Bacterial Surface Protein L Binds and Inactivates Neutrophil Proteins S100A8/A9

被引:14
作者
Akerstrom, Bo [1 ]
Bjorck, Lars [1 ]
机构
[1] Lund Univ, BMC, Dept Clin Sci, Div Infect Med, SE-22184 Lund, Sweden
基金
瑞典研究理事会;
关键词
REVERSIBLE ANTIMICROBIAL ACTIVITY; KAPPA-LIGHT-CHAIN; PEPTOSTREPTOCOCCUS-MAGNUS; ESCHERICHIA-COLI; ANAEROBIC COCCI; HIGH-AFFINITY; S100; FAMILY; IN-VITRO; CALPROTECTIN; CALCIUM;
D O I
10.4049/jimmunol.0901487
中图分类号
R392 [医学免疫学]; Q939.91 [免疫学];
学科分类号
100102 ;
摘要
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.
引用
收藏
页码:4583 / 4592
页数:10
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