The antibacterial activity of peptides derived from human beta-2 glycoprotein I is inhibited by protein H and M1 protein from Streptococcus pyogenes.

Research output: Contribution to journalArticle


During the last years, the importance of antibacterial peptides has attracted considerable attention. We report here that peptides derived from the fifth domain of beta-2 glycoprotein I (beta(2)GPI), a human heparin binding plasma protein, have antibacterial activities against Gram-positive and Gram-negative bacteria. Streptococcus pyogenes, an important human pathogen that can survive and grow in human blood, has developed mechanisms to escape the attack by these peptides. Thus, protein H and M1 protein, two surface proteins of the highly pathogenic S. pyogenes AP1 strain, bind full-length beta(2)GPI and thereby prevent the processing of beta(2)GPI by proteases from polymorphonuclear neutrophils (PMNs) into antibacterial peptides. In addition, protein H and M1 protein, released from the bacterial cell wall by PMN-derived proteases, bind to, and inhibit the activity of, beta(2)GPI-derived antibacterial peptides. Taken together, the data suggest that the interaction between the streptococcal proteins and beta(2)GPI or beta(2)GPI-derived peptides presents a novel mechanism to resist an antibacterial attack by beta(2)GPI-cleavage products.


  • Maria Nilsson
  • Sylwia Wasylik
  • Matthias Mörgelin
  • Anders Olin
  • Joost C M Meijers
  • Ronald H W M Derksen
  • Philip G de Groot
  • Heiko Herwald
Research areas and keywords

Subject classification (UKÄ) – MANDATORY

  • Infectious Medicine
Original languageEnglish
Pages (from-to)482-492
JournalMolecular Microbiology
Issue number3
StatePublished - 2008
Publication categoryResearch