Article
Importance of arginine 20 of the swine vesicular disease virus 2A protease for activity and virulence.
Journal of virology - 1 Jan 2005
Inoue Toru, Alexandersen Soren, Clark Angela T, Murphy Ciara, Quan Melvyn, Reid Scott M, Sakoda Yoshihiro, Johns Helen L, Belsham Graham J
Abstract excerpt
A major virulence determinant of swine vesicular disease virus (SVDV), an Enterovirus that causes an acute vesicular disease, has been mapped to residue 20 of the 2A protease. The SVDV 2A protease cleaves the 1D-2A junction in the viral polyprotein, induces cleavage of translation initiation factor eIF4GI, and stimulates the activity of enterovirus internal ribosome entry sites (IRESs). The 2A protease from an...
Topics
- Amino Acid Sequence
- Animals
- Arginine
- Base Sequence
- Cysteine Endopeptidases
- Enterovirus B, Human
- Enterovirus Infections
- Gene Expression Regulation, Viral
- Molecular Sequence Data
- Mutation
- Sequence Analysis, DNA
- Swine Vesicular Disease
- Viral Proteins
