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. 1984 Oct;52(1):82–87. doi: 10.1128/jvi.52.1.82-87.1984

Identification of multiple forms of the noncapsid parvovirus protein NCVP1 in H-1 parvovirus-infected cells.

P R Paradiso
PMCID: PMC254492  PMID: 6481857

Abstract

Analysis of extracts of H-1 parvovirus-infected cells with virus-specific antiserum led to the identification of two forms of the noncapsid virus protein NCVP1. These two proteins had apparent molecular weights of 84,000 (NCVP1) and 92,000 (NCVP1') and were structurally related, based on their immunological reactivity and on peptide map analysis. Both of these proteins appeared early in the virus infection, about the same time that capsid proteins appeared. NCVP1' was a highly phosphorylated protein which was apparently derived from NCVP1 via a post-translational event. Phosphoserine was the predominant phosphorylated amino acid in NCVP1' and appeared to be localized in one site or a few sites on the protein. The possible involvement of these noncapsid proteins in parvovirus DNA replication is discussed.

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