Two forms of VPg on poliovirus RNAs.

Abstract:

:The protein (VPg) linked to the 5' termini of poliovirus RNAs resolved into two species when subjected to non-equilibrium electrofocusing. The differently charged forms of VPg were not due to protein phosphorylation nor to variability of the number of phosphate residues associated with the nucleotide moiety remaining after RNase digestion of the nucleoprotein. Single-stranded viral RNA isolated from mature virions contained predominantly the more basic form of VPg, whereas unpackaged single-stranded RNa remaining in cells at the end of the virus replication cycle contained predominantly the more acidic form of VPg. Replicative-form (RF) molecules also contained both species of VPg, with the more acidic form representing the major species. Both plus and minus RNA strands in RF had similar VPg compositions; however, there appeared to be a strongly selective loss of VPg from only the minus strand in RF, particularly at late times postinfection.

journal_name

J Virol

journal_title

Journal of virology

authors

Richards OC,Hey TD,Ehrenfeld E

doi

10.1128/JVI.38.3.863-871.1981

subject

Has Abstract

pub_date

1981-06-01 00:00:00

pages

863-71

issue

3

eissn

0022-538X

issn

1098-5514

journal_volume

38

pub_type

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