Interaction of mumps virus V protein variants with STAT1-STAT2 heterodimer: experimental and theoretical studies.

ABSTRACT:

Background

Mumps virus V protein has the ability to inhibit the interferon-mediated antiviral response by inducing degradation of STAT proteins. Two virus variants purified from Urabe AM9 mumps virus vaccine differ in their replication and transcription efficiency in cells primed with interferon. Virus susceptibility to IFN was associated with insertion of a non-coded glycine at position 156 in the V protein (VGly) of one virus variant, whereas resistance to IFN was associated with preservation of wild-type phenotype in the V protein (VWT) of the other variant.

Results

VWT and VGly variants of mumps virus were cloned and sequenced from Urabe AM9 vaccine strain. VGly differs from VWT protein because it possesses an amino acid change Gln103Pro (Pro103) and the Gly156 insertion

SUBMITTER: Rosas-Murrieta NH 

PROVIDER: S-EPMC2958915 | biostudies-literature | 2010 Oct

REPOSITORIES: biostudies-literature