期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1979
卷号：76
期号：8
页码：3765-3768
DOI：10.1073/pnas.76.8.3765
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：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.
