Structures of rotavirus reassortants demonstrate correlation of altered conformation of the VP4 spike and expression of unexpected VP4-associated phenotypes

J Virol. 2003 Mar;77(5):3291-6. doi: 10.1128/jvi.77.5.3291-3296.2003.


Numerous prior studies have indicated that viable rotavirus reassortants containing structural proteins of heterologous parental origin may express unexpected phenotypes, such as changes in infectivity and immunogenicity. To provide a structural basis for alterations in phenotypic expression, a three-dimensional structural analysis of these reassortants was conducted. The structures of the reassortants show that while VP4 generally maintains the parental structure when moved to a heterologous protein background, in certain reassortants, there are subtle alterations in the conformation of VP4. The alterations in VP4 conformation correlated with expression of unexpected VP4-associated phenotypes. Interactions between heterologous VP4 and VP7 in reassortants expressing unexpected phenotypes appeared to induce the conformational alterations seen in VP4.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Antigens, Viral*
  • Capsid Proteins / chemistry*
  • Capsid Proteins / genetics
  • Capsid Proteins / metabolism
  • Cattle
  • Models, Molecular
  • Phenotype
  • Protein Conformation*
  • Reassortant Viruses / chemistry*
  • Reassortant Viruses / genetics
  • Rotavirus / chemistry*
  • Rotavirus / genetics*


  • Antigens, Viral
  • Capsid Proteins
  • VP4 protein, Rotavirus
  • VP6 protein, Rotavirus
  • VP7 protein, Rotavirus