{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,24]],"date-time":"2026-09-24T17:27:07Z","timestamp":1790270827030,"version":"4.1.0"},"reference-count":81,"publisher":"Wiley","issue":"1","license":[{"start":{"date-parts":[[2016,10,27]],"date-time":"2016-10-27T00:00:00Z","timestamp":1477526400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Molecular Microbiology"],"published-print":{"date-parts":[[2017,1]]},"abstract":"<jats:title>Summary<\/jats:title><jats:p>While protein glycosylation has been reported in several spirochetes including the syphilis bacterium <jats:italic>Treponema pallidum<\/jats:italic> and Lyme disease pathogen <jats:italic>Borrelia burgdorferi<\/jats:italic>, the pertinent glycan structures and their roles remain uncharacterized. Herein, a novel glycan with an unusual chemical composition and structure in the oral spirochete <jats:italic>Treponema denticola<\/jats:italic>, a keystone pathogen of periodontitis was reported. The identified glycan of mass 450.2 Da is composed of a monoacetylated nonulosonic acid (Non) with a novel extended N7 acyl modification, a 2\u2010methoxy\u20104,5,6\u2010trihydroxy\u2010hexanoyl residue in which the Non has a pseudaminic acid configuration (L\u2010<jats:italic>glycero<\/jats:italic>\u2010L\u2010<jats:italic>manno<\/jats:italic>) and is <jats:bold>\u03b2<\/jats:bold>\u2010linked to serine or threonine residues. This novel glycan modifies the flagellin proteins (FlaBs) of <jats:italic>T. denticola<\/jats:italic> by <jats:italic>O<\/jats:italic>\u2010linkage at multiple sites near the D1 domain, a highly conserved region of bacterial flagellins that interact with Toll\u2010like receptor 5. Furthermore, mutagenesis studies demonstrate that the glycosylation plays an essential role in the flagellar assembly and motility of <jats:italic>T. denticola<\/jats:italic>. To our knowledge, this novel glycan and its unique modification sites have not been reported previously in any bacteria.<\/jats:p>","DOI":"10.1111\/mmi.13544","type":"journal-article","created":{"date-parts":[[2016,10,7]],"date-time":"2016-10-07T12:09:41Z","timestamp":1475842181000},"page":"67-85","source":"Crossref","is-referenced-by-count":37,"title":["A novel glycan modifies the flagellar filament proteins of the oral bacterium <i><scp>T<\/scp>reponema denticola<\/i>"],"prefix":"10.1111","volume":"103","author":[{"given":"Kurni","family":"Kurniyati","sequence":"first","affiliation":[{"name":"Department of Oral Biology The State University of New York at Buffalo New York NY 14214 USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"John F.","family":"Kelly","sequence":"additional","affiliation":[{"name":"Vaccine Program, Human Health Therapeutics, National Research Council Ottawa Ontario K1A 0R6 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