{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,2]],"date-time":"2026-10-02T09:26:03Z","timestamp":1790933163134,"version":"4.1.0"},"reference-count":43,"publisher":"American Society for Microbiology","issue":"18","license":[{"start":{"date-parts":[[2007,9,15]],"date-time":"2007-09-15T00:00:00Z","timestamp":1189814400000},"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":["J Bacteriol"],"published-print":{"date-parts":[[2007,9,15]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            Type IV pili (TFP) play central roles in the expression of many phenotypes including motility, multicellular behavior, sensitivity to bacteriophages, natural genetic transformation, and adherence. In\n            <jats:italic>Neisseria gonorrhoeae<\/jats:italic>\n            , these properties require ancillary proteins that act in conjunction with TFP expression and influence organelle dynamics. Here, the intrinsic contributions of the pilin protein itself to TFP dynamics and associated phenotypes were examined by expressing the\n            <jats:italic>Pseudomonas aeruginosa<\/jats:italic>\n            PilA\n            <jats:sup>PAK<\/jats:sup>\n            pilin subunit in\n            <jats:italic>N. gonorrhoeae<\/jats:italic>\n            . We show here that, although PilA\n            <jats:sup>PAK<\/jats:sup>\n            pilin can be readily assembled into TFP in this background, steady-state levels of purifiable fibers are dramatically reduced relative those of endogenous pili. This defect is due to aberrant TFP dynamics as it is suppressed in the absence of the PilT pilus retraction ATPase. Functionally, PilA\n            <jats:sup>PAK<\/jats:sup>\n            pilin complements gonococcal adherence for human epithelial cells but only in a\n            <jats:italic>pilT<\/jats:italic>\n            background, and this property remains dependent on the coexpression of both the PilC adhesin and the PilV pilin-like protein. Since\n            <jats:italic>P. aeruginosa<\/jats:italic>\n            pilin only moderately supports neisserial sequence-specific transformation despite its assembly proficiency, these results together suggest that PilA\n            <jats:sup>PAK<\/jats:sup>\n            pilin functions suboptimally in this environment. This appears to be due to diminished compatibility with resident proteins essential for TFP function and dynamics. Despite this, PilA\n            <jats:sup>PAK<\/jats:sup>\n            pili support retractile force generation in this background equivalent to that reported for endogenous pili. Furthermore, PilA\n            <jats:sup>PAK<\/jats:sup>\n            pili are both necessary and sufficient for bacteriophage PO4 binding, although the strain remains phage resistant. Together, these findings have significant implications for TFP biology in both\n            <jats:italic>N. gonorrhoeae<\/jats:italic>\n            and\n            <jats:italic>P. aeruginosa<\/jats:italic>\n            .\n          <\/jats:p>","DOI":"10.1128\/jb.00407-07","type":"journal-article","created":{"date-parts":[[2007,6,16]],"date-time":"2007-06-16T11:57:59Z","timestamp":1181995079000},"page":"6676-6685","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":32,"title":["<i>Pseudomonas aeruginosa<\/i>\n            Type IV Pilus Expression in\n            <i>Neisseria gonorrhoeae<\/i>\n            : Effects of Pilin Subunit Composition on Function and Organelle Dynamics"],"prefix":"10.1128","volume":"189","author":[{"given":"Hanne C.","family":"Winther-Larsen","sequence":"first","affiliation":[{"name":"Centre for Molecular Biology and Neuroscience"},{"name":"Department of Molecular Biosciences, University of Oslo, 0316 Oslo, Norway"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Matthew C.","family":"Wolfgang","sequence":"additional","affiliation":[{"name":"Department of Microbiology and Immunology, University of North Carolina School of Medicine, Chapel Hill, North Carolina 27599"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jos P. M.","family":"van Putten","sequence":"additional","affiliation":[{"name":"Department of Infectious Diseases and Immunology, Utrecht University, NL-3584 CL, Utrecht, The Netherlands"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Norbert","family":"Roos","sequence":"additional","affiliation":[{"name":"Department of Molecular Biosciences, University of Oslo, 0316 Oslo, Norway"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Finn Erik","family":"Aas","sequence":"additional","affiliation":[{"name":"Centre for Molecular Biology and Neuroscience"},{"name":"Department of Molecular Biosciences, University of Oslo, 0316 Oslo, Norway"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Wolfgang M.","family":"Egge-Jacobsen","sequence":"additional","affiliation":[{"name":"Centre for Molecular Biology and Neuroscience"},{"name":"Department of Molecular Biosciences, University of Oslo, 0316 Oslo, Norway"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Berenike","family":"Maier","sequence":"additional","affiliation":[{"name":"Department of Biological Sciences, Columbia University, New York, New York 10027"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Michael","family":"Koomey","sequence":"additional","affiliation":[{"name":"Centre for Molecular Biology and Neuroscience"},{"name":"Department of Molecular Biosciences, University of Oslo, 0316 Oslo, Norway"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"crossref","first-page":"69","DOI":"10.1111\/j.1365-2958.2006.05482.x","volume":"63","year":"2007","unstructured":"Aas, F. E., H. C. Winther-Larsen, M. Wolfgang, S. Frye, C. L\u00f8vold, N. Roos, J. P. van Putten, and M. Koomey. 2007. Substitutions in the N-terminal alpha helical spine of Neisseria gonorrhoeae pilin affect type IV pilus assembly, dynamics, and associated functions. Mol. Microbiol. 63 : 69-85.","journal-title":"Mol. Microbiol."},{"key":"e_1_3_2_3_2","doi-asserted-by":"crossref","first-page":"749","DOI":"10.1046\/j.1365-2958.2002.03193.x","volume":"46","year":"2002","unstructured":"Aas, F. E., M. Wolfgang, S. Frye, S. Dunham, C. L\u00f8vold, and M. Koomey. 2002. Competence for natural transformation in Neisseria gonorrhoeae: components of DNA binding and uptake linked to type IV pilus expression. Mol. Microbiol. 46 : 749-760.","journal-title":"Mol. 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