title: 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.
abstract: 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 for VP0 cleavage. This mutant provides an example of the multifunctionality of picornavirus capsid residues.
authors.affiliation: Centro de Biología Molecular Severo Ochoa (CSIC-UAM), Cantoblanco, Madrid, Spain.
authors.forename: Angela
authors.initials: A
authors.lastname: Vázquez-Calvo
authors.forename: Flavia
authors.initials: F
authors.lastname: Caridi
authors.forename: Francisco
authors.initials: F
authors.lastname: Sobrino
authors.forename: Miguel A
authors.initials: MA
authors.lastname: Martín-Acebes
mesh_terms: D019943:Amino Acid Substitution; D000818:Animals; D036022:Capsid Proteins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D002460:Cell Line; D006224:Cricetinae; D029544:Foot-and-Mouth Disease Virus / Q000502:physiology*; D006639:Histidine; D006863:Hydrogen-Ion Concentration; D008958:Models, Molecular; D009154:Mutation; D011487:Protein Conformation; D055503:Protein Multimerization; D059748:Proteolysis; D014443:Tyrosine
chemical_list: D036022:Capsid Proteins; D014443:Tyrosine; D006639:Histidine