The antibacterial activity of peptides derived from human beta-2 glycoprotein I is inhibited by protein H and M1 protein from Streptococcus pyogenes.
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.
Nilsson
Maria
M
Division of Infection Medicine, Department of Clinical Sciences, Lund University, Lund, Sweden. maria_e.nilsson@hotmail.com
Wasylik
Sylwia
S
Mörgelin
Matthias
M
Olin
Anders I
AI
Meijers
Joost C M
JC
Derksen
Ronald H W M
RH
de Groot
Philip G
PG
Herwald
Heiko
H
D000900:Anti-Bacterial Agents / Q000037:antagonists & inhibitors* / Q000494:pharmacology*; D000942:Antigens, Bacterial / Q000378:metabolism*; D001425:Bacterial Outer Membrane Proteins / Q000378:metabolism*; D001426:Bacterial Proteins / Q000378:metabolism*; D002352:Carrier Proteins / Q000378:metabolism*; D004926:Escherichia coli / Q000187:drug effects / Q000648:ultrastructure; D006801:Humans; D008565:Membrane Proteins / Q000378:metabolism*; D050296:Microbial Viability; D046529:Microscopy, Electron, Transmission; D016253:Microscopy, Immunoelectron; D008954:Models, Biological; D009504:Neutrophils / Q000201:enzymology / Q000276:immunology; D011485:Protein Binding; D013211:Staphylococcus aureus / Q000187:drug effects; D013297:Streptococcus pyogenes / Q000276:immunology / Q000378:metabolism* / Q000648:ultrastructure; D053482:beta 2-Glycoprotein I / Q000037:antagonists & inhibitors* / Q000494:pharmacology*
D000900:Anti-Bacterial Agents; D000942:Antigens, Bacterial; D001425:Bacterial Outer Membrane Proteins; D001426:Bacterial Proteins; D002352:Carrier Proteins; D008565:Membrane Proteins; D053482:beta 2-Glycoprotein I; C064006:protein H, Streptococcus; C014689:streptococcal M protein