Back to Search Start Over

Increased flexibility of the SARS-CoV-2 RNA-binding site causes resistance to remdesivir.

Authors :
Shiho Torii
Kwang Su Kim
Jun Koseki
Rigel Suzuki
Shoya Iwanami
Yasuhisa Fujita
Yong Dam Jeong
Jumpei Ito
Hiroyuki Asakura
Mami Nagashima
Kenji Sadamasu
Kazuhisa Yoshimura
Genotype to Phenotype Japan (G2P-Japan) Consortium
Kei Sato
Yoshiharu Matsuura
Teppei Shimamura
Shingo Iwami
Takasuke Fukuhara
Source :
PLoS Pathogens, Vol 19, Iss 3, p e1011231 (2023)
Publication Year :
2023
Publisher :
Public Library of Science (PLoS), 2023.

Abstract

Mutations continue to accumulate within the SARS-CoV-2 genome, and the ongoing epidemic has shown no signs of ending. It is critical to predict problematic mutations that may arise in clinical environments and assess their properties in advance to quickly implement countermeasures against future variant infections. In this study, we identified mutations resistant to remdesivir, which is widely administered to SARS-CoV-2-infected patients, and discuss the cause of resistance. First, we simultaneously constructed eight recombinant viruses carrying the mutations detected in in vitro serial passages of SARS-CoV-2 in the presence of remdesivir. We confirmed that all the mutant viruses didn't gain the virus production efficiency without remdesivir treatment. Time course analyses of cellular virus infections showed significantly higher infectious titers and infection rates in mutant viruses than wild type virus under treatment with remdesivir. Next, we developed a mathematical model in consideration of the changing dynamic of cells infected with mutant viruses with distinct propagation properties and defined that mutations detected in in vitro passages canceled the antiviral activities of remdesivir without raising virus production capacity. Finally, molecular dynamics simulations of the NSP12 protein of SARS-CoV-2 revealed that the molecular vibration around the RNA-binding site was increased by the introduction of mutations on NSP12. Taken together, we identified multiple mutations that affected the flexibility of the RNA binding site and decreased the antiviral activity of remdesivir. Our new insights will contribute to developing further antiviral measures against SARS-CoV-2 infection.

Details

Language :
English
ISSN :
15537366 and 15537374
Volume :
19
Issue :
3
Database :
Directory of Open Access Journals
Journal :
PLoS Pathogens
Publication Type :
Academic Journal
Accession number :
edsdoj.357fa629fa24023ac92f08664dbc0ff
Document Type :
article
Full Text :
https://doi.org/10.1371/journal.ppat.1011231