GS-5806 Inhibits Pre- to Postfusion Conformational Changes of the Respiratory Syncytial Virus Fusion Protein
Author(s) -
Dharmaraj Samuel,
Weimei Xing,
Anita NiedzielaMajka,
Jinny S. Wong,
Magdeleine Hung,
Katherine M. Brendza,
Michel Perron,
Robert Jordan,
David Sperandio,
Xiaohong Liu,
Richard L. Mackman,
Roman Sakowicz
Publication year - 2015
Publication title -
antimicrobial agents and chemotherapy
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.07
H-Index - 259
eISSN - 1070-6283
pISSN - 0066-4804
DOI - 10.1128/aac.00761-15
Subject(s) - virus , lipid bilayer fusion , fusion protein , viral envelope , viral entry , biology , cell fusion , virology , paramyxoviridae , in vitro , pneumovirinae , viral replication , cell , biochemistry , recombinant dna , viral disease , gene
GS-5806 is a small-molecule inhibitor of human respiratory syncytial virus fusion protein-mediated viral entry. During viral entry, the fusion protein undergoes major conformational changes, resulting in fusion of the viral envelope with the host cell membrane. This process is reproduced in vitro using a purified, truncated respiratory syncytial virus (RSV) fusion protein. GS-5806 blocked these conformational changes, suggesting a possible mechanism for antiviral activity.
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