Abstract
The resistance to phagocytosis of the group A streptococci has been attributed mainly to the presence of the surface antigen, M protein. In the present study, we addressed the question of whether the phagocytosis resistance of the group A streptococci is due to their ability to impair the function of the phagocytic cells. The results of these studies demonstrate that the presence of a large excess of a phagocytosis-resistant strain of streptococci does not significantly interfere with either the antibody-independent or the antibody-dependent phagocytosis of streptococci. Apparently, a phagocytosis-resistant strain of streptococci does not bring about a generalized deactivation of the phagocytic plasma membrane. This suggests that if the resistance of the group A streptococci is due to any deactivating influence at all on the phagocytic plasma membrane, it is likely to be confined to the contact area of the cocci with the phagocyte.
Full text
PDF



Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- BECKER C. G. SELECTION OF GROUP A STREPTOCOCCI RICH IN M-PROTEIN FROM POPULATIONS POOR IN M-PROTEIN. Am J Pathol. 1964 Jan;44:51–60. [PMC free article] [PubMed] [Google Scholar]
- Beachey E. H., Stollerman G. H. Toxic effects of streptococcal M protein on platelets and polymorphonuclear leukocytes in human blood. J Exp Med. 1971 Aug 1;134(2):351–365. doi: 10.1084/jem.134.2.351. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Bisno A. L. Alternate complement pathway activation by group A streptococci: role of M-protein. Infect Immun. 1979 Dec;26(3):1172–1176. doi: 10.1128/iai.26.3.1172-1176.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Fischetti V. A., Jones K. F., Manjula B. N., Scott J. R. Streptococcal M6 protein expressed in Escherichia coli. Localization, purification, and comparison with streptococcal-derived M protein. J Exp Med. 1984 Apr 1;159(4):1083–1095. doi: 10.1084/jem.159.4.1083. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Jacks-Weis J., Kim Y., Cleary P. P. Restricted deposition of C3 on M+ group A streptococci: correlation with resistance to phagocytosis. J Immunol. 1982 Apr;128(4):1897–1902. [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. 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]
- Manjula B. N., Fischetti V. A. Tropomyosin-like seven residue periodicity in three immunologically distinct streptococal M proteins and its implications for the antiphagocytic property of the molecule. J Exp Med. 1980 Mar 1;151(3):695–708. doi: 10.1084/jem.151.3.695. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Manjula B. N., Trus B. L., Fischetti V. A. Presence of two distinct regions in the coiled-coil structure of the streptococcal Pep M5 protein: relationship to mammalian coiled-coil proteins and implications to its biological properties. Proc Natl Acad Sci U S A. 1985 Feb;82(4):1064–1068. doi: 10.1073/pnas.82.4.1064. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Peterson P. K., Schmeling D., Cleary P. P., Wilkinson B. J., Kim Y., Quie P. G. Inhibition of alternative complement pathway opsonization by group A streptococcal M protein. J Infect Dis. 1979 May;139(5):575–585. doi: 10.1093/infdis/139.5.575. [DOI] [PubMed] [Google Scholar]
- Phillips G. N., Jr, Flicker P. F., Cohen C., Manjula B. N., Fischetti V. A. Streptococcal M protein: alpha-helical coiled-coil structure and arrangement on the cell surface. Proc Natl Acad Sci U S A. 1981 Aug;78(8):4689–4693. doi: 10.1073/pnas.78.8.4689. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Rotta J., Krause R. M., Lancefield R. C., Everly W., Lackland H. New approaches for the laboratory recognition of M types of group A streptococci. J Exp Med. 1971 Nov 1;134(5):1298–1315. doi: 10.1084/jem.134.5.1298. [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]
- WILEY G. G., WILSON A. T. The ability of group A streptococci killed by heat or mercury arc irradiation to resist ingestion by phagocytes. J Exp Med. 1956 Jan 1;103(1):15–36. doi: 10.1084/jem.103.1.15. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Weis J. J., Law S. K., Levine R. P., Cleary P. P. Resistance to phagocytosis by group A streptococci: failure of deposited complement opsonins to interact with cellular receptors. J Immunol. 1985 Jan;134(1):500–505. [PubMed] [Google Scholar]
- Whitnack E., Beachey E. H. Antiopsonic activity of fibrinogen bound to M protein on the surface of group A streptococci. J Clin Invest. 1982 Apr;69(4):1042–1045. doi: 10.1172/JCI110508. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Whitnack E., Dale J. B., Beachey E. H. Common protective antigens of group A streptococcal M proteins masked by fibrinogen. J Exp Med. 1984 Apr 1;159(4):1201–1212. doi: 10.1084/jem.159.4.1201. [DOI] [PMC free article] [PubMed] [Google Scholar]