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The antibacterial activity of peptides derived from human beta‐2 glycoprotein I is inhibited by protein H and M1 protein from Streptococcus pyogenes
Author(s) -
Nilsson Maria,
Wasylik Sylwia,
Mörgelin Matthias,
Olin Anders I.,
Meijers Joost C. M.,
Derksen Ronald H. W. M.,
De Groot Philip G.,
Herwald Heiko
Publication year - 2008
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.2007.05974.x
Subject(s) - biology , streptococcus pyogenes , glycoprotein , microbiology and biotechnology , beta (programming language) , antibacterial peptide , antibacterial activity , peptide , streptococcus , biochemistry , bacteria , staphylococcus aureus , genetics , computer science , programming language
Summary 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 (β 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 β 2 GPI and thereby prevent the processing of β 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, β 2 GPI‐derived antibacterial peptides. Taken together, the data suggest that the interaction between the streptococcal proteins and β 2 GPI or β 2 GPI‐derived peptides presents a novel mechanism to resist an antibacterial attack by β 2 GPI‐cleavage products.