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Characterization of V36C, a Novel Amino Acid Substitution Conferring Hepatitis C Virus (HCV) Resistance to Telaprevir, a Potent Peptidomimetic Inhibitor of HCV Protease
Journal article   Open access   Peer reviewed

Characterization of V36C, a Novel Amino Acid Substitution Conferring Hepatitis C Virus (HCV) Resistance to Telaprevir, a Potent Peptidomimetic Inhibitor of HCV Protease

Laetitia Barbotte, Abdelhakim Ahmed-Belkacem, Stéphane Chevaliez, Alexandre Soulier, Christophe Hézode, Henri Wajcman, Doug J Bartels, Yi Zhou, Andrzej Ardzinski, Nagraj Mani, …
Antimicrobial agents and chemotherapy, Vol.54(6), pp.2681-2683
06/2010
DOI: 10.1128/AAC.01796-09
PMCID: PMC2876365
PMID: 20368394
url
https://europepmc.org/articles/pmc2876365View
Published (Version of record) Open Access

Abstract

We characterized a novel substitution conferring moderate resistance to telaprevir, a peptidomimetic inhibitor of hepatitis C virus protease. V36C conferred a 4.0-fold increase in the telaprevir 50% inhibitory concentration in an enzyme assay and a 9.5-fold increase in the replicon model. The replication capacity of a replicon harboring V36C was close to that of the wild-type protease. This case emphasizes the complexity of hepatitis C virus resistance to protease inhibitors.
Antiviral Agents Hepacivirus Oligopeptides Serine Proteinase Inhibitors

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