A theoretical study of the acidification of the rhinovirus capsid

FEBS Lett. 1989 Nov 6;257(2):403-7. doi: 10.1016/0014-5793(89)81582-0.

Abstract

Electrostatic calculations for human rhinovirus 14 indicate that histidine-base residue pairs in the region of a beta-strand interaction between pentamers may be involved in a pH-induced process that leads to the release of viral RNA. Other picornavirus sequences are examined for these residue pairs, a subset of which is present in enteroviruses. Foot and mouth disease virus possesses one of the residue pairs, and cardioviruses, which undergo a separate pH and halide ion-induced capsid dissociation, possess none.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Capsid / physiology*
  • Histidine
  • Hydrogen-Ion Concentration
  • Isoelectric Point
  • Mengovirus / physiology
  • Models, Molecular
  • Protein Conformation
  • Rhinovirus / physiology*
  • Rhinovirus / ultrastructure
  • Structure-Activity Relationship

Substances

  • Histidine