Three capsid amino acids notably influence coxsackie B3 virus stability

J Gen Virol. 2016 Jan;97(1):60-68. doi: 10.1099/jgv.0.000319. Epub 2015 Oct 20.

Abstract

Coxsackievirus B3 strain 28 (CVB3/28) is less stable at 37 °C than eight other CVB3 strains with which it has been compared, including four in this study. In a variant CVB3/28 population selected for increased stability at 37 °C, the capsid proteins of the stable variant differed from the parental CVB3/28 by two mutations in Vp1 and one mutation in Vp3, each of which resulted in altered protein sequences. Each of the amino acid changes was individually associated with a more stable virus. Competition between CVB3/28 and a more stable derivative of the strain showed that propagation of the less stable virus was favoured in receptor-rich HeLa cells.

MeSH terms

  • Amino Acids / analysis*
  • Capsid Proteins / chemistry
  • Capsid Proteins / genetics*
  • Enterovirus B, Human / genetics
  • Enterovirus B, Human / physiology*
  • Enterovirus B, Human / radiation effects*
  • Epithelial Cells / virology
  • HeLa Cells
  • Humans
  • Microbial Viability / radiation effects*
  • Mutant Proteins / genetics
  • Mutation, Missense
  • Temperature
  • Virus Attachment

Substances

  • Amino Acids
  • Capsid Proteins
  • Mutant Proteins