Abstract
Human reovirus s1 mRNA, which codes for the viral hemagglutinin, also directs the synthesis of a previously unrecognized polypeptide of molecular mass 14 kDa in reticulocyte and wheat germ extracts. Hybrid-arrest of translation by selected restriction fragments of cloned S1 DNA indicated that synthesis of the 14-kDa polypeptide initiates at the second AUG. This was confirmed by NH2-terminal sequence analyses. The coding sequence for the 14-kDa polypeptide thus lies entirely within the hemagglutinin gene but in a different reading frame. Although not found in virions, the 14-kDa polypeptide apparently is formed in virus-infected mouse L cells, as demonstrated by comparison of [35S]methionine-labeled polypeptides in cell extracts with the corresponding in vitro products.
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