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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.

Nilsson, Maria LU ; Wasylik, Sylwia; Mörgelin, Matthias LU ; Olin, Anders LU ; Meijers, Joost C M; Derksen, Ronald H W M; de Groot, Philip G and Herwald, Heiko LU (2008) In Molecular Microbiology 67(3). 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 (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... (More)
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. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Molecular Microbiology
volume
67
issue
3
pages
482 - 492
publisher
Wiley-Blackwell
external identifiers
  • pmid:18093092
  • wos:000252175600002
  • scopus:37749036783
ISSN
1365-2958
DOI
10.1111/j.1365-2958.2007.05974.x
language
English
LU publication?
yes
id
68b3b12b-4989-4dbc-a5b1-90fbbb2e01d3 (old id 1035075)
alternative location
http://www.ncbi.nlm.nih.gov/pubmed/18093092?dopt=Abstract
date added to LUP
2009-07-27 13:58:11
date last changed
2017-10-01 03:38:40
@article{68b3b12b-4989-4dbc-a5b1-90fbbb2e01d3,
  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 (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.},
  author       = {Nilsson, Maria and Wasylik, Sylwia and Mörgelin, Matthias and Olin, Anders and Meijers, Joost C M and Derksen, Ronald H W M and de Groot, Philip G and Herwald, Heiko},
  issn         = {1365-2958},
  language     = {eng},
  number       = {3},
  pages        = {482--492},
  publisher    = {Wiley-Blackwell},
  series       = {Molecular Microbiology},
  title        = {The antibacterial activity of peptides derived from human beta-2 glycoprotein I is inhibited by protein H and M1 protein from Streptococcus pyogenes.},
  url          = {http://dx.doi.org/10.1111/j.1365-2958.2007.05974.x},
  volume       = {67},
  year         = {2008},
}