{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,23]],"date-time":"2026-10-23T22:31:08Z","timestamp":1792794668709,"version":"4.5.0"},"reference-count":53,"publisher":"Wiley","issue":"6","license":[{"start":{"date-parts":[[2006,5,9]],"date-time":"2006-05-09T00:00:00Z","timestamp":1147132800000},"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":[[2006,6]]},"abstract":"<jats:title>Summary<\/jats:title><jats:p> <jats:italic>Streptococcus agalactiae<\/jats:italic>[group B streptococcus (GBS)] is the leading cause of neonatal pneumonia, sepsis and meningitis. An <jats:italic>in silico<\/jats:italic> genome analysis indicated that GBS strain NEM316 encodes five putative sortases, including the major class A sortase enzyme and four class C sortases. The genes encoding the class C sortases are tandemly arranged in two different loci, <jats:italic>srtC1\u2010C2<\/jats:italic> and <jats:italic>srtC3\u2010C4<\/jats:italic>, with a similar genetic organization and are thought to be involved in pilus biosynthesis. Each pair of sortase genes is flanked by LPXTG protein encoding genes, two upstream and one downstream, and a divergently transcribed regulatory gene located upstream from this locus. We demonstrated that strain NEM316 expresses only the <jats:italic>srtC3\u2010C4<\/jats:italic> locus, which encodes three surface proteins (Gbs1474, Gbs1477 and Gbs1478) that polymerize to form appendages resembling pili. Structural and functional analysis of this locus revealed that: (i) the transcriptional activator RogB is required for expression of the <jats:italic>srtC3\u2010C4<\/jats:italic> operon; (ii) Gbs1477, and either SrtC3 or SrtC4 are absolutely required for pilus biogenesis; and (iii) GBS NEM316 pili are composed of three surface proteins, Gbs1477, the <jats:italic>bona fide<\/jats:italic> pilin which is the major component, Gbs1474, a minor associated component, and Gbs1478, a pilus\u2010associated adhesin. Surprisingly, pilus\u2010like structures can be formed in the absence of the two minor components, i.e. the putative anchor Gbs1474 or the adhesin Gbs1478. Adherence assays showed that Gbs1478 confers adhesive capacity to the pilus. This study provides the first evidence that adhesive pili are also present in Gram\u2010positive pathogens.<\/jats:p>","DOI":"10.1111\/j.1365-2958.2006.05190.x","type":"journal-article","created":{"date-parts":[[2006,5,9]],"date-time":"2006-05-09T10:56:55Z","timestamp":1147172215000},"page":"1401-1413","source":"Crossref","is-referenced-by-count":231,"title":["Assembly and role of pili in group B streptococci"],"prefix":"10.1111","volume":"60","author":[{"given":"Shaynoor","family":"Dramsi","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Elise","family":"Caliot","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Isabelle","family":"Bonne","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"St\u00e9phanie","family":"Guadagnini","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Marie\u2010Christine","family":"Pr\u00e9vost","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mila","family":"Kojadinovic","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lila","family":"Lalioui","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Claire","family":"Poyart","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Patrick","family":"Trieu\u2010Cuot","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2006,5,9]]},"reference":[{"key":"e_1_2_6_2_1","doi-asserted-by":"publisher","DOI":"10.1128\/JB.184.8.2181-2191.2002"},{"key":"e_1_2_6_3_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.0511017103"},{"key":"e_1_2_6_4_1","doi-asserted-by":"publisher","DOI":"10.1128\/IAI.70.6.2869-2876.2002"},{"key":"e_1_2_6_5_1","doi-asserted-by":"publisher","DOI":"10.1128\/jb.175.11.3628-3635.1993"},{"key":"e_1_2_6_6_1","doi-asserted-by":"crossref","first-page":"840","DOI":"10.1128\/iai.52.3.840-845.1986","article-title":"A 160\u2010kilodalton epithelial cell surface glycoprotein recognized by plant lectins that inhibit the adherence of Actinomyces naeslundii","volume":"52","author":"Brennan M.J.","year":"1986","journal-title":"Infect Immun"},{"key":"e_1_2_6_7_1","doi-asserted-by":"crossref","unstructured":"Brochet M. 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