Publication | Open Access
Picornaviral VPg sequences are contained in the replicase precursor
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Citations
23
References
1980
Year
Tryptic PeptidesViral ReplicationMolecular VirologyProtein FoldingNatural SciencesPathogenesisImmunologyRna ReplicaseDna ReplicationMolecular BiologyVirologyReplicase PrecursorProtein X-ray CrystallographyProtein EvolutionViral Structural ProteinMedicineVirion RnaStructural Biology
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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