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. 1980 Aug;35(2):414–419. doi: 10.1128/jvi.35.2.414-419.1980

Picornaviral VPg sequences are contained in the replicase precursor.

M A Pallansch, O M Kew, A C Palmenberg, F Golini, E Wimmer, R R Rueckert
PMCID: PMC288826  PMID: 6255181

Abstract

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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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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