Streptococcal M1 protein constructs a pathological host fibrinogen network
نویسندگان
چکیده
منابع مشابه
Fibrinogen Precipitation by Streptococcal M Protein
Evidence confirming the identity of fibrinogen-precipitating factor and streptococcal M protein is provided by the demonstration of bactericidal, mouse protective, and long chain-producing antibodies in the sera of rabbits immunized with washed M-fibrinogen precipitates. Two precipitin lines were observed in immunoelectrophoresis of human plasma vs. rabbit anti-M-fibrinogen antiserum; no precip...
متن کاملStreptococcal M1 Strikes by Neutralizing Cathelicidins.
Virulent group A streptococci have become a serious threat, with the emergence of the hypervirulent lineage M1T1. In this issue of Cell Host & Microbe, LaRock et al. (2015), uncover a role for the streptococcal M1 protein in neutralizing a key human antimicrobial peptide, cathelicidin.
متن کاملGroup A Streptococcal M1 Protein Provides Resistance against the Antimicrobial Activity of Histones
Histones are essential elements of chromatin structure and gene regulation in eukaryotes. An unexpected attribute of these nuclear proteins is their antimicrobial activity. A framework for histone release and function in host defense in vivo was revealed with the discovery of neutrophil extracellular traps, a specialized cell death process in which DNA-based structures containing histones are e...
متن کاملGroup A Streptococcal M1 Protein Sequesters Cathelicidin to Evade Innate Immune Killing.
The antimicrobial peptide LL-37 is generated upon proteolytic cleavage of cathelicidin and limits invading pathogens by directly targeting microbial membranes as well as stimulating innate immune cell function. However, some microbes evade LL-37-mediated defense. Notably, group A Streptococcus (GAS) strains belonging to the hypervirulent M1T1 serogroup are more resistant to human LL-37 than oth...
متن کاملM1 protein allows Group A streptococcal survival in phagocyte extracellular traps through cathelicidin inhibition.
M1 protein contributes to Group A Streptococcus (GAS) systemic virulence by interfering with phagocytosis and through proinflammatory activities when released from the cell surface. Here we identify a novel role of M1 protein in the stimulation of neutrophil and mast cell extracellular trap formation, yet also subsequent survival of the pathogen within these DNA-based innate defense structures....
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Nature
سال: 2011
ISSN: 0028-0836,1476-4687
DOI: 10.1038/nature09967