Role of arginine-56 within the structural protein VP3 of foot-and-mouth disease virus (FMDV) O1 Campos in virus virulence

Manuel V. Borca, Juan M. Pacheco, Lauren G. Holinka, Consuelo Carrillo, Ethan Hartwig, Damià Garriga, Edward J Kramer, Luis Rodriguez, Maria E. Piccone

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28 Citations (Scopus)

Abstract

FMDV O1 subtype undergoes antigenic variation under diverse growth conditions. Of particular is the amino acid variation observed at position 56 within the structural proteininterest VP3. Selective pressures influence whether histidine (H) or arginine (R) is present at this position, ultimately influencing in vitro plaque morphology and in vivo pathogenesis in cattle. Using reverse genetics techniques, we have constructed FMDV type O1 Campos variants differing only at VP3 position 56, possessing either an H or R (O1Ca-VP3-56H and O1Ca-VP3-56R, respectively), and characterized their in vitro phenotype and virulence in the natural host. Both viruses showed similar growth kinetics in vitro. Conversely, they had distinct temperature-sensitivity (ts) and displayed significantly different pathogenic profiles in cattle and swine. O1Ca-VP3-56H was thermo stable and induced typical clinical signs of FMD, whereas O1Ca-VP3-56R presented a ts phenotype and was nonpathogenic unless VP3 position 56 reverted in vivo to either H or cysteine (C).

Original languageEnglish
Pages (from-to)37-45
Number of pages9
JournalVirology
Volume422
Issue number1
DOIs
Publication statusPublished - 5 Jan 2012
Externally publishedYes

Keywords

  • Foot-and-mouth disease virus
  • Structural protein VP3
  • Virus attenuation

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