The study elucidates the precursor-product relationships of encephalomyocarditis virus polypeptides, identifying polypeptide A as the precursor to capsid proteins.
No immediate clinical implications for myocarditis; leaves open precursor roles in human picornavirus pathogenesis.
The interrelationship of encephalomyocarditis (EMC) virus‐specific polypeptides was analysed by comparing their [ 35 S]methionine‐labelled tryptic peptides using thin‐layer electrophoresis and chromatography. It was found that the peptide patterns of EMC virus is similar to that of polypeptide A, whereas the fingerprint patterns of polypeptides C, D and E are similar to each other but differ greatly from that of A and purified virus. This is consistent with the proposal that polypeptide A is the precursor of the virus capsid proteins, and that polypeptide E is the cleavage product of D and C. The large number of labelled peptides found in the digests of low‐molecular‐weight proteins G, H, I indicates that they are a mixture of different polypeptides of similar molecular weight generated by the intracellular cleavage of large precursor molecules.
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Dobos et al. (1973) studied this question.
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