Structure and Function of a Genetically Engineered Mimic of a Nonenveloped Virus Entry Intermediate

  • Banerjee M
  • Speir J
  • Kwan M
  • et al.
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Abstract

Divalent metal ions are components of numerous icosahedral virus capsids. Flock House virus (FHV), a small RNA virus of the family Nodaviridae , was utilized as an accessible model system with which to address the effects of metal ions on capsid structure and on the biology of virus-host interactions. Mutations at the calcium-binding sites affected FHV capsid stability and drastically reduced virus infectivity, without altering the overall architecture of the capsid. The mutations also altered the conformation of gamma, a membrane-disrupting, virus-encoded peptide usually sequestered inside the capsid, by increasing its exposure under neutral pH conditions. Our data demonstrate that calcium binding is essential for maintaining a pH-based control on gamma exposure and host membrane disruption, and they reveal a novel rationale for the metal ion requirement during virus entry and infectivity. In the light of the phenotypes displayed by a calcium site mutant of FHV, we suggest that this mutant corresponds to an early entry intermediate formed in the endosomal pathway.

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Banerjee, M., Speir, J. A., Kwan, M. H., Huang, R., Aryanpur, P. P., Bothner, B., & Johnson, J. E. (2010). Structure and Function of a Genetically Engineered Mimic of a Nonenveloped Virus Entry Intermediate. Journal of Virology, 84(9), 4737–4746. https://doi.org/10.1128/jvi.02670-09

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