Identification and characterization of a porcine parvovirus nonstructural polypeptide

T. W. Molitor, H. S. Joo, M. S. Collett

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27 Scopus citations

Abstract

Sera from porcine parvovirus (PPV)-infected swine fetuses immunoprecipitated and 84- to 86-kilodalton polypeptide in addition to the A and B viron structural proteins. This polypeptide, designated NS-1, was present in PPV-infected cell lysates but not in purified virions. Partial proteolysis mapping revealed that NS-1 was not related to the A and B viral structural proteins. All three proteins in infected cells were phosphorylated at serine residues, and NS-1 also contained phosphothreonine. From pulse-labeling experiments with either 32P(i) or [35S]methionine, NS-1 was found to first appear 5 to 7 h postinfection, whereas the viral structural polypeptides were first synthesized 9 to 11 h postinfection. Pulse-chase experiments revealed that NS-1 initially appeared as an 84-kilodalton protein and was subsequently structurally modified to forms of slower electrophoretic mobilities. The time of appearance of NS-1 after virus infection coincided with the initiation of viral DNS synthesis, suggesting that this polypeptide (and the modified forms thereof) may be involved in PPV replication.

Original languageEnglish (US)
Pages (from-to)554-559
Number of pages6
JournalJournal of virology
Volume55
Issue number3
DOIs
StatePublished - Jan 1 1985

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