ArticleJournal of molecular biology2011
Accessory mutations maintain stability in drug-resistant HIV-1 protease.
Article in Journal of molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
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Who cites it
47 citing papers in PubMed.
- Dynamic signature of activity-stability tradeoff in lactamase evolution.Nature communications · 2026Article
- Premature Activation of the HIV-1 Protease Is Influenced by Polymorphisms in the Hinge Region.Viruses · 2024Article
- Kinetic coevolutionary models predict the temporal emergence of HIV-1 resistance mutations under drug selection pressure.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Direct-acting antiviral resistance of Hepatitis C virus is promoted by epistasis.Nature communications · 2023Article
- A yeast-based system to study SARS-CoV-2 Mpro structure and to identify nirmatrelvir resistant mutations.PLoS pathogens · 2023Article
- Article
- Contingency and Entrenchment of Drug-Resistance Mutations in HIV Viral Proteins.The journal of physical chemistry. B · 2022Article
- Viral proteases as therapeutic targets.Molecular aspects of medicine · 2022Review
- Antiretroviral therapy resistance mutations among HIV infected people in Kazakhstan.Scientific reports · 2022Article
- A yeast-based system to study SARS-CoV-2 Mpro structure and to identify nirmatrelvir resistant mutations.Research square · 2022Article
- A yeast-based system to study SARS-CoV-2 MbioRxiv : the preprint server for biology · 2022Article
- Covariation of viral recombination with single nucleotide variants during virus evolution revealed by CoVaMa.Nucleic acids research · 2022Article
- Potential Resistance of SARS-CoV-2 Main Protease (Mpro) against Protease Inhibitors: Lessons Learned from HIV-1 Protease.International journal of molecular sciences · 2022Review
- Elasticity-Associated Functionality and Inhibition of the HIV Protease.Advances in experimental medicine and biology · 2022Article
- The evolution of the HIV-1 protease folding stability.Virus evolution · 2022Article
- Deciphering Complex Mechanisms of Resistance and Loss of Potency through Coupled Molecular Dynamics and Machine Learning.Journal of chemical theory and computation · 2021Article
- Acquired HIV-1 Protease Conformational Flexibility Associated with Lopinavir Failure May Shape the Outcome of Darunavir Therapy after Antiretroviral Therapy Switch.Biomolecules · 2021Article
- Identification of an Antiretroviral Small Molecule That Appears To Be a Host-Targeting Inhibitor of HIV-1 Assembly.Journal of virology · 2021Article
- Antiretroviral Imprints and Genomic Plasticity of HIV-1Frontiers in microbiology · 2021Article
- Evolution of drug resistance in HIV protease.BMC bioinformatics · 2020Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
The underlying mechanisms driving the evolution of drug resistance in human immunodeficiency virus (HIV) are only partially understood. We investigated the evolutionary cost of the major resistance mutations in HIV-1 protease in terms of protein stability. The accumulation of resistance mutations destabilizes the protease, limiting further adaptation. From an analysis of clinical isolates, we identified specific accessory mutations that were able to restore the stability of the protease or even increase it beyond the wild-type baseline. Resistance mutations were also found to decrease the activity of HIV protease near neutral pH values, while incorporating stabilizing mutations improved the enzyme's pH tolerance. These findings help us to explain the prevalence of mutations located far from the active site and underscore the importance of protein stability during the evolution of drug resistance in HIV.
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