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Updated: Jun 20, 2026

Expression, Purification, and Antimicrobial Activity of S100A12
Published on: May 13, 2017
Bacterial surface protein L binds and inactivates neutrophil proteins S100A8/A9
1Department of Clinical Sciences, Division of Infection Medicine, Lund University, BMC, B14, Solvegatan 19, Lund SE-22184, Sweden. bo.akerstrom@med.lu.se
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.
Insights
Finegoldia magna, an opportunistic pathogen, uses its surface protein L to evade immune defenses. Protein L binds both immunoglobulins and S100A8/A9 antibacterial proteins, protecting the bacteria from innate and adaptive immunity.
Area of Science:
- Microbiology
- Immunology
- Bacterial Pathogenesis
Background:
- Finegoldia magna is a commensal bacterium and opportunistic pathogen.
- Certain F. magna isolates express protein L, which binds immunoglobulins (Igs) via Ig light chains.
- S100A8/A9 are antibacterial proteins found in neutrophils and extracellularly during inflammation.
Purpose of the Study:
- To investigate the interaction between F. magna protein L and S100A8/A9.
- To determine if protein L influences bacterial susceptibility to S100A8/A9.
Main Methods:
- Protein L domain analysis.
- Co-immunoprecipitation assays.
- Bacterial killing assays.
Main Results:
- The N-terminal A domain of protein L binds S100A8/A9.
- F. magna expressing protein L are protected against S100A8/A9-mediated killing.
- Protein L binds Igs and S100A8/A9 independently.
Conclusions:
- F. magna protein L actively manipulates both adaptive (Ig) and innate (S100A8/A9) immune mechanisms.
- This interaction confers bacterial resistance to host defense proteins.
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