{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,26]],"date-time":"2026-09-26T10:29:50Z","timestamp":1790418590705,"version":"4.1.0"},"reference-count":42,"publisher":"American Society for Microbiology","issue":"11","license":[{"start":{"date-parts":[[2007,11,1]],"date-time":"2007-11-01T00:00:00Z","timestamp":1193875200000},"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":[[2007,11]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n                  <jats:p>\n                    <jats:italic>Borrelia burgdorferi<\/jats:italic>\n                    CspZ (TIGR open reading frame designation, BBH06) is part of a functionally related group of proteins that bind one or more members of the factor H (FH) protein family. In this report we assess the conservation, distribution, properties, and ligand binding abilities of CspZ from the three main\n                    <jats:italic>Borrelia<\/jats:italic>\n                    species associated with Lyme disease infections in humans. CspZ (also referred to as BbCRASP-2 in the literature) was found to be highly conserved at the intraspecies level but divergent at the interspecies level. All CspZ orthologs that originated from\n                    <jats:italic>B. burgdorferi<\/jats:italic>\n                    isolates bound FH from a diverse group of mammals. In contrast, CspZ derived from\n                    <jats:italic>B. garinii<\/jats:italic>\n                    and\n                    <jats:italic>B. afzelii<\/jats:italic>\n                    did not. Regardless of the\n                    <jats:italic>Borrelia<\/jats:italic>\n                    species of origin, all CspZ proteins tested bound to unknown \u223c60-kDa serum proteins produced by different mammals. To further define the molecular basis for the differential binding of CspZ orthologs to host proteins, DNA sequence, truncation, and site-directed mutagenesis analyses were performed. DNA sequence analyses revealed that\n                    <jats:italic>B. garinii<\/jats:italic>\n                    and\n                    <jats:italic>B. afzelii<\/jats:italic>\n                    CspZ orthologs possess a 64-amino-acid N-terminal domain that is absent from\n                    <jats:italic>B. burgdorferi<\/jats:italic>\n                    CspZ. However, binding analyses of recombinant proteins revealed that this domain does not in and of itself influence ligand binding properties. Truncation and mutagenesis analyses further revealed that the key determinants required for ligand binding are discontinuous and that the presentation of the ligand binding pocket is dependent on alpha helices with high coiled-coil formation probability. The data presented here provide insight into the molecular basis of CspZ-ligand interactions and suggest that CspZ orthologs from diverse\n                    <jats:italic>Borrelia<\/jats:italic>\n                    species can contribute to the host-pathogen interaction through their interaction with serum proteins.\n                  <\/jats:p>","DOI":"10.1128\/iai.00850-07","type":"journal-article","created":{"date-parts":[[2007,9,10]],"date-time":"2007-09-10T20:54:39Z","timestamp":1189457679000},"page":"5272-5281","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":57,"title":["Delineation of Species-Specific Binding Properties of the CspZ Protein (BBH06) of Lyme Disease Spirochetes: Evidence for New Contributions to the Pathogenesis of\n                    <i>Borrelia<\/i>\n                    spp"],"prefix":"10.1128","volume":"75","author":[{"given":"Elizabeth A.","family":"Rogers","sequence":"first","affiliation":[{"name":"Department of Microbiology and Immunology, Medical College of Virginia at Virginia Commonwealth University"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Richard T.","family":"Marconi","sequence":"additional","affiliation":[{"name":"Department of Microbiology and Immunology, Medical College of Virginia at Virginia Commonwealth University"},{"name":"Center for the Study of Biological Complexity, Richmond, Virginia 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