Article
An increase in acid resistance of foot-and-mouth disease virus capsid is mediated by a tyrosine replacement of the VP2 histidine previously associated with VP0 cleavage.
Journal of virology - 1 Mar 2014
Vázquez-Calvo Angela, Caridi Flavia, Sobrino Francisco, Martín-Acebes Miguel A
Abstract excerpt
The foot-and-mouth disease virus (FMDV) capsid is highly acid labile, but introduction of amino acid replacements, including an N17D change in VP1, can increase its acid resistance. Using mutant VP1 N17D as a starting point, we isolated a virus with higher acid resistance carrying an additional replacement, VP2 H145Y, in a residue highly conserved among picornaviruses, which has been proposed to be responsible...
Topics
- Amino Acid Substitution
- Animals
- Capsid Proteins
- Cell Line
- Cricetinae
- Foot-and-Mouth Disease Virus
- Histidine
- Hydrogen-Ion Concentration
- Models, Molecular
- Mutation
- Protein Conformation
- Protein Multimerization
- Proteolysis
- Tyrosine