{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,21]],"date-time":"2026-10-21T16:24:48Z","timestamp":1792599888194,"version":"4.5.0"},"reference-count":60,"publisher":"American Society for Microbiology","issue":"2","license":[{"start":{"date-parts":[[2018,2,1]],"date-time":"2018-02-01T00:00:00Z","timestamp":1517443200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"funder":[{"DOI":"10.13039\/100000002","name":"HHS | National Institutes of Health","doi-asserted-by":"publisher","award":["AI089921"],"award-info":[{"award-number":["AI089921"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["Infect Immun"],"published-print":{"date-parts":[[2018,2]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            The Lyme disease-causing organism\n            <jats:named-content content-type=\"genus-species\">Borrelia burgdorferi<\/jats:named-content>\n            is transmitted into the mammalian host by an infected-tick bite. Successful infection relies on the ability of this extracellular pathogen to persist and colonize different tissues.\n            <jats:named-content content-type=\"genus-species\">B. burgdorferi<\/jats:named-content>\n            encodes a large number of adhesins that are able to interact with host ligands to facilitate adherence and tissue colonization. Multiple glycosaminoglycan binding proteins present in\n            <jats:named-content content-type=\"genus-species\">B. burgdorferi<\/jats:named-content>\n            offer a degree of redundancy of function during infection, and this highlights the importance of glycosaminoglycans as host cell receptors for spirochete adherence. Of particular interest in this study is\n            <jats:named-content content-type=\"genus-species\">Borrelia<\/jats:named-content>\n            glycosaminoglycan binding protein (Bgp), which binds to heparin-related glycosaminoglycans. The properties of a\n            <jats:italic>bgp<\/jats:italic>\n            transposon mutant and a\n            <jats:italic>trans<\/jats:italic>\n            -complemented derivative were compared to those of the wild-type\n            <jats:named-content content-type=\"genus-species\">B. burgdorferi<\/jats:named-content>\n            in the\n            <jats:italic>in vitro<\/jats:italic>\n            binding assays and in infection studies using a C3H\/HeJ mouse infection model. We determined that the loss of Bgp impairs spirochete adherence, infectivity, and tissue colonization, resulting in a reduction of inflammatory manifestations of Lyme disease. Although Bgp is not essential for infectivity, it is an important virulence factor of\n            <jats:named-content content-type=\"genus-species\">B. burgdorferi<\/jats:named-content>\n            that allows adherence and tissue colonization and contributes to disease severity.\n          <\/jats:p>","DOI":"10.1128\/iai.00667-17","type":"journal-article","created":{"date-parts":[[2017,11,20]],"date-time":"2017-11-20T16:30:20Z","timestamp":1511195420000},"update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":15,"title":["The Borrelia burgdorferi Glycosaminoglycan Binding Protein Bgp in the B31 Strain Is Not Essential for Infectivity despite Facilitating Adherence and Tissue Colonization"],"prefix":"10.1128","volume":"86","author":[{"given":"Samantha","family":"Schlachter","sequence":"first","affiliation":[{"name":"Department of Microbiology, Biochemistry and Molecular Genetics, Rutgers New Jersey Medical School, Newark, 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