{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,13]],"date-time":"2026-10-13T00:40:26Z","timestamp":1791852026432,"version":"4.3.4"},"reference-count":57,"publisher":"American Society for Microbiology","issue":"1","license":[{"start":{"date-parts":[[2009,1,1]],"date-time":"2009-01-01T00:00:00Z","timestamp":1230768000000},"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":[[2009,1]]},"abstract":"<jats:title>ABSTRACT<\/jats:title><jats:p><jats:italic>Chlamydia trachomatis<\/jats:italic>is a globally important obligate intracellular bacterial pathogen that is a leading cause of sexually transmitted disease and blinding trachoma. Effective control of these diseases will likely require a preventative vaccine.<jats:italic>C. trachomatis<\/jats:italic>polymorphic membrane protein D (PmpD) is an attractive vaccine candidate as it is conserved among<jats:italic>C. trachomatis<\/jats:italic>strains and is a target of broadly cross-reactive neutralizing antibodies. We show here that immunoaffinity-purified native PmpD exists as an oligomer with a distinct 23-nm flower-like structure. Two-dimensional blue native-sodium dodecyl sulfate-polyacrylamide gel electrophoresis analyses showed that the oligomers were composed of full-length PmpD (p155) and two proteolytically processed fragments, the p73 passenger domain (PD) and the p82 translocator domain. We also show that PmpD undergoes an infection-dependent proteolytic processing step late in the growth cycle that yields a soluble extended PD (p111) that was processed into a p73 PD and a novel p30 fragment. Interestingly, soluble PmpD peptides possess putative eukaryote-interacting functional motifs, implying potential secondary functions within or distal to infected cells. Collectively, our findings show that PmpD exists as two distinct forms, a surface-associated oligomer exhibiting a higher-order flower-like structure and a soluble form restricted to infected cells. We hypothesize that PmpD is a multifunctional virulence factor important in chlamydial pathogenesis and could represent novel vaccine or drug targets for the control of human chlamydial infections.<\/jats:p>","DOI":"10.1128\/iai.01173-08","type":"journal-article","created":{"date-parts":[[2008,11,11]],"date-time":"2008-11-11T01:46:12Z","timestamp":1226367972000},"page":"508-516","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":75,"title":["<i>Chlamydia trachomatis<\/i>Polymorphic Membrane Protein D Is an Oligomeric Autotransporter with a Higher-Order Structure"],"prefix":"10.1128","volume":"77","author":[{"given":"Kena A.","family":"Swanson","sequence":"first","affiliation":[{"name":"Laboratory of Intracellular Parasites"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lacey D.","family":"Taylor","sequence":"additional","affiliation":[{"name":"Laboratory of Intracellular Parasites"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Shaun D.","family":"Frank","sequence":"additional","affiliation":[{"name":"Laboratory of Intracellular Parasites"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gail L.","family":"Sturdevant","sequence":"additional","affiliation":[{"name":"Laboratory of Intracellular Parasites"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Elizabeth R.","family":"Fischer","sequence":"additional","affiliation":[{"name":"Research Technologies Branch, Rocky Mountain Laboratories, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Hamilton, Montana 59840"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"John H.","family":"Carlson","sequence":"additional","affiliation":[{"name":"Laboratory of Intracellular Parasites"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"William M.","family":"Whitmire","sequence":"additional","affiliation":[{"name":"Laboratory of Intracellular Parasites"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Harlan D.","family":"Caldwell","sequence":"additional","affiliation":[{"name":"Laboratory of Intracellular Parasites"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"publisher","DOI":"10.1046\/j.1365-2958.1998.00861.x"},{"key":"e_1_3_2_3_2","first-page":"193","volume":"3","year":"1993","unstructured":"Boulikas, T. 1993. 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