Epistatic interactions promote persistence of NS3-Q80K in HCV infection by compensating for protein folding instability.


Journal

The Journal of biological chemistry
ISSN: 1083-351X
Titre abrégé: J Biol Chem
Pays: United States
ID NLM: 2985121R

Informations de publication

Date de publication:
09 2021
Historique:
received: 11 05 2021
revised: 27 07 2021
accepted: 29 07 2021
pubmed: 3 8 2021
medline: 15 12 2021
entrez: 2 8 2021
Statut: ppublish

Résumé

The Q80K polymorphism in the NS3-4A protease of the hepatitis C virus is associated with treatment failure of direct-acting antiviral agents. This polymorphism is highly prevalent in genotype 1a infections and stably transmitted between hosts. Here, we investigated the underlying molecular mechanisms of evolutionarily conserved coevolving amino acids in NS3-Q80K and revealed potential implications of epistatic interactions in immune escape and variants persistence. Using purified protein, we characterized the impact of epistatic amino acid substitutions on the physicochemical properties and peptide cleavage kinetics of the NS3-Q80K protease. We found that Q80K destabilized the protease protein fold (p < 0.0001). Although NS3-Q80K showed reduced peptide substrate turnover (p < 0.0002), replicative fitness in an H77S.3 cell culture model of infection was not significantly inferior to the WT virus. Epistatic substitutions at residues 91 and 174 in NS3-Q80K stabilized the protein fold (p < 0.0001) and leveraged the WT protease stability. However, changes in protease stability inversely correlated with enzymatic activity. In infectious cell culture, these secondary substitutions were not associated with a gain of replicative fitness in NS3-Q80K variants. Using molecular dynamics, we observed that the total number of residue contacts in NS3-Q80K mutants correlated with protein folding stability. Changes in the number of contacts reflected the compensatory effect on protein folding instability by epistatic substitutions. In summary, epistatic substitutions in NS3-Q80K contribute to viral fitness by mechanisms not directly related to RNA replication. By compensating for protein-folding instability, epistatic interactions likely protect NS3-Q80K variants from immune cell recognition.

Identifiants

pubmed: 34339738
pii: S0021-9258(21)00833-4
doi: 10.1016/j.jbc.2021.101031
pmc: PMC8405986
pii:
doi:

Substances chimiques

Viral Nonstructural Proteins 0

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

101031

Informations de copyright

Copyright © 2021 The Authors. Published by Elsevier Inc. All rights reserved.

Déclaration de conflit d'intérêts

Conflict of interest The authors declare that they have no conflicts of interest with the contents of this article.

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Auteurs

Georg Dultz (G)

Department of Internal Medicine 1, Goethe University Hospital Frankfurt, Frankfurt am Main, Germany.

Sanjay K Srikakulam (SK)

Helmholtz Institute for Pharmaceutical Research Saarland (HIPS), Helmholtz Centre for Infection Research, Saarland University Campus, Saarbrücken, Germany; Graduate School of Computer Science, Saarland University, Saarbrücken, Germany; Interdisciplinary Graduate School of Natural Product Research, Saarland University, Saarbrücken, Germany.

Michael Konetschnik (M)

Department of Internal Medicine 1, Goethe University Hospital Frankfurt, Frankfurt am Main, Germany.

Tetsuro Shimakami (T)

Department of Gastroenterology, Kanazawa University Hospital, Kanazawa, Japan.

Nadezhda T Doncheva (NT)

Novo Nordisk Foundation Center for Protein Research, University of Copenhagen, Copenhagen, Denmark.

Julia Dietz (J)

Department of Internal Medicine 1, Goethe University Hospital Frankfurt, Frankfurt am Main, Germany.

Christoph Sarrazin (C)

Department of Internal Medicine 1, Goethe University Hospital Frankfurt, Frankfurt am Main, Germany.

Ricardo M Biondi (RM)

Molecular Targeting, Instituto de Investigación en Biomedicina de Buenos Aires (IBioBA) - CONICET - Partner Institute of the Max Planck Society, Buenos Aires, Argentina.

Stefan Zeuzem (S)

Department of Internal Medicine 1, Goethe University Hospital Frankfurt, Frankfurt am Main, Germany; University Center for Infectious Diseases, University Hospital Frankfurt, Frankfurt am Main, Germany.

Robert Tampé (R)

Institute of Biochemistry, Biocenter, Goethe University Frankfurt, Frankfurt am Main, Germany.

Olga V Kalinina (OV)

Helmholtz Institute for Pharmaceutical Research Saarland (HIPS), Helmholtz Centre for Infection Research, Saarland University Campus, Saarbrücken, Germany; Medical Faculty, Saarland University, Homburg, Germany; Center for Bioinformatics, Saarland Informatics Campus, Saarbrücken, Germany.

Christoph Welsch (C)

Department of Internal Medicine 1, Goethe University Hospital Frankfurt, Frankfurt am Main, Germany; University Center for Infectious Diseases, University Hospital Frankfurt, Frankfurt am Main, Germany. Electronic address: christoph.welsch@kgu.de.

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