{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,18]],"date-time":"2026-06-18T06:57:49Z","timestamp":1781765869928,"version":"3.54.5"},"reference-count":62,"publisher":"American Society for Microbiology","issue":"9","license":[{"start":{"date-parts":[[2011,9,1]],"date-time":"2011-09-01T00:00:00Z","timestamp":1314835200000},"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":["Infect Immun"],"published-print":{"date-parts":[[2011,9]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            After transmission by an infected tick, the Lyme disease spirochete,\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            sensu lato, colonizes the mammalian skin and may disseminate systemically. The three major species of Lyme disease spirochete\u2014\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            sensu stricto,\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">B. garinii<\/jats:named-content>\n            , and\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">B. afzelii<\/jats:named-content>\n            \u2014are associated with different chronic disease manifestations. Colonization is likely promoted by the ability to bind to target tissues, and Lyme disease spirochetes utilize multiple adhesive molecules to interact with diverse mammalian components. The allelic variable surface lipoprotein decorin binding protein A (DbpA) promotes bacterial binding to the proteoglycan decorin and to the glycosaminoglycan (GAG) dermatan sulfate. To assess allelic variation of DbpA in GAG-, decorin-, and cell-binding activities, we expressed\n            <jats:italic>dbpA<\/jats:italic>\n            alleles derived from diverse Lyme disease spirochetes in\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            strain B314, a noninfectious and nonadherent strain that lacks\n            <jats:italic>dbpA<\/jats:italic>\n            . Each DbpA allele conferred upon\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            strain B314 the ability to bind to cultured kidney epithelial (but not glial or endothelial) cells, as well as to purified decorin and dermatan sulfate. Nevertheless, allelic variation of DbpA was associated with dramatic differences in substrate binding activity. In most cases, decorin and dermatan sulfate binding correlated well, but DbpA of\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">B. afzelii<\/jats:named-content>\n            strain VS461 promoted differential binding to decorin and dermatan sulfate, indicating that the two activities are separable. DbpA from a clone of\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            strain N40 that can cause disseminated infection in mice displayed relatively low adhesive activity, indicating that robust DbpA-mediated adhesive activity is not required for spread in the mammalian host.\n          <\/jats:p>","DOI":"10.1128\/iai.00163-11","type":"journal-article","created":{"date-parts":[[2011,6,28]],"date-time":"2011-06-28T06:56:41Z","timestamp":1309244201000},"page":"3501-3509","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":62,"title":["Allelic Variation of the Lyme Disease Spirochete Adhesin DbpA Influences Spirochetal Binding to Decorin, Dermatan Sulfate, and Mammalian Cells"],"prefix":"10.1128","volume":"79","author":[{"given":"Vivian M.","family":"Benoit","sequence":"first","affiliation":[{"name":"Department of Microbiology and Physiological Systems, University of Massachusetts Medical School, Worcester, Massachusetts"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Joshua R.","family":"Fischer","sequence":"additional","affiliation":[{"name":"Program in Immunology and Virology, University of Massachusetts Medical School, Worcester, Massachusetts"},{"name":"Present address: Monsanto, Inc., St. Louis, MO 63167."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yi-Pin","family":"Lin","sequence":"additional","affiliation":[{"name":"Department of Microbiology and Physiological Systems, University of Massachusetts Medical School, Worcester, Massachusetts"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nikhat","family":"Parveen","sequence":"additional","affiliation":[{"name":"Department of Microbiology and Molecular Genetics, University of Medicine and Dentistry of New Jersey, Newark, New Jersey"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"John M.","family":"Leong","sequence":"additional","affiliation":[{"name":"Department of Microbiology and Physiological Systems, University of Massachusetts Medical School, Worcester, Massachusetts"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"publisher","DOI":"10.1128\/JCM.43.4.1879-1884.2005"},{"key":"e_1_3_2_3_2","first-page":"521","article-title":"Isolation and cultivation of Lyme disease spirochetes","volume":"57","author":"Barbour A. 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