The streptococcal M protein: a highly versatile molecule

Interaction of the M-protein of group A Streptococcus (GAS) with its numerous host binding partners might assist the bacteria in evading host immune responses. Although the extensive diversity of this protein has been highlighted by different GAS typing schemes, most of the structural and functional...

Full description

Saved in:
Bibliographic Details
Published in:Trends in microbiology (Regular ed.) 2010-06, Vol.18 (6), p.275-282
Main Authors: Smeesters, Pierre R, McMillan, David J, Sriprakash, Kadaba S
Format: Article
Language:English
Subjects:
Antigens, Bacterial - chemistry
Antigens, Bacterial - immunology
Antigens, Bacterial - metabolism
Bacterial Adhesion
Bacterial Outer Membrane Proteins - chemistry
Bacterial Outer Membrane Proteins - immunology
Bacterial Outer Membrane Proteins - metabolism
Carrier Proteins - chemistry
Carrier Proteins - immunology
Carrier Proteins - metabolism
Fibrinolysis
Humans
Immune response
Immunoglobulins - immunology
Immunoglobulins - metabolism
Inflammation - immunology
Inflammation - microbiology
Internal Medicine
Kininogens - metabolism
Ligands
Protein Conformation
Streptococcal Infections - immunology
Streptococcal Infections - metabolism
Streptococcal Infections - microbiology
Streptococcus
Streptococcus pyogenes - chemistry
Streptococcus pyogenes - genetics
Streptococcus pyogenes - immunology
Streptococcus pyogenes - metabolism
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Interaction of the M-protein of group A Streptococcus (GAS) with its numerous host binding partners might assist the bacteria in evading host immune responses. Although the extensive diversity of this protein has been highlighted by different GAS typing schemes, most of the structural and functional information has been obtained from a limited number of types. Increasing numbers of epidemiological, clinical and biological reports suggest that the structure and function of the M protein is less conserved than previously thought. This review focuses on the known interactions between M proteins and host ligand proteins, emphasizing that our understanding of this well-studied molecule is fragmented.
ISSN:0966-842X
1878-4380
DOI:10.1016/j.tim.2010.02.007