Evidence map›Paper›PMID 25100843›Full record

ArticleJournal of virology2014

Coronaviruses resistant to a 3C-like protease inhibitor are attenuated for replication and pathogenesis, revealing a low genetic barrier but high fitness cost of resistance.

Xufang Deng, Sarah E StJohn, Heather L Osswald, Amornrat O'Brien, Bridget S Banach, Katrina Sleeman, Arun K Ghosh, Andrew D Mesecar, Susan C Baker

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing papers in PubMed
0.9field-weighted citation impact, top 27% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

55 citing papers in PubMed, 102 citations in OpenAlex.

  1. Trial
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  7. Expression and immunogenicity of non-structural protein 8 of porcine epidemic diarrhea virus.Veterinary research forum : an international quarterly journal · 2024
    Article
  8. Article
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  11. NMR Observation of Sulfhydryl Signals in SARS-CoV-2 Main Protease Aids Structural Studies.Chembiochem : a European journal of chemical biology · 2022
    Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors at 2 institutions in 1 country.

Xufang DengDepartment of Microbiology and Immunology, Loyola University Chicago, Stritch School of Medicine, Maywood, Illinois, USA.
Sarah E StJohnDepartments of Biological Science and Chemistry, Purdue University, West Lafayette, Indiana, USA.
Heather L OsswaldDepartments of Chemistry and Medicinal Chemistry, Purdue University, West Lafayette, Indiana, USA.
Amornrat O'BrienDepartment of Microbiology and Immunology, Loyola University Chicago, Stritch School of Medicine, Maywood, Illinois, USA.
Bridget S BanachDepartment of Microbiology and Immunology, Loyola University Chicago, Stritch School of Medicine, Maywood, Illinois, USA.
Katrina SleemanDepartment of Microbiology and Immunology, Loyola University Chicago, Stritch School of Medicine, Maywood, Illinois, USA.
Arun K GhoshDepartments of Chemistry and Medicinal Chemistry, Purdue University, West Lafayette, Indiana, USA.
Andrew D MesecarDepartments of Biological Science and Chemistry, Purdue University, West Lafayette, Indiana, USA.
Susan C BakerDepartment of Microbiology and Immunology, Loyola University Chicago, Stritch School of Medicine, Maywood, Illinois, USA sbaker1@luc.edu.
Loyola University Chicago · USPurdue University West Lafayette · US

Funding

Mechanisms of viral proteases in coronavirus replication and pathogenesisR01AI085089 · NIAID · LOYOLA UNIVERSITY CHICAGO · PI BAKER, SUSAN C., MESECAR, ANDREW D · 2010 to 2019
$6.8M
POLYMERASE PROTEINS IN CORONAVIRUS REPLICATIONR01AI026603 · NIAID · VANDERBILT UNIVERSITY MEDICAL CENTER · PI DENISON, MARK R · 1994 to 2014
$4.1M
Design & Synthesis of Nonpeptide Protease InhibitorsR37GM053386 · NIGMS · PURDUE UNIVERSITY · PI GHOSH, ARUN K · 2011 to 2018
$3.9M
CORONAVIRUS--ANALYSIS OF POLYMERASE GENE PRODUCTSR29AI026603 · NIAID · VANDERBILT UNIVERSITY · PI DENISON, MARK R · 1988 to 1992
–
NIAID NIH HHS AI026603NIAID NIH HHS AI085089NIAID NIH HHS R01 AI026603NIAID NIH HHS R01 AI085089NIGMS NIH HHS R37 GM053386
6 · The paper itself

Abstract

Viral protease inhibitors are remarkably effective at blocking the replication of viruses such as human immunodeficiency virus and hepatitis C virus, but they inevitably lead to the selection of inhibitor-resistant mutants, which may contribute to ongoing disease. Protease inhibitors blocking the replication of coronavirus (CoV), including the causative agents of severe acute respiratory syndrome (SARS) and Middle East respiratory syndrome (MERS), provide a promising foundation for the development of anticoronaviral therapeutics. However, the selection and consequences of inhibitor-resistant CoVs are unknown. In this study, we exploited the model coronavirus, mouse hepatitis virus (MHV), to investigate the genotype and phenotype of MHV quasispecies selected for resistance to a broad-spectrum CoV 3C-like protease (3CLpro) inhibitor. Clonal sequencing identified single or double mutations within the 3CLpro coding sequence of inhibitor-resistant virus. Using reverse genetics to generate isogenic viruses with mutant 3CLpros, we found that viruses encoding double-mutant 3CLpros are fully resistant to the inhibitor and exhibit a significant delay in proteolytic processing of the viral replicase polyprotein. The inhibitor-resistant viruses also exhibited postponed and reduced production of infectious virus particles. Biochemical analysis verified double-mutant 3CLpro enzyme as impaired for protease activity and exhibiting reduced sensitivity to the inhibitor and revealed a delayed kinetics of inhibitor hydrolysis and activity restoration. Furthermore, the inhibitor-resistant virus was shown to be highly attenuated in mice. Our study provides the first insight into the pathogenicity and mechanism of 3CLpro inhibitor-resistant CoV mutants, revealing a low genetic barrier but high fitness cost of resistance. Importance: RNA viruses are infamous for their ability to evolve in response to selective pressure, such as the presence of antiviral drugs. For coronaviruses such as the causative agent of Middle East respiratory syndrome (MERS), protease inhibitors have been developed and shown to block virus replication, but the consequences of selection of inhibitor-resistant mutants have not been studied. Here, we report the low genetic barrier and relatively high deleterious consequences of CoV resistance to a 3CLpro protease inhibitor in a coronavirus model system, mouse hepatitis virus (MHV). We found that although mutations that confer resistance arise quickly, the resistant viruses replicate slowly and do not cause lethal disease in mice. Overall, our study provides the first analysis of the low barrier but high cost of resistance to a CoV 3CLpro inhibitor, which will facilitate the further development of protease inhibitors as anti-coronavirus therapeutics.

Indexed as

Virus ReplicationAnimalsCell LineCell Line, TumorCoronavirusCricetinaeDrug Resistance, ViralHumansMiceMice, Inbred C57BLProtease InhibitorsProtease Inhibitors

Identifiers

PMID25100843
PMCPMC4178758
OpenAlexW2006452064

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.