Cellular and biochemical responses of human T lymphocytes stimulated with streptococcal M proteins

Purified group A streptococcal M proteins, pep M5 and pep M6, bearing heart cross-reactive epitopes were compared with pep M24, which lacks such epitopes, in their ability to induce functional differentiation of human T lymphocytes. Lymphocytes activated by pep M5 and pep M6 demonstrated cytotoxic a...

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Published in:The Journal of immunology (1950) Vol. 142; no. 3; pp. 966 - 970
Main Authors: Kotb, M, Courtney, HS, Dale, JB, Beachey, EH
Format: Journal Article
Language:English
Published: Bethesda, MD Am Assoc Immnol 01-02-1989
American Association of Immunologists
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Summary:Purified group A streptococcal M proteins, pep M5 and pep M6, bearing heart cross-reactive epitopes were compared with pep M24, which lacks such epitopes, in their ability to induce functional differentiation of human T lymphocytes. Lymphocytes activated by pep M5 and pep M6 demonstrated cytotoxic activity against cultured heart cells, whereas pep M24-activated cells differentiated into suppressor T cells, which specifically blocked cytotoxic T lymphocytes against cultured human myocardial cells and not NK cell activity against K562 cells. Pep M5 and not pep M24 induced an increase in the number of CD4, 4B4, helper/inducer T cells. In addition, these M proteins appear to induce different biochemical changes in T lymphocytes. Both pep M5 and pep M24 induced the phosphorylation of a 35-kDa cytoplasmic protein; however, only pep M5 induced the phosphorylation of a 28-kDa membrane protein, primarily in CD4 T cells. These data indicate that the virulent M protein Ag of group A streptococci may exert their effect on the human immune system via different mechanisms. Determining these mechanisms and the biochemical pathways involved in T cell differentiation triggered by these Ag may be important in understanding the pathogenesis of post-streptococcal diseases.
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ISSN:0022-1767
1550-6606
DOI:10.4049/jimmunol.142.3.966