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

doi:10.1126/science.3018924

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

Research output: Contribution to journal › Article › peer-review

323 Scopus citations

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 language	English (US)
Pages (from-to)	1286-1293
Number of pages	8
Journal	Science
Volume	233
Issue number	4770
DOIs	https://doi.org/10.1126/science.3018924
State	Published - 1986
Externally published	Yes

ASJC Scopus subject areas

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title = "The site of attachment in human rhinovirus 14 for antiviral agents that inhibit uncoating",

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.",

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

year = "1986",

doi = "10.1126/science.3018924",

language = "English (US)",

volume = "233",

pages = "1286--1293",

journal = "Science",

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T1 - The site of attachment in human rhinovirus 14 for antiviral agents that inhibit uncoating

AU - Smith, Thomas J.

AU - Kremer, Marcia J.

AU - Luo, Ming

AU - Vriend, Gerrit

AU - Arnold, Edward

AU - Kamer, Greg

AU - Rossmann, Michael G.

AU - McKinlay, Mark A.

AU - Diana, Guy D.

AU - Otto, Michael J.

PY - 1986

Y1 - 1986

N2 - 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.

AB - 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.

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

Abstract

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