Key result
A single amino acid substitution (N17D) at the N terminus of the VP1 capsid protein increased the resistance of foot-and-mouth disease virus to acid-induced inactivation and capsid dissociation.
Population
Foot-and-mouth disease virus (FMDV) variants (six variants and parental C-S8c1 virus)
Comparison
Amino acid replacement N17D at the N terminus of… vs Parental C-S8c1 virus
Design
Preclinical
Authors
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Supports capsid engineering for acid-stable FMDV; leaves open translation to field strains or livestock trials.
A single amino acid substitution (N17D) in the FMDV capsid increases viral resistance to acid-induced disassembly, illustrating the adaptive flexibility of viral quasispecies.
Martín-Acebes et al. (2010) studied Foot-and-mouth disease virus (FMDV). Amino acid replacement N17D at the N terminus of VP1 capsid protein vs. Parental C-S8c1 virus was evaluated on Resistance to acid-induced inactivation and capsid dissociation. A single amino acid substitution (N17D) at the N terminus of the VP1 capsid protein increased the resistance of foot-and-mouth disease virus to acid-induced inactivation and capsid dissociation.
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