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.
Full text
PDF



Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Amons R., van Agthoven A., Pluijms W., Möller W. A comparison of the alanine-rich sequences of the L7/L12-ribosomal proteins from rat liver, Artemia salina and Escherichia coli, with the amino-terminal region of the alkali light chain A1 from rabbit myosin. FEBS Lett. 1978 Feb 15;86(2):282–284. doi: 10.1016/0014-5793(78)80580-8. [DOI] [PubMed] [Google Scholar]
- Bailey K. Tropomyosin: a new asymmetric protein component of the muscle fibril. Biochem J. 1948;43(2):271–279. doi: 10.1042/bj0430271. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Barker W. C., Dayhoff M. O. Evolution of lipoproteins deduced from protein sequence data. Comp Biochem Physiol B. 1977;57(4):309–315. doi: 10.1016/0305-0491(77)90060-8. [DOI] [PubMed] [Google Scholar]
- Beachey E. H., Seyer J. M., Kang A. H. Repeating covalent structure of streptococcal M protein. Proc Natl Acad Sci U S A. 1978 Jul;75(7):3163–3167. doi: 10.1073/pnas.75.7.3163. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Björk I., Petersson B. A., Sjöquist J. Some physiochemical properties of protein A from Staphylococcus aureus. Eur J Biochem. 1972 Sep 25;29(3):579–584. doi: 10.1111/j.1432-1033.1972.tb02024.x. [DOI] [PubMed] [Google Scholar]
- Collins J. H., Elzinga M. The primary structure of actin from rabbit skeletal muscle. Completion and analysis of the amino acid sequence. J Biol Chem. 1975 Aug 10;250(15):5915–5920. [PubMed] [Google Scholar]
- Deisenhofer J., Jones T. A., Huber R., Sjödahl J., Sjöquist J. Crystallization, crystal structure analysis and atomic model of the complex formed by a human Fc fragment and fragment B of protein A from Staphylococcus aureus. Hoppe Seylers Z Physiol Chem. 1978 Aug;359(8):975–985. doi: 10.1515/bchm2.1978.359.2.975. [DOI] [PubMed] [Google Scholar]
- DiRienzo J. M., Nakamura K., Inouye M. The outer membrane proteins of Gram-negative bacteria: biosynthesis, assembly, and functions. Annu Rev Biochem. 1978;47:481–532. doi: 10.1146/annurev.bi.47.070178.002405. [DOI] [PubMed] [Google Scholar]
- Dossett J. H., Kronvall G., Williams R. C., Jr, Quie P. G. Antiphagocytic effects of staphylococcal protein A. J Immunol. 1969 Dec;103(6):1405–1410. [PubMed] [Google Scholar]
- Fischetti V. A., Gotschlich E. C., Siviglia G., Zabriskie J. B. Streptococcal M protein extracted by nonionic detergent. I. Properties of the antiphagocytic and type-specific molecules. J Exp Med. 1976 Jul 1;144(1):32–53. doi: 10.1084/jem.144.1.32. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Fischetti V. A. Streptococcal M protein extracted by nonionic detergent. II. Analysis of the antibody response to the multiple antigenic determinants of the M-protein molecule. J Exp Med. 1977 Oct 1;146(4):1108–1123. doi: 10.1084/jem.146.4.1108. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Fischetti V. A. Streptococcal M protein extracted by nonionic detergent. III. Correlation between immunological cross-reactions and structural similarities with implications for antiphagocytosis. J Exp Med. 1978 Jun 1;147(6):1771–1778. doi: 10.1084/jem.147.6.1771. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Fox E. N. M proteins of group A streptococci. Bacteriol Rev. 1974 Mar;38(1):57–86. doi: 10.1128/br.38.1.57-86.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Fox E. N., Wittner M. K. New observations on the structure and antigenicity of the M proteins of the group A streptococcus. Immunochemistry. 1969 Jan;6(1):11–24. doi: 10.1016/0019-2791(69)90174-8. [DOI] [PubMed] [Google Scholar]
- Fox E. N., Wittner M. K. The multiple molecular structure of the M proteins of group A streptococci. Proc Natl Acad Sci U S A. 1965 Oct;54(4):1118–1125. doi: 10.1073/pnas.54.4.1118. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Frank G., Weeds A. G. The amino-acid sequence of the alkali light chains of rabbit skeletal-muscle myosin. Eur J Biochem. 1974 May 15;44(2):317–334. doi: 10.1111/j.1432-1033.1974.tb03489.x. [DOI] [PubMed] [Google Scholar]
- Henderson L. E., Gilden R. V., Oroszlan S. Amino acid sequence homology between histone H5 and murine leukemia virus phosphoprotein p12. Science. 1979 Mar 30;203(4387):1346–1348. doi: 10.1126/science.218289. [DOI] [PubMed] [Google Scholar]
- KAPLAN M. H. IMMUNOLOGIC RELATION OF STREPTOCOCCAL AND TISSUE ANTIGENS. I. PROPERTIES OF AN ANTIGEN IN CERTAIN STRAINS OF GROUP A STREPTOCOCCI EXHIBITING AN IMMUNOLOGIC CROSS-REACTION WITH HUMAN HEART TISSUE. J Immunol. 1963 Apr;90:595–606. [PubMed] [Google Scholar]
- LANCEFIELD R. C. Current knowledge of type-specific M antigens of group A streptococci. J Immunol. 1962 Sep;89:307–313. [PubMed] [Google Scholar]
- LANCEFIELD R. C., PERLMANN G. E. Preparation and properties of type-specific M antigen isolated from a group A, type 1 hemolytic streptococcus. J Exp Med. 1952 Jul;96(1):71–82. doi: 10.1084/jem.96.1.71. [DOI] [PMC free article] [PubMed] [Google Scholar]
- LANCEFIELD R. C. Persistence of type-specific antibodies in man following infection with group A streptococci. J Exp Med. 1959 Aug 1;110(2):271–292. doi: 10.1084/jem.110.2.271. [DOI] [PMC free article] [PubMed] [Google Scholar]
- LOWEY S. COMPARATIVE STUDY OF THE ALPHA-HELICAL MUSCLE PROTEINS. TYROSYL TITRATION AND EFFECT OF PH ON CONFORMATION. J Biol Chem. 1965 Jun;240:2421–2427. [PubMed] [Google Scholar]
- Mannherz H. G., Goody R. S. Proteins of contractile systems. Annu Rev Biochem. 1976;45:427–465. doi: 10.1146/annurev.bi.45.070176.002235. [DOI] [PubMed] [Google Scholar]
- McLachlan A. D., Stewart M., Smillie L. B. Sequence repeats in alpha-tropomyosin. J Mol Biol. 1975 Oct 25;98(2):281–291. doi: 10.1016/s0022-2836(75)80118-5. [DOI] [PubMed] [Google Scholar]
- Sjodahl J. Repetitive sequences in protein A from Staphylococcus aureus. Arrangement of five regions within the protein, four being highly homologous and Fc-binding. Eur J Biochem. 1977 Mar 1;73(2):343–351. doi: 10.1111/j.1432-1033.1977.tb11324.x. [DOI] [PubMed] [Google Scholar]
- Sjödahl J. Repetitive sequences in protein A from Staphyloccus aureus: three highly homologous Fc-binding regions. FEBS Lett. 1976 Aug 1;67(1):62–67. doi: 10.1016/0014-5793(76)80871-x. [DOI] [PubMed] [Google Scholar]
- Sjödahl J. Structural studies on the four repetitive Fc-binding regions in protein A from Staphylococcus aureus. Eur J Biochem. 1977 Sep;78(2):471–490. doi: 10.1111/j.1432-1033.1977.tb11760.x. [DOI] [PubMed] [Google Scholar]
- Straus D. C., Lange C. F. Immunochemistry and end-group analyses of group A streptococcal M proteins. Infect Immun. 1972 Jun;5(6):927–932. doi: 10.1128/iai.5.6.927-932.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Swanson J., Hsu K. C., Gotschlich E. C. Electron microscopic studies on streptococci. I. M antigen. J Exp Med. 1969 Nov 1;130(5):1063–1091. doi: 10.1084/jem.130.5.1063. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Vosti K. L., Johnson R. H., Dillon M. F. Further characterization of purified fractions of M protein from a strain of group A, type 12 Streptococcus. J Immunol. 1971 Jul;107(1):104–114. [PubMed] [Google Scholar]
- Wiley G. G., Bruno P. N. Cross-reactions among Group A streptococci. I. Precipitin and bactericidal cross-reactions among types 33, 41, 43, 52, and Ross. J Exp Med. 1968 Nov 1;128(5):959–968. doi: 10.1084/jem.128.5.959. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Ycas M. On certain homologies between proteins. J Mol Evol. 1976 Apr 9;7(3):215–244. doi: 10.1007/BF01731490. [DOI] [PubMed] [Google Scholar]
- Zabriskie J. B., Freimer E. H. An immunological relationship between the group. A streptococcus and mammalian muscle. J Exp Med. 1966 Oct 1;124(4):661–678. doi: 10.1084/jem.124.4.661. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Zucker-Franklin D. Immunophagocytosis of human amyloid fibrils by leukocytes. J Ultrastruct Res. 1970 Aug;32(3):247–257. doi: 10.1016/s0022-5320(70)80005-3. [DOI] [PubMed] [Google Scholar]