Structure, function, and genetics of streptococcal M protein.

Abstract

Streptococcal M protein is a coiled-coil fibrillar structure extending about 60 nm from the cell wall. From DNA sequencing of the M6 protein gene, it has been determined that the C-terminal end contains a membrane anchor and an adjacent cell wall stabilization domain, both of which are similar to C-terminal regions of surface proteins in other gram-positive organisms. Studies with monoclonal antibodies revealed that the C-terminal half of the protein is conserved among M proteins of different serotypes, whereas the N-terminal half varies. The M protein contains tandem repeats, which, through homologous recombination, are responsible for the observed size variation of the M proteins from different streptococcal strains. M protein size mutants occur in a laboratory-grown culture at a frequency of 1/2,000 colony-forming units. DNA sequence analysis of the M gene in size mutants derived from a single strain suggests that sequence changes which result from homologous recombination may play a role in the antigenic variation of M protein.