The mumps virus V protein is unstable in virus infected cells.
The mumps virus (MuV) V protein was characterized in virus infected cells by the use of antipeptide sera. In radioimmune precipitation assay (RIPA), the sera reacted with the V protein and also immunoprecipitated the nucleocapsid (NP) and phospho (P) proteins. However, by depletion RIPA (in which either the NP and P proteins or the V protein were removed) and Western immunoblotting, it was demonstrated that the V protein was not associated with the NP and P proteins, but that the anti-V sera cross-reacted with the NP protein. Pulse-chase experiments demonstrated that the V protein was gradually decreased during the chase period and could not be detected by antibodies raised against peptides representing three different regions of the protein at the end of the chase, while the NP and P proteins were relatively stable during the chase period. These results suggest that the V protein is unstable and degraded gradually in virus infected cells.
Hu
A
A
Department of Virology, School of Medicine, Karolinska Institute, Stockholm, Sweden.
Schwartz
S
S
Utter
G
G
Orvell
C
C
Kövamees
J
J
Norrby
E
E
D000595:Amino Acid Sequence; D000818:Animals; D015153:Blotting, Western; D006801:Humans; D008969:Molecular Sequence Data; D009109:Mumps virus / Q000378:metabolism* / Q000502:physiology; D015531:Radioimmunoprecipitation Assay; D014709:Vero Cells; D014764:Viral Proteins / Q000378:metabolism*; D014779:Virus Replication
D014764:Viral Proteins