Bacterial Surface Protein L Binds and Inactivates Neutrophil Proteins S100A8/A9
Bacterial Surface Protein L Binds and Inactivates Neutrophil Proteins S100A8/A9
复制标题
DOI：
10.4049/jimmunol.0901487
复制
发表时间：
2009-10-01
影响因子：
4.4
通讯作者：
Bjorck, Lars
中科院分区：
文献类型：
--
作者：
Akerstrom, Bo;Bjorck, Lars
Finegoldia Magna是一种厌氧细菌，是所有非无菌身体表面正常人类菌群的一部分，但它也是一种重要的机会病原体，可引起广泛的感染。一些更常与临床感染相关的F.Magna分离株表达L蛋白，这是一种含有多个同源结构域(B1-B5)的表面蛋白，通过与Ig L链相互作用结合免疫球蛋白。本研究表明，L蛋白的N端A结构域与S100A8/A9结合，抗菌蛋白大量存在于中性粒细胞的胞浆中，但在炎症过程中也存在于组织细胞外。结果表明，表达L蛋白的麦格纳酵母不受S100A8/A9的杀伤。免疫球蛋白和S100A8/A9与L蛋白独立相互作用，表明这种细菌表面蛋白既能操纵获得性免疫防御机制，又能操纵天然免疫防御机制。免疫学杂志，2009,183：4583-4592。
Finegoldia magna is an anaerobic bacterial species that is part of the normal human flora on all nonsterile body surfaces, but it is also a significant opportunistic pathogen causing a wide range of infections. Some isolates of F. magna that are more frequently associated with clinical infection express protein L, a surface protein containing multiple homologous domains (B1-B5) that bind Igs through interactions with Ig L chains. The present study shows that the N-terminal A domain of protein L binds S100A8/A9, antibacterial proteins present in large amounts in the cytoplasm of neutrophils, but also extracellularly in tissues during inflammation. As a result, protein L-expressing F. magna are protected against killing by S100A8/A9. Igs and S100A8/A9 were found to interact independently with protein L, demonstrating that this bacterial surface protein is capable of manipulating both adaptive and innate immune defense mechanisms. The Journal of Immunology, 2009, 183: 4583-4592.