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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1035075
- author
- 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
- organization
- publishing date
- 2008
- 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
- 2016-04-01 11:44:13
- date last changed
- 2022-01-26 17:28:49
@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}},
doi = {{10.1111/j.1365-2958.2007.05974.x}},
volume = {{67}},
year = {{2008}},
}