2024-03-28T07:58:34Zhttp://digital.csic.es/dspace-oai/requestoai:digital.csic.es:10261/1240122021-12-27T16:38:41Zcom_10261_79com_10261_1col_10261_332
Vázquez-Calvo, Ángela
Caridi, Flavia
Sobrino Castelló, Francisco
Martín-Acebes, Miguel Ángel
2015-10-28T11:56:10Z
2015-10-28T11:56:10Z
2013-12-18
Journal of Virology 88: 3039- 3042 (2014)
http://hdl.handle.net/10261/124012
10.1128/JVI.03222-13
24352460
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. © 2014, American Society for Microbiology.
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openAccess
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
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