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Mol Microbiol. 1993 May;8(5):981-91.

Nucleotide substitutions and small-scale insertion produce size and antigenic variation in group A streptococcal M1 protein.

Author information

1
Department of Food Science and Nutrition, University of Minnesota, St. Paul 55108.

Abstract

The presence of M protein on the surface of group A streptococci (GAS) confers the ability of the cell to resist phagocytosis in the absence of type-specific antibodies. It undergoes antigenic variation with more than 80 different serotypes having been defined. We have sequenced the M protein gene (emm1.1) from strain CS190 and present evidence that individual nucleotide substitutions are responsible for sequence variation in the N-terminal non-repeat region of emm1.1 and these substitutions have altered antibody recognition of opsonic epitopes. The N-terminal non-repeat domains of two other closely related strains, 71-155 and 76-088, were found to have sequence identical to emm1.1 with the addition of a 21 bp insert. This study provides the first evidence that nucleotide substitutions and small insertions are responsible for size and antigenic variation in the N-terminal non-repeat domain of the M protein of GAS.

PMID:
8355619
[Indexed for MEDLINE]

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