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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1979 Aug;76(8):3765–3768. doi: 10.1073/pnas.76.8.3765

Amino acid sequence and physicochemical similarities between streptococcal M protein and mammalian tropomyosin.

B Hosein, M McCarty, V A Fischetti
PMCID: PMC383914  PMID: 386347

Abstract

The amino-terminal sequences of two peptides of type 24 streptococcal M protein show similarities with that of rabbit skeletal muscle tropomyosin, having up to 40% identical residues and probabilities of occurring by chance as low as P less than 10(-5). In addition, a hexapeptide (Glu-Ala-Glu-Lys-Ala-Ala) that is found five times in the M24 protein was shown to be identical to a sequence in tropomyosin. Similarities are also seen in the amino acid compositions and physicochemical properties of the two proteins. The amino-terminal sequences of peptides from another bacterial surface protein, staphylococcal protein A, are highly correlated with segments of two other myofibrillar proteins, rabbit actin (P less than 10(-7)) and rabbit myosin A1 light chain (P less than 10(-6)). The data presented suggest that a close structural relationship exists between mammalian muscle proteins and the biologically active surface proteins of staphylococci and streptococci. In addition, the correlation between sequences in M protein and tropomyosin represents direct evidence of a structural similarity at a molecular level between a streptococcal protein and a mammalian muscle component and may therefore prove relevant to the pathogenicity of the streptococcus.

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Selected References

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