Journal of Virology · 1980 · 41 citations · 23 references
Life SciencesBiochemistryMolecular BiologyMolecular VirologyStructural BiologyVirologyProteolytic ProcessingViral InfectionsViral Protein ProcessingViral ReplicationViral Rna BiologyViral StructureProteolytic Cleavage Of Viral PolyproteinsProteolytic Processing Of Viral Structural ProteinsViral PolymerasesViral ProteasesViral Replicase ComplexViral Replication Protein ProcessingViral Rna StructureVirion Maturation
It has previously been shown that the RNA replicase of encephalomyocarditis virus contains two virus-coded proteins, D and E, which are produced in two successive proteolytic steps: (i) C leads to D + ?; and (ii) D leads to p22 + E. It is here shown (i) that virus protein H (molecular weight, 12,000) is the previously unidentified product of the first step and (ii) that VPg, a protein linked covalently to the virion RNA, yields two tryptic peptides found in protein C but not in protein D. The results suggest that VPg is derived by cleavage of protein C and that protein H may be intermediate. Preliminary experiments with VPg sequences in polioviral noncapsid protein 1b, the counterpart of encephalomyocarditis viral protein C, were inconclusive.
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A protein covalently linked to poliovirus genome RNA.
Y F Lee, Akio Nomoto, B M Detjen et al. · Proceedings of the National Academy of Sciences · 1977 · 425 citations · Full text
James B. Flanegan, R F Petterson, Victor Ambros et al. · Proceedings of the National Academy of Sciences · 1977 · 346 citations · Full text
Life Sciences, Biochemistry, Biology +13
The location of the polio genome protein in viral RNAs and its implication for RNA synthesis
Akio Nomoto, B M Detjen, Rudy Pozzatti et al. · Nature · 1977 · 267 citations