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The major outer sheath protein is a highly expressed virulence factor of the well\u2010characterized species\n                    <jats:italic>Treponema denticola<\/jats:italic>\n                    . Msp forms an oligomeric membrane protein complex with adhesin and porin properties and contributes to host\u2013microbial interaction.\n                    <jats:italic>Treponema maltophilum<\/jats:italic>\n                    and\n                    <jats:italic>Treponema lecithinolyticum<\/jats:italic>\n                    species are also prominent during periodontitis but are relatively understudied. Msp\u2010like membrane surface proteins exist in\n                    <jats:italic>T. maltophilum<\/jats:italic>\n                    (MspA) and\n                    <jats:italic>T. lecithinolyticum<\/jats:italic>\n                    (MspTL), but limited information exists regarding their structural features or functionality. Protein profiling reveals numerous differences between these species, but minimal differences between strains of the same species. Using protein modeling tools, we predict MspA and MspTL monomeric forms to be large \u03b2\u2010barrel structures composed of 20 all\u2010next\u2010neighbor antiparallel \u03b2 strands which most likely adopt a homotrimer formation. Using cell fractionation, Triton X\u2010114 phase partitioning, heat modifiability, and chemical and detergent release assays, we found evidence of amphiphilic integral membrane\u2010associated oligomerization for both native MspA and MspTL in intact spirochetes. Proteinase K accessibility and immunofluorescence assays demonstrate surface exposure of MspA and MspTL. Functionally, purified recombinant MspA or MspTL monomer proteins can impair neutrophil chemotaxis. Expressions of MspA or MspTL with a PelB leader sequence in\n                    <jats:italic>Escherichia coli<\/jats:italic>\n                    also demonstrate surface exposure and can impair neutrophil chemotaxis in an in vivo air pouch model of inflammation. Collectively, our data demonstrate that MspA and MspTL membrane proteins can contribute to pathogenesis of these understudied oral spirochete species.\n                  <\/jats:p>","DOI":"10.1111\/omi.12484","type":"journal-article","created":{"date-parts":[[2024,9,12]],"date-time":"2024-09-12T09:18:57Z","timestamp":1726132737000},"page":"17-36","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":5,"title":["Topology and functional characterization of major outer membrane proteins of\n                    <i>Treponema maltophilum<\/i>\n                    and\n                    <i>Treponema lecithinolyticum<\/i>"],"prefix":"10.1111","volume":"40","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-7005-4288","authenticated-orcid":false,"given":"Natalie K.","family":"Anselmi","sequence":"first","affiliation":[{"name":"Department of Oral Biology, School of Dental Medicine University at Buffalo, The State University of New York  Buffalo New York USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Stephen T.","family":"Vanyo","sequence":"additional","affiliation":[{"name":"Department of Oral Biology, School of Dental Medicine University at Buffalo, The State University of New York  Buffalo New York USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5939-736X","authenticated-orcid":false,"given":"Nicholas D.","family":"Clark","sequence":"additional","affiliation":[{"name":"Department of Structural Biology, Jacobs School of Medicine and Biomedical Sciences University at Buffalo, The State University of New York  Buffalo New York USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0904-4387","authenticated-orcid":false,"given":"Dayron M. 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