{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,27]],"date-time":"2026-09-27T10:59:25Z","timestamp":1790506765227,"version":"4.1.0"},"reference-count":48,"publisher":"American Society for Microbiology","issue":"18","license":[{"start":{"date-parts":[[2010,9,15]],"date-time":"2010-09-15T00:00:00Z","timestamp":1284508800000},"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":[[2010,9,15]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            Adhesive pili on the surface of the serotype M1\n            <jats:italic>Streptococcus pyogenes<\/jats:italic>\n            strain SF370 are composed of a major backbone subunit (Spy0128) and two minor subunits (Spy0125 and Spy0130), joined covalently by a pilin polymerase (Spy0129). Previous studies using recombinant proteins showed that both minor subunits bind to human pharyngeal (Detroit) cells (A. G. Manetti et al., Mol. Microbiol. 64:968-983, 2007), suggesting both may act as pilus-presented adhesins. While confirming these binding properties, studies described here indicate that Spy0125 is the pilus-presented adhesin and that Spy0130 has a distinct role as a wall linker. Pili were localized predominantly to cell wall fractions of the wild-type\n            <jats:italic>S. pyogenes<\/jats:italic>\n            parent strain and a\n            <jats:italic>spy0125<\/jats:italic>\n            deletion mutant. In contrast, they were found almost exclusively in culture supernatants in both\n            <jats:italic>spy0130<\/jats:italic>\n            and\n            <jats:italic>srtA<\/jats:italic>\n            deletion mutants, indicating that the housekeeping sortase (SrtA) attaches pili to the cell wall by using Spy0130 as a linker protein. Adhesion assays with antisera specific for individual subunits showed that only anti-rSpy0125 serum inhibited adhesion of wild-type\n            <jats:italic>S. pyogenes<\/jats:italic>\n            to human keratinocytes and tonsil epithelium to a significant extent. Spy0125 was localized to the tip of pili, based on a combination of mutant analysis and liquid chromatography-tandem mass spectrometry analysis of purified pili. Assays comparing parent and mutant strains confirmed its role as the adhesin. Unexpectedly, apparent spontaneous cleavage of a labile, proline-rich (8 of 14 residues) sequence separating the N-terminal \u223c1\/3 and C-terminal \u223c2\/3 of Spy0125 leads to loss of the N-terminal region, but analysis of internal\n            <jats:italic>spy0125<\/jats:italic>\n            deletion mutants confirmed that this has no significant effect on adhesion.\n          <\/jats:p>","DOI":"10.1128\/jb.00071-10","type":"journal-article","created":{"date-parts":[[2010,7,17]],"date-time":"2010-07-17T01:45:48Z","timestamp":1279331148000},"page":"4651-4659","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":49,"title":["Roles of Minor Pilin Subunits Spy0125 and Spy0130 in the Serotype M1\n            <i>Streptococcus pyogenes<\/i>\n            Strain SF370"],"prefix":"10.1128","volume":"192","author":[{"given":"Wendy D.","family":"Smith","sequence":"first","affiliation":[{"name":"Institute for Cell and Molecular Biosciences"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jonathan A.","family":"Pointon","sequence":"additional","affiliation":[{"name":"Institute for Cell and Molecular Biosciences"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Emily","family":"Abbot","sequence":"additional","affiliation":[{"name":"Institute for Cell and Molecular Biosciences"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hae Joo","family":"Kang","sequence":"additional","affiliation":[{"name":"Maurice Wilkins Centre for Molecular Biodiscovery and School of Biological Sciences, University of Auckland, Auckland, New Zealand"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Edward N.","family":"Baker","sequence":"additional","affiliation":[{"name":"Maurice Wilkins Centre for Molecular Biodiscovery and School of Biological Sciences, University of Auckland, Auckland, New Zealand"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Barry H.","family":"Hirst","sequence":"additional","affiliation":[{"name":"Institute for Cell and Molecular Biosciences"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Janet A.","family":"Wilson","sequence":"additional","affiliation":[{"name":"Institute for Cellular Medicine, Faculty of Medical Sciences, Newcastle University, Framlington Place, Newcastle upon Tyne NE2 4HH, United Kingdom"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mark J.","family":"Banfield","sequence":"additional","affiliation":[{"name":"Department of Biological Chemistry, John Innes Centre, Norwich NR4 7UH, United Kingdom"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Michael A.","family":"Kehoe","sequence":"additional","affiliation":[{"name":"Institute for Cell and Molecular Biosciences"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1462-5822.2007.00918.x"},{"key":"e_1_3_2_3_2","doi-asserted-by":"publisher","DOI":"10.1128\/JB.00384-08"},{"key":"e_1_3_2_4_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.0511017103"},{"key":"e_1_3_2_5_2","doi-asserted-by":"crossref","first-page":"495","DOI":"10.1111\/j.1365-2958.2007.05939.x","volume":"66","year":"2007","unstructured":"Budzik, J. 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