{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,27]],"date-time":"2026-01-27T23:37:59Z","timestamp":1769557079014,"version":"3.49.0"},"reference-count":52,"publisher":"American Society for Microbiology","issue":"2","license":[{"start":{"date-parts":[[2019,1,15]],"date-time":"2019-01-15T00:00:00Z","timestamp":1547510400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"funder":[{"DOI":"10.13039\/100000072","name":"HHS | NIH | National Institute of Dental and Craniofacial Research","doi-asserted-by":"publisher","award":["DE-025225"],"award-info":[{"award-number":["DE-025225"]}],"id":[{"id":"10.13039\/100000072","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000072","name":"HHS | NIH | National Institute of Dental and Craniofacial Research","doi-asserted-by":"publisher","award":["DE-018221"],"award-info":[{"award-number":["DE-018221"]}],"id":[{"id":"10.13039\/100000072","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["J Bacteriol"],"published-print":{"date-parts":[[2019,1,15]]},"abstract":"<jats:p><jats:italic>Treponema denticola<\/jats:italic>is among a small subset of the oral microbiota contributing to severe periodontal disease. Due to its relative genetic tractability,<jats:italic>T. denticola<\/jats:italic>is a model organism for studying<jats:italic>Treponema<\/jats:italic>physiology and host-microbe interactions.<jats:italic>T. denticola<\/jats:italic>Msp is a highly expressed outer membrane-associated oligomeric protein that binds fibronectin, has cytotoxic pore-forming activity, and disrupts intracellular regulatory pathways. It shares homology with the orthologous group of<jats:italic>T. pallidum<\/jats:italic>Tpr proteins, one of which is implicated in<jats:italic>T. pallidum in vivo<\/jats:italic>antigenic variation. The outer membrane topologies of both Msp and the Tpr family proteins are unresolved, with conflicting reports on protein domain localization and function. In this study, we combined empirical immunological data derived both from diverse<jats:italic>T. denticola<\/jats:italic>strains and from recombinant Msp expression in<jats:italic>E. coli<\/jats:italic>with<jats:italic>in silico<\/jats:italic>predictive structural modeling of<jats:italic>T. denticola<\/jats:italic>Msp membrane topology, to move toward resolution of this important issue in<jats:italic>Treponema<\/jats:italic>biology.<\/jats:p>","DOI":"10.1128\/jb.00528-18","type":"journal-article","created":{"date-parts":[[2018,10,25]],"date-time":"2018-10-25T13:01:34Z","timestamp":1540472494000},"update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":11,"title":["Immunotopological Analysis of the<i>Treponema denticola<\/i>Major Surface Protein (Msp)"],"prefix":"10.1128","volume":"201","author":[{"given":"Valentina","family":"Godovikova","sequence":"first","affiliation":[{"name":"Department of Biologic and Materials Sciences, School of Dentistry, University of Michigan, Ann Arbor, Michigan, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"M. 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