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lüll Streptococcal M protein: molecular design and biological behavior Fischetti VAClin Microbiol Rev 1989[Jul]; 2 (3): 285-314M protein is a major virulence determinant for the group A streptococcus by virtue of its ability to allow the organism to resist phagocytosis. Common in eucaryotes, the fibrillar coiled-coil design for the M molecule may prove to be a common motif for surface proteins in gram-positive organisms. This type of structure offers the organism several distinct advantages, ranging from antigenic variation to multiple functional domains. The close resemblance of this molecular design to that of certain mammalian proteins could help explain on a molecular level the formation of epitopes responsible for serological cross-reactions between microbial and mammalian proteins. Many of the approaches described in the elucidation of the M-protein structure may be applied for characterizing similar molecules in other microbial systems.|*Antigens, Bacterial/physiology[MESH]|*Bacterial Outer Membrane Proteins[MESH]|*Bacterial Proteins/physiology/ultrastructure[MESH]|*Carrier Proteins[MESH]|Amino Acid Sequence[MESH]|Animals[MESH]|Antigenic Variation[MESH]|Bacterial Vaccines/immunology[MESH]|Cross Reactions[MESH]|Genes, Bacterial[MESH]|Humans[MESH]|Molecular Sequence Data[MESH]|Sequence Homology, Nucleic Acid[MESH]|Streptococcal Infections/prevention & control[MESH] |