Abstract
Partial sequences of three immunologically distinct group A streptococcal M proteins (M5, M6, and M24) revealed significant homology with each other, certain amino acid residues being conserved within the three molecules. In addition, a common feature of the sequenced regions of these M proteins was their high alpha-helical potential and the presence of a repeating seven residue periodicity that is characteristic of the double helical coiled-coil molecule, tropomyosin. The existence of a tropomyosin-like seven residue periodicity strongly suggests that regions of these three M proteins may participate in intra- and/or intermolecular coiled-coil interactions. Because of the constraints imposed by such a repeating periodicity, certain conserved residues within the M proteins would occupy spatially equivalent positions in the tertiary structure of these molecules. This common characteristic could play an important role in the common antiphagocytic property of the immunologically diverse M molecules. In addition to similarities in the secondary structure of M proteins and tropomyosin, significant sequence homology has also been observed between certain regions of these molecules with up to 50% identical residues. As a result of the striking structural similarity with tropomyosin, M proteins may play a regulatory role in the contractile mechanisms involved in phagocytosis.