The study identifies the specific viral polypeptides associated with poliovirus replication complexes and demonstrates the effect of amino acid depletion on their composition.
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Does not yet inform antiviral strategies; leaves open how amino acid availability modulates poliovirus replication complex composition in vivo.
Viral polypeptides associated with the membrane-free replication complex of poliovirus RNA were multiple in nature. The structural protein precursors [VP0, VP1, VP3] predominated, and because they were found in a cytoplasmic component with the same S value and density as the replication complex are likely to be attached to it in vivo. They were not present in the form of empty capsids. The electrophoretic polypeptide pattern of the membrane-bound replication complex was similar but showed a predominance of NCVPX or VP1, unless the cells were slightly depleted in amino acids when the non-structural polypeptide NCVP2 became important. Cystine was the only amino acid capable of reversing this depletion effect on its own.
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Wright et al. (1976) studied this question.
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