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Title of Journal: Arch Virol

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Abbravation: Archives of Virology

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Publisher

Springer Vienna

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DOI

10.1002/star.19530050812

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ISSN

1432-8798

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Selection and characterization of an acidresistan

Authors: Te Liang Decheng Yang Mengmeng Liu Chao Sun Fang Wang Jingfei Wang Haiwei Wang Shanshan Song Guohui Zhou Li Yu
Publish Date: 2013/10/12
Volume: 159, Issue: 4, Pages: 657-667
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Abstract

Footandmouth disease virus FMDV loses infectivity and immunogenicity due to its disassembly in culture environments below pH 68 To study the molecular basis of viral resistance to acidinduced disassembly and improve the acid stability of inactivated FMD vaccines during the manufacturing process type O FMDV mutants with increased resistance to acid inactivation were selected and the genes encoding their capsid proteins were sequenced Three amino acid substitutions VP1 N17D VP2 D86A and VP4 S73N were found in all of the mutants When these substitutions were introduced into seven infectious FMDV clones alone or combined a single amino acid substitution in the VP1 protein N17D which also appears in type C FMDV acidresistant mutants was found to be responsible for the increased resistance to acid inactivation for type O FMDV In addition although viral fitness was reduced under standard culture conditions viral growth kinetics and virulence were not significantly altered in the rescued mutant virus rN17D with the VP1 N17D substitution Importantly the N17D substitution could confer improved immunogenicity to the mutant virus rN17D under acidic conditions compared with its parental virus O/YS/CHA/05 These results demonstrate that the N17D substitution in VP1 is the molecular determinant of the acidresistant phenotype in type O FMDV indicating the potential for use of this substitution to improve the acid stability of inactivated FMD vaccines during the vaccine production process

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