The study demonstrates that a tyrosine replacement of the VP2 histidine (VP2 H145Y) increases the acid resistance of the FMDV capsid, highlighting the multifunctionality of picornavirus capsid residues.
Answers are grounded in this paper and cite their sources.
Supports FMDV capsid engineering for stability; leaves open translation to vaccine efficacy in vivo.
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.
No takes yet. Share an insight, caveat, or question.
Vázquez-Calvo et al. (2013) studied this question.
Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context: