In:
Molecular Microbiology, Wiley, Vol. 67, No. 3 ( 2008-02), p. 482-492
Abstract:
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.
Type of Medium:
Online Resource
ISSN:
0950-382X
,
1365-2958
DOI:
10.1111/mmi.2008.67.issue-3
DOI:
10.1111/j.1365-2958.2007.05974.x
Language:
English
Publisher:
Wiley
Publication Date:
2008
detail.hit.zdb_id:
1501537-3
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