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DOI 10.1128/iai.06294-11

Медицинская библиотека · Infection and immunity · 2012

Fhb, a novel factor H-binding surface protein, contributes to the antiphagocytic ability and virulence of Streptococcus suis.

Pian Yaya, Gan Shuzhen, Wang Shujie, Guo Jie, Wang Pingping, Zheng Yuling, Cai Xuehui, Jiang Yongqiang, Yuan Yuan

СтатьяПоддержка исследования: вне правительства СШАПеревод в очереди

Аннотация

Streptococcus suis serotype 2 is a Gram-positive bacterium that causes sepsis and meningitis in piglets and humans. The mechanisms of S. suis serotype 2 invasive disease are not well understood. The surface proteins of pathogens usually play important roles in infection and bacterium-host interactions. Here, we identified a novel surface protein that contributed significantly to the virulence of S. suis serotype 2 in a piglet infection model. This protein showed little similarity to other reported proteins and exhibited strong binding activity to human factor H (hFH). It was designated Fhb (factor H-binding protein). The fhb genes found in S. suis serotypes 1, 2, 4, 7, and 9 exhibited molecular polymorphism. Fhb possessed two proline-rich repeat sequences and XPZ domains, and one repeat sequence exhibited a high homology to Bac, an IgA-binding protein of Streptococcus agalactiae. Evidence strongly indicated that fhb-deficient mutants had diminished phagocytosis resistance in bactericidal assays. In addition, Fhb plays important roles in complement-mediated immunity by interacting with hFH. These findings indicated that Fhb is a crucial surface protein contributing to the virulence of S. suis, with important functions in evading innate immune defenses by interaction with host complement regulatory factor hFH.

Для цитирования: Pian Yaya, Gan Shuzhen, Wang Shujie, Guo Jie, Wang Pingping, Zheng Yuling, Cai Xuehui, Jiang Yongqiang, Yuan Yuan. Fhb, a novel factor H-binding surface protein, contributes to the antiphagocytic ability and virulence of Streptococcus suis.. Infection and immunity. 2012. DOI: 10.1128/iai.06294-11.

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