Characterization of the vaccinia virus A35R protein and its role in virulence.

ABSTRACT: The vaccinia virus A35R gene is highly conserved among poxviruses and encodes a previously uncharacterized hydrophobic acidic protein. Western blotting with anti-A35R peptide antibodies indicated that the protein is expressed early in infection and resolved as a single sharp band of approximately 23 kDa, slightly higher than the 20 kDa predicted from its sequence. The protein band appeared to be the same molecular weight on sodium dodecyl sulfate-polyacrylamide gel electrophoresis, whether expressed in an in vitro transcription/translation system without microsomes or expressed in infected cells, suggesting that it was not glycosylated. A mutant virus with the A35R gene deleted (vA35Delta) formed wild-type-sized plaques on all cell lines tested (human, monkey, mouse, and rabbit); thus, A35

SUBMITTER: Roper RL 

PROVIDER: S-EPMC1317533 | biostudies-literature | 2006 Jan

REPOSITORIES: biostudies-literature