{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,30]],"date-time":"2026-10-30T16:09:06Z","timestamp":1793376546078,"version":"4.5.0"},"reference-count":66,"publisher":"American Society for Microbiology","issue":"1","license":[{"start":{"date-parts":[[2016,1,1]],"date-time":"2016-01-01T00:00:00Z","timestamp":1451606400000},"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":[[2016,1]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            The oral Gram-negative anaerobic bacterium\n            <jats:named-content content-type=\"genus-species\">Porphyromonas gingivalis<\/jats:named-content>\n            is an important pathogen involved in chronic periodontitis. Among its virulence factors, the major extracellular proteinases, Arg-gingipain and Lys-gingipain, are of interest given their abilities to degrade host proteins and process other virulence factors. Gingipains possess C-terminal domains (CTDs) and are translocated to the cell surface or into the extracellular milieu by the type IX secretion system (T9SS). Gingipains contribute to the colonial pigmentation of the bacterium on blood agar. In this study, Omp17, the PGN_0300 gene product, was found in the outer membrane fraction. A mutant lacking Omp17 did not show pigmentation on blood agar and showed reduced proteolytic activity of the gingipains. CTD-containing proteins were released from bacterial cells without cleavage of the CTDs in the\n            <jats:italic>omp17<\/jats:italic>\n            mutant. Although synthesis of the anionic polysaccharide (A-LPS) was not affected in the\n            <jats:italic>omp17<\/jats:italic>\n            mutant, the processing of and A-LPS modification of CTD-containing proteins was defective. PorU, a C-terminal signal peptidase that cleaves the CTDs of other CTD-containing proteins, was not detected in any membrane fraction of the\n            <jats:italic>omp17<\/jats:italic>\n            mutant, suggesting that the defective maturation of CTD-containing proteins by impairment of Omp17 is partly due to loss of function of PorU. In the mouse subcutaneous infection experiment, the\n            <jats:italic>omp17<\/jats:italic>\n            mutant was less virulent than the wild type. These results suggested that Omp17 is involved in\n            <jats:named-content content-type=\"genus-species\">P. gingivalis<\/jats:named-content>\n            virulence.\n          <\/jats:p>","DOI":"10.1128\/iai.01308-15","type":"journal-article","created":{"date-parts":[[2015,10,27]],"date-time":"2015-10-27T02:14:06Z","timestamp":1445912046000},"page":"230-240","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":34,"title":["Involvement of an Skp-Like Protein, PGN_0300, in the Type IX Secretion System of Porphyromonas gingivalis"],"prefix":"10.1128","volume":"84","author":[{"given":"Yuko","family":"Taguchi","sequence":"first","affiliation":[{"name":"Department of Periodontal Science, Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama University, Okayama, 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