Structural analysis of small RNA viruses reveals a conserved hydrophobic pocket that serves as a target for antiviral agents.
May enable rhinovirus antivirals; leaves open clinical efficacy and safety in humans.
The 3-dimensional structures of a number of small animal RNA viruses are now known to near-atomic resolution. All these viruses have similar structures and have, in all probability, diverged from a common ancestral virus able to infect a variety of organisms. The structures have elucidated the site of attachment to host cell receptors and the mode of protection of this site against host immune pressure. An internal hydrophobic pocket in rhinoviruses is the site for binding of antiviral drugs that inhibit uncoating and can inhibit attachment in some viruses. The pocket is probably a functional necessity, and thus is a suitable target for well-designed antiviral agents in many viruses.
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Michael G. Rossmann (1989) studied this question.
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