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首页> 外文期刊>Infection and immunity >M-Ficolin Binds Selectively to the Capsular Polysaccharides of Streptococcus pneumoniae Serotypes 19B and 19C and of a Streptococcus mitis Strain
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M-Ficolin Binds Selectively to the Capsular Polysaccharides of Streptococcus pneumoniae Serotypes 19B and 19C and of a Streptococcus mitis Strain

机译：M-Ficolin选择性地绑定到肺炎链球菌血清型19B和19C以及肺炎链球菌菌株的荚膜多糖。

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The three human ficolins (H-, L-, and M-ficolins) and mannan-binding lectin are pattern recognition molecules of the innate immune system mediating activation of the lectin pathway of the complement system. These four human proteins bind to some microorganisms and may be involved in the resolution of infections. We investigated binding selectivity by examining the binding of M-ficolin to a panel of more than 100 different streptococcal strains (Streptococcus pneumoniae and Streptococcus mitis), each expressing distinct polysaccharide structures. M-ficolin binding was observed for three strains only: strains of the pneumococcal serotypes 19B and 19C and a single S. mitis strain expressing a similar polysaccharide structure. The bound M-ficolin, in association with MASP-2, mediated the cleavage of complement factor C4. Binding to the bacteria was inhibitable by N-acetylglucosamine, indicating that the interaction with the bacterial surface takes place via the fibrinogen-like domain. The common N-acetylmannosamine residue present in the structures of the four capsular polysaccharides of group 19 is linked via a phosphodiester bond. This residue is apparently not a ligand for M-ficolin, since the lectin binds to two of the group 19 polysaccharides only. M-ficolin bound strongly to serotype 19B and 19C polysaccharides. In contrast to those of serotypes 19A and 19F, serotype 19B and 19C polysaccharides contain an extra N-acetylmannosamine residue linked via glycoside linkage only. Thus, this extra residue seems to be the M-ficolin ligand. In conclusion, we were able to demonstrate specific binding of M-ficolin to some capsular polysaccharides of the opportunistic pathogen S. pneumoniae and of the commensal bacterium S. mitis.
机译：三种人纤维蛋白（H-，L-和M-纤维蛋白）和甘露聚糖结合的凝集素是先天免疫系统的模式识别分子，介导补体系统的凝集素途径的激活。这四种人类蛋白质与某些微生物结合，可能参与感染的解决。我们通过检查M-纤维胶凝蛋白与一组100多种不同的链球菌菌株（肺炎链球菌和肺炎链球菌）的结合来研究结合选择性，每种菌株均表达不同的多糖结构。仅在三种菌株中观察到了M-纤维胶凝蛋白的结合：肺炎球菌血清型19B和19C的菌株以及表达相似多糖结构的单个链球菌。结合的M-纤维胶蛋白与MASP-2结合，介导补体因子C4的裂解。 N-乙酰氨基葡糖可抑制与细菌的结合，表明与细菌表面的相互作用是通过纤维蛋白原样结构域发生的。存在于第19组的四个荚膜多糖结构中的常见N-乙酰甘露糖胺残基通过磷酸二酯键连接。该残基显然不是M-纤维胶凝蛋白的配体，因为凝集素仅结合19族多糖中的两个。 M-纤维胶凝蛋白与血清型19B和19C多糖牢固结合。与血清型19A和19F的那些相反，血清型19B和19C的多糖仅包含通过糖苷键连接的额外的N-乙酰甘露糖胺残基。因此，该额外的残基似乎是M-费柯林配体。总之，我们能够证明M-纤维胶凝蛋白与机会性病原体肺炎链球菌和共生细菌S. mitis的某些荚膜多糖特异性结合。

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