{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,11,6]],"date-time":"2025-11-06T12:05:12Z","timestamp":1762430712228},"reference-count":25,"publisher":"Microbiology Society","issue":"7","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2013,7,1]]},"abstract":"<jats:p>\n                  <jats:italic>Streptococcus suis<\/jats:italic> is a major swine pathogen and an emerging zoonotic agent. The ability of pathogenic bacteria to bind the complement regulator factor H on their cell surface may allow them to avoid complement attack and phagocytosis. The aim of this study was to characterize a new cell surface protein possessing factor H-binding activity in <jats:italic>S. suis<\/jats:italic> serotype 2. The capacity of <jats:italic>S. suis<\/jats:italic> to bind the complement regulator factor H on its surface was demonstrated by ELISA. Using a factor I\u2013cofactor assay, it was found that the functional activity of factor H bound to <jats:italic>S. suis<\/jats:italic> was kept. Since the product of gene <jats:italic>SSU0186<\/jats:italic> in <jats:italic>S. suis<\/jats:italic> P1\/7 shared similarity with a <jats:italic>Streptococcus pneumoniae<\/jats:italic> protein (named PspC) possessing factor H-binding activity, it was proposed as a putative factor H receptor in <jats:italic>S. suis. SSU0186<\/jats:italic> has a 1686 bp open reading frame encoding a 561 amino acid protein containing the Gram-positive cell wall anchoring motif (LPXTG) at the carboxy-terminal, an amino-terminal signal sequence, an \u03b1-helix domain, a proline-rich region and a G5 domain. The <jats:italic>SSU0186<\/jats:italic> gene was cloned in <jats:italic>Escherichia coli<\/jats:italic> and the purified recombinant factor H-binding protein showed a molecular mass of 95 kDa, as determined by SDS-PAGE. The protein possessed the functional property of binding factor H. Sera from <jats:italic>S. suis<\/jats:italic>-infected pigs reacted with the recombinant factor H receptor, suggesting that it is produced during the course of infections. In conclusion, we identified a novel <jats:italic>S. suis<\/jats:italic> cell surface protein that binds the complement factor H. This cell surface protein may help <jats:italic>S. suis<\/jats:italic> to resist complement attack and phagocytosis and contribute to pathogenesis.<\/jats:p>","DOI":"10.1099\/jmm.0.057877-0","type":"journal-article","created":{"date-parts":[[2013,4,26]],"date-time":"2013-04-26T01:49:11Z","timestamp":1366940951000},"page":"1073-1080","source":"Crossref","is-referenced-by-count":18,"title":["Identification and characterization of a new cell surface protein possessing factor H-binding activity in the swine pathogen and zoonotic agent Streptococcus suis"],"prefix":"10.1099","volume":"62","author":[{"given":"Katy","family":"Vaillancourt","sequence":"first","affiliation":[{"name":"Groupe de Recherche en \u00c9cologie Buccale (GREB), Facult\u00e9 de M\u00e9decine Dentaire, Universit\u00e9 Laval, Quebec City, Quebec, Canada"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Laetitia","family":"Bonifait","sequence":"additional","affiliation":[{"name":"Centre de Recherche en 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