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.

journal_name

J Virol

journal_title

Journal of virology

authors

Vázquez-Calvo A,Caridi F,Sobrino F,Martín-Acebes MA

doi

10.1128/JVI.03222-13

subject

Has Abstract

pub_date

2014-03-01 00:00:00

pages

3039-42

issue

5

eissn

0022-538X

issn

1098-5514

pii

JVI.03222-13

journal_volume

88

pub_type

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