The Journal of Experimental Medicine
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Journal of Experimental Medicine, Vol 164, 1785-1790, Copyright © 1986 by Rockefeller University Press

ARTICLES

Sequence of myosin-crossreactive epitopes of streptococcal M protein

JB Dale and EH Beachey

Group A streptococcal M proteins contain epitopes that crossreact with sarcolemmal membrane proteins of human myocardium and myosin. In the present study, synthetic peptide copies spanning the entire 197-residue pepsin extracted fragment of type 5 M protein were used to localize the myosin-crossreactive epitopes of the molecule. Peptide 84-116 inhibited by 75% the binding of myosin-crossreactive antibodies evoked by pep M5, as determined by ELISA. Immunoblot inhibition studies confirmed that peptide 84-116 almost totally inhibited the binding of pep M5 antibodies to the heavy chain of human cardiac myosin. None of the remaining synthetic peptides, including peptide 1-35, which contains protective epitopes, inhibited antibodies binding to myosin. Two of three rabbits immunized with peptide 84-116 developed low but significant levels of antibodies crossreactive with myosin. Identification of the primary structures containing tissue- crossreactive as opposed to protective epitopes should not only allow the development of safe and effective M protein vaccines, but may also provide insights into the pathogenesis of rheumatic heart disease.
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