{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,4]],"date-time":"2026-10-04T05:59:57Z","timestamp":1791093597969,"version":"4.1.0"},"reference-count":40,"publisher":"American Society for Microbiology","issue":"12","license":[{"start":{"date-parts":[[2012,12,1]],"date-time":"2012-12-01T00:00:00Z","timestamp":1354320000000},"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":[[2012,12]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            The type IV pilus of\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Neisseria meningitidis<\/jats:named-content>\n            is the major factor for meningococcal adhesion to host cells. In this study, we showed that a mutant of\n            <jats:italic>N. meningitidis pilV<\/jats:italic>\n            , a minor pilin protein, internalized less efficiently to human endothelial and epithelial cells than the wild-type strain. Matrix-assisted laser desorption ionization\u2013time of flight mass spectrometry and electrospray ionization tandem mass spectrometry analyses showed that PilE, the major subunit of pili, was less glycosylated at its serine 62 residue (Ser62) in the \u0394\n            <jats:italic>pilV<\/jats:italic>\n            mutant than in the\n            <jats:italic>pilV<\/jats:italic>\n            <jats:sup>+<\/jats:sup>\n            strain, whereas phosphoglycerol at PilE Ser93 and phosphocholine at PilE Ser67 were not changed. Introduction of the\n            <jats:italic>pglL<\/jats:italic>\n            mutation, which results in complete loss of O-linked glycosylation from Ser62, slightly reduced\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">N. meningitidis<\/jats:named-content>\n            internalization into human brain microvascular endothelial cells, whereas the addition of the \u0394\n            <jats:italic>pilV<\/jats:italic>\n            mutation greatly reduced\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">N. meningitidis<\/jats:named-content>\n            internalization. The accumulation of ezrin, which is part of the cytoskeleton ERM family, was observed with\n            <jats:italic>pilV<\/jats:italic>\n            <jats:sup>+<\/jats:sup>\n            , \u0394\n            <jats:italic>pglL<\/jats:italic>\n            , and\n            <jats:italic>pilE<\/jats:italic>\n            (S62A) strains but not with the \u0394\n            <jats:italic>pilV<\/jats:italic>\n            mutant. These results suggested that whereas\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">N. meningitidis<\/jats:named-content>\n            pilin originally had an adhesive activity that was less affected by minor pilin proteins, the invasive function evolved with incorporation of the PilV protein into the pili to promote the\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">N. meningitidis<\/jats:named-content>\n            internalization into human cells.\n          <\/jats:p>","DOI":"10.1128\/iai.00423-12","type":"journal-article","created":{"date-parts":[[2012,9,18]],"date-time":"2012-09-18T05:59:52Z","timestamp":1347947992000},"page":"4154-4166","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":26,"title":["Meningococcal PilV Potentiates Neisseria meningitidis Type IV Pilus-Mediated Internalization into Human Endothelial and Epithelial Cells"],"prefix":"10.1128","volume":"80","author":[{"given":"Hideyuki","family":"Takahashi","sequence":"first","affiliation":[{"name":"Department of Bacteriology I, National Institute of Infectious Diseases, Tokyo, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tatsuo","family":"Yanagisawa","sequence":"additional","affiliation":[{"name":"RIKEN Systems and Structural Biology Center, Tsurumi, Yokohama, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kwang Sik","family":"Kim","sequence":"additional","affiliation":[{"name":"Division of Pediatric Infectious Diseases, Department of Pediatrics, School of Medicine, John Hopkins University, Baltimore, Maryland, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Shigeyuki","family":"Yokoyama","sequence":"additional","affiliation":[{"name":"RIKEN Systems and Structural Biology Center, Tsurumi, Yokohama, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Makoto","family":"Ohnishi","sequence":"additional","affiliation":[{"name":"Department of Bacteriology I, National Institute of Infectious Diseases, Tokyo, 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