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Epitopes of streptococcal M proteins shared with cardiac myosin

We present evidence that M proteins from three different serotypes of group A streptococci share epitopes with cardiac myosin. Rabbit antisera evoked by a purified fragment of type 5 M protein crossreacted with myosin, but not alpha-tropomyosin, actin, or myosin light chains. In enzyme-linked immuno...

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Detalles Bibliográficos
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1985
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2187745/
https://www.ncbi.nlm.nih.gov/pubmed/2410530
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description We present evidence that M proteins from three different serotypes of group A streptococci share epitopes with cardiac myosin. Rabbit antisera evoked by a purified fragment of type 5 M protein crossreacted with myosin, but not alpha-tropomyosin, actin, or myosin light chains. In enzyme-linked immunosorbent assays, the myosin-crossreactive antibodies were totally inhibited by type 5 M protein and partially inhibited by types 6 and 19 M proteins. The affinity-purified myosin antibodies opsonized type 5 streptococci, indicating that they were directed against protective M protein epitopes on the surface of the organisms. Immunoblot analyses demonstrated the binding of the crossreactive antibodies to myosin heavy chains. Sera from patients with acute rheumatic fever showed significantly stronger reactions with myosin than did sera from their siblings, hospitalized controls, or patients with poststreptococcal glomerulonephritis.
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spelling pubmed-21877452008-04-17 Epitopes of streptococcal M proteins shared with cardiac myosin J Exp Med Articles We present evidence that M proteins from three different serotypes of group A streptococci share epitopes with cardiac myosin. Rabbit antisera evoked by a purified fragment of type 5 M protein crossreacted with myosin, but not alpha-tropomyosin, actin, or myosin light chains. In enzyme-linked immunosorbent assays, the myosin-crossreactive antibodies were totally inhibited by type 5 M protein and partially inhibited by types 6 and 19 M proteins. The affinity-purified myosin antibodies opsonized type 5 streptococci, indicating that they were directed against protective M protein epitopes on the surface of the organisms. Immunoblot analyses demonstrated the binding of the crossreactive antibodies to myosin heavy chains. Sera from patients with acute rheumatic fever showed significantly stronger reactions with myosin than did sera from their siblings, hospitalized controls, or patients with poststreptococcal glomerulonephritis. The Rockefeller University Press 1985-08-01 /pmc/articles/PMC2187745/ /pubmed/2410530 Text en This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Articles
Epitopes of streptococcal M proteins shared with cardiac myosin
title Epitopes of streptococcal M proteins shared with cardiac myosin
title_full Epitopes of streptococcal M proteins shared with cardiac myosin
title_fullStr Epitopes of streptococcal M proteins shared with cardiac myosin
title_full_unstemmed Epitopes of streptococcal M proteins shared with cardiac myosin
title_short Epitopes of streptococcal M proteins shared with cardiac myosin
title_sort epitopes of streptococcal m proteins shared with cardiac myosin
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2187745/
https://www.ncbi.nlm.nih.gov/pubmed/2410530