Bacterial surface protein L binds and inactivates neutrophil proteins S100A8/A9.

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Abstract

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.

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  • Immunology in the medical area
Original languageEnglish
Pages (from-to)4583-4592
JournalJournal of immunology (Baltimore, Md. : 1950)
Volume183
Issue number7
Publication statusPublished - 2009
Publication categoryResearch
Peer-reviewedYes