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Department of Clinical Sciences, Division of Infection Medicine, Lund University, Lund, Sweden
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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1 This work was supported by the Swedish Research Council (Projects 7144 and 7480), Swedish Government Funds for Clinical Research (ALF), Swedish Society for Medical Research, Royal Physiographic Society (Lund), Foundations of Greta and Johan Kock, Torsten and Ragnar Söderberg, Alfred Österlund, the Blood and Defence Network, Lund University, the Crafoord Foundation, the Thelma Zoéga Foundation, and Hansa Medical AB.
2 Address correspondence and reprint requests to Dr. Bo Åkerström or Dr. Lars Björck, Lund University, BMC, B14, Solvegatan 19, SE-22184, Lund, Sweden. E-mail addresses: bo.akerstrom{at}med.lu.se and lars.bjorck{at}med.lu.se
3 Abbreviations used in this paper: TH, Todd-Hewitt; FXa, factor Xa; PBSAT, PBS containing 0.02% (w/v) of NaN3 and 0.05% of Tween 20; PVDF, polyvinylidene difluoride; SPRIA, solid-phase RIA.
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