/jats:italic>\n            cells was insensitive to proteinase K digestion, and indirect immunofluorescence microscopy showed that BBA74 was not exposed on the cell surface. Triton X-114 extraction of outer membrane vesicle preparations indicated that BBA74 is not an integral membrane protein. Taken together, the data indicate that BBA74 is a periplasmic, outer membrane-associated protein that lacks properties typically associated with porins.\n          <\/jats:p>","DOI":"10.1128\/jb.01239-06","type":"journal-article","created":{"date-parts":[[2006,12,23]],"date-time":"2006-12-23T01:34:25Z","timestamp":1166837665000},"page":"2063-2068","update-policy":"http:\/\/dx.doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":31,"title":["<i>Borrelia burgdorferi<\/i>\n            BBA74, a Periplasmic Protein Associated with the Outer Membrane, Lacks Porin-Like Properties"],"prefix":"10.1128","volume":"189","author":[{"given":"Vishwaroop","family":"Mulay","sequence":"first","affiliation":[{"name":"Departments of Biochemistry &amp; Molecular Biology"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Melissa J.","family":"Caimano","sequence":"additional","affiliation":[{"name":"Departments of Medicine"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Dionysios","family":"Liveris","sequence":"additional","affiliation":[{"name":"Microbiology &amp; Immunology, New York Medical College, Valhalla, New York 10595"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Daniel C.","family":"Desrosiers","sequence":"additional","affiliation":[{"name":"Departments of Medicine"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Justin D.","family":"Radolf","sequence":"additional","affiliation":[{"name":"Departments of Medicine"},{"name":"Genetics and Developmental Biology, University of Connecticut Health Center, Farmington, Connecticut 06030"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ira","family":"Schwartz","sequence":"additional","affiliation":[{"name":"Departments of Biochemistry &amp; Molecular Biology"},{"name":"Microbiology &amp; Immunology, New York Medical College, Valhalla, New York 10595"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"crossref","first-page":"740","DOI":"10.1056\/NEJM198303313081302","volume":"308","year":"1983","unstructured":"Benach, J. 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