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Volume 62, Issue 7

Identification and characterization of a new cell surface protein possessing factor H-binding activity in the swine pathogen and zoonotic agent Free

Abstract

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 serotype 2. The capacity of to bind the complement regulator factor H on its surface was demonstrated by ELISA. Using a factor I–cofactor assay, it was found that the functional activity of factor H bound to was kept. Since the product of gene in P1/7 shared similarity with a protein (named PspC) possessing factor H-binding activity, it was proposed as a putative factor H receptor in 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 α-helix domain, a proline-rich region and a G5 domain. The gene was cloned in 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 -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 cell surface protein that binds the complement factor H. This cell surface protein may help to resist complement attack and phagocytosis and contribute to pathogenesis.

  • Received:
  • Accepted:
  • Published Online:
© 2013 SGM
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/content/journal/jmm/10.1099/jmm.0.057877-0
2013-07-01
2024-04-19
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Identification and characterization of a new cell surface protein possessing factor H-binding activity in the swine pathogen and zoonotic agent Streptococcus suis
J. Med. Microbiol. 62, 1073 (2013); https://doi.org/10.1099/jmm.0.057877-0
/content/journal/jmm/10.1099/jmm.0.057877-0
/content/journal/jmm/10.1099/jmm.0.057877-0
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