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Protein Science, Vol 3, Issue 10 1712-1725, Copyright © 1994 by Cold Spring Harbor Laboratory Press

INVITED PAPER, SPECIAL SECTION IN HONOR OF MAX PERUTZ

Viral cell recognition and entry

M. G. ROSSMANN
Department of Biological Sciences, Purdue University, West Lafayette, Indiana 47907-1392

Rhinovirus infection is initiated by the recognition of a specific cell-surface receptor. The major group of rhinovirus serotypes attach to intercellular adhesion molecule-1 (ICAM-1). The attachment process initiates a series of conformational changes resulting in the loss of genomic RNA from the virion. X-ray crystallography and sequence comparisons suggested that a deep crevice or canyon is the site on the virus recognized by the cellular receptor molecule. This has now been verified by electron microscopy of human rhinovirus 14 (HRV14) and HRV16 complexed with a soluble component of ICAM-1. A hydrophobic pocket underneath the canyon is the site of binding of various hydrophobic drug compounds that can inhibit attachment and uncoating. This pocket is also associated with an unidentified, possibly cellular in origin, ``pocket factor.'' The pocket factor binding site overlaps the binding site of the receptor. It is suggested that competition between the pocket factor and receptor regulates the conformational changes required for the initiation of the entry of the genomic RNA into the cell.
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Copyright © 1994 by The Protein Society.