The site of attachment in human rhinovirus 14 for antiviral agents that inhibit uncoating

Thomas J. Smith, Marcia J. Kremer, Ming Luo, Gerrit Vriend, Edward Arnold, Greg Kamer, Michael G. Rossmann, Mark A. McKinlay, Guy D. Diana, Michael J. Otto

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Abstract

WIN 51711 and WIN 52084 are structurally related, antiviral compounds that inhibit the replication of rhino (common cold) viruses and related picornaviruses. They prevent the pH-mediated uncoating of the viral RNA. The compounds consist of a 3-methylisoxazole group that inserts itself into the hydrophobic interior of the VP1 β-barrel, a connecting seven-membered aliphatic chain, and a 4-oxazolinylphenoxy group (OP) that covers the entrance to an ion channel in the floor of the "canyon." Viral disassembly may be inhibited by preventing the collapse of the VP1 hydrophobic pocket or by blocking the flow of ions into the virus interior.

Original languageEnglish (US)
Pages (from-to)1286-1293
Number of pages8
JournalScience
Volume233
Issue number4770
DOIs
StatePublished - Jan 1 1986
Externally publishedYes

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Cite this

Smith, T. J., Kremer, M. J., Luo, M., Vriend, G., Arnold, E., Kamer, G., Rossmann, M. G., McKinlay, M. A., Diana, G. D., & Otto, M. J. (1986). The site of attachment in human rhinovirus 14 for antiviral agents that inhibit uncoating. Science, 233(4770), 1286-1293. https://doi.org/10.1126/science.3018924