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

Bo Akerström1, Lars Björck

  • 1Department of Clinical Sciences, Division of Infection Medicine, Lund University, BMC, B14, Solvegatan 19, Lund SE-22184, Sweden. bo.akerstrom@med.lu.se

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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