Three Residues in HIV-1 Matrix Contribute to Protease Inhibitor Susceptibility and Replication Capacity
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| Published in | Antimicrobial Agents and Chemotherapy Vol. 55; no. 3; pp. 1106 - 1113 |
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| AbstractList | Other than cleavage site mutations, there is little data on specific positions within Gag that impact on HIV protease inhibitor susceptibility. We have recently shown that non-cleavage site mutations in gag, particularly within matrix protein can restore replication capacity and further reduce protease inhibitor drug susceptibility when coexpressed with a drug-resistant (mutant) protease. The matrix protein of this patient-derived virus was studied in order to identify specific changes responsible for this phenotype. Three amino acid changes in matrix (R76K, Y79F, and T81A) had an impact on replication capacity as well as drug susceptibility. Introduction of these three changes into wild-type (WT) matrix resulted in an increase in the replication capacity of the protease mutant virus to a level similar to that achieved by all the changes within the mutant matrix and part of the capsid protein. Pairs of changes to wild-type matrix led to an increased replication capacity of the protease mutant (although less than with all three changes). Having only these three changes to matrix in a wild-type virus (with wild-type protease) resulted in a 5- to 7-fold change in protease inhibitor 50% effective concentration (EC₅₀). Individual changes did not have as great an effect on replication capacity or drug susceptibility, demonstrating an interaction between these positions, also confirmed by sequence covariation analysis. Molecular modeling predicts that each of the three mutations would result in a loss of hydrogen bonds within α-helix-4 of matrix, leading to the hypothesis that more flexibility within this region or altered matrix structure would account for our findings. Other than cleavage site mutations, there is little data on specific positions within Gag that impact on HIV protease inhibitor susceptibility. We have recently shown that non-cleavage site mutations in gag, particularly within matrix protein can restore replication capacity and further reduce protease inhibitor drug susceptibility when coexpressed with a drug-resistant (mutant) protease. The matrix protein of this patient-derived virus was studied in order to identify specific changes responsible for this phenotype. Three amino acid changes in matrix (R76K, Y79F, and T81A) had an impact on replication capacity as well as drug susceptibility. Introduction of these three changes into wild-type (WT) matrix resulted in an increase in the replication capacity of the protease mutant virus to a level similar to that achieved by all the changes within the mutant matrix and part of the capsid protein. Pairs of changes to wild-type matrix led to an increased replication capacity of the protease mutant (although less than with all three changes). Having only these three changes to matrix in a wild-type virus (with wild-type protease) resulted in a 5- to 7-fold change in protease inhibitor 50% effective concentration (EC50). Individual changes did not have as great an effect on replication capacity or drug susceptibility, demonstrating an interaction between these positions, also confirmed by sequence covariation analysis. Molecular modeling predicts that each of the three mutations would result in a loss of hydrogen bonds within alpha -helix-4 of matrix, leading to the hypothesis that more flexibility within this region or altered matrix structure would account for our findings. Classifications Services AAC Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter current issue AAC About AAC Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy AAC RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • journals@asmusa.org Print ISSN: 0066-4804 Online ISSN: 1098-6596 Copyright © 2014 by the American Society for Microbiology. For an alternate route to AAC .asm.org, visit: AAC Other than cleavage site mutations, there is little data on specific positions within Gag that impact on HIV protease inhibitor susceptibility. We have recently shown that non-cleavage site mutations in gag, particularly within matrix protein can restore replication capacity and further reduce protease inhibitor drug susceptibility when coexpressed with a drug-resistant (mutant) protease. The matrix protein of this patient-derived virus was studied in order to identify specific changes responsible for this phenotype. Three amino acid changes in matrix (R76K, Y79F, and T81A) had an impact on replication capacity as well as drug susceptibility. Introduction of these three changes into wild-type (WT) matrix resulted in an increase in the replication capacity of the protease mutant virus to a level similar to that achieved by all the changes within the mutant matrix and part of the capsid protein. Pairs of changes to wild-type matrix led to an increased replication capacity of the protease mutant (although less than with all three changes). Having only these three changes to matrix in a wild-type virus (with wild-type protease) resulted in a 5- to 7-fold change in protease inhibitor 50% effective concentration (EC50). Individual changes did not have as great an effect on replication capacity or drug susceptibility, demonstrating an interaction between these positions, also confirmed by sequence covariation analysis. Molecular modeling predicts that each of the three mutations would result in a loss of hydrogen bonds within α-helix-4 of matrix, leading to the hypothesis that more flexibility within this region or altered matrix structure would account for our findings. Other than cleavage site mutations, there is little data on specific positions within Gag that impact on HIV protease inhibitor susceptibility. We have recently shown that non-cleavage site mutations in gag , particularly within matrix protein can restore replication capacity and further reduce protease inhibitor drug susceptibility when coexpressed with a drug-resistant (mutant) protease. The matrix protein of this patient-derived virus was studied in order to identify specific changes responsible for this phenotype. Three amino acid changes in matrix (R76K, Y79F, and T81A) had an impact on replication capacity as well as drug susceptibility. Introduction of these three changes into wild-type (WT) matrix resulted in an increase in the replication capacity of the protease mutant virus to a level similar to that achieved by all the changes within the mutant matrix and part of the capsid protein. Pairs of changes to wild-type matrix led to an increased replication capacity of the protease mutant (although less than with all three changes). Having only these three changes to matrix in a wild-type virus (with wild-type protease) resulted in a 5- to 7-fold change in protease inhibitor 50% effective concentration (EC 50 ). Individual changes did not have as great an effect on replication capacity or drug susceptibility, demonstrating an interaction between these positions, also confirmed by sequence covariation analysis. Molecular modeling predicts that each of the three mutations would result in a loss of hydrogen bonds within α-helix-4 of matrix, leading to the hypothesis that more flexibility within this region or altered matrix structure would account for our findings. |
| Author | Patricia A. Cane Richard E. Myers Madhavi Kolli Deenan Pillay Celia Schiffer Chris M. Parry |
| AuthorAffiliation | Centre for Infections, Health Protection Agency, 61 Colindale Avenue, London NW9 5EQ, United Kingdom, 1 UCL/MRC Centre for Medical Molecular Virology, Division of Infection and Immunity, UCL, Windeyer Institute, 46 Cleveland Street, London W1T 4JF, United Kingdom, 2 Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, Massachusetts 01605 3 |
| AuthorAffiliation_xml | – name: Centre for Infections, Health Protection Agency, 61 Colindale Avenue, London NW9 5EQ, United Kingdom, 1 UCL/MRC Centre for Medical Molecular Virology, Division of Infection and Immunity, UCL, Windeyer Institute, 46 Cleveland Street, London W1T 4JF, United Kingdom, 2 Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, Massachusetts 01605 3 |
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| Keywords | Immunopathology HIV-1 virus Retroviridae AIDS Immune deficiency Lentivirus Infection Virus Sensitivity Residue Viral disease Antiviral Replication Human immunodeficiency virus Protease inhibitor Matrix system |
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| SubjectTerms | Amino acid sequence Antibiotics. Antiinfectious agents. Antiparasitic agents Antiviral Agents Biological and medical sciences Capsid protein Cell Line Data processing Drug resistance Drug Resistance, Viral - genetics Drugs Enzyme-Linked Immunosorbent Assay gag Gene Products, Human Immunodeficiency Virus - chemistry gag Gene Products, Human Immunodeficiency Virus - genetics Gag protein HIV Antigens - chemistry HIV Antigens - genetics HIV Protease Inhibitors HIV Protease Inhibitors - pharmacology HIV-1 Human immunodeficiency virus 1 Human viral diseases Humans Hydrogen bonding Immunodeficiencies Immunodeficiencies. Immunoglobulinopathies Immunopathology Infectious diseases matrix protein Medical sciences Molecular modelling Mutagenesis, Site-Directed Mutation Pharmacology. Drug treatments Proteinase inhibitors Replication Viral diseases Viral diseases of the lymphoid tissue and the blood. Aids Virus Replication - genetics |
| Title | Three Residues in HIV-1 Matrix Contribute to Protease Inhibitor Susceptibility and Replication Capacity |
| URI | http://aac.asm.org/content/55/3/1106.abstract https://www.ncbi.nlm.nih.gov/pubmed/21149628 https://journals.asm.org/doi/10.1128/AAC.01228-10 https://search.proquest.com/docview/907156668 https://pubmed.ncbi.nlm.nih.gov/PMC3067102 |
| Volume | 55 |
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