title: The antibacterial activity of peptides derived from human beta-2 glycoprotein I is inhibited by protein H and M1 protein from Streptococcus pyogenes.
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.
authors: Division of Infection Medicine, Department of Clinical Sciences, Lund University, Lund, Sweden. maria_e.nilsson@hotmail.com
authors: Maria
authors: M
authors: Nilsson
authors: Sylwia
authors: S
authors: Wasylik
authors: Matthias
authors: M
authors: Mörgelin
authors: Anders I
authors: AI
authors: Olin
authors: Joost C M
authors: JC
authors: Meijers
authors: Ronald H W M
authors: RH
authors: Derksen
authors: Philip G
authors: PG
authors: de Groot
authors: Heiko
authors: H
authors: Herwald
mesh_terms: 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*
chemical_list: 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