HIV-1 Protease Codon 36 Polymorphisms and Differential Development of Resistance to Nelfinavir, Lopinavir, and Atazanavir in Different HIV-1 Subtypes
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| Published in | Antimicrobial Agents and Chemotherapy Vol. 54; no. 7; pp. 2878 - 2885 |
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Washington, DC
American Society for Microbiology
01.07.2010
American Society for Microbiology (ASM) |
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The amino acid at position 36 of the HIV-1 protease differs among various viral subtypes, in that methionine is usually found in subtype B viruses but isoleucine is common in other subtypes. This polymorphism is associated with higher rates of treatment failure involving protease inhibitors (PIs) in non-subtype B-infected patients. To investigate this, we generated genetically homogeneous wild-type viruses from subtype B, subtype C, and CRF02_AG full-length molecular clones and showed that subtype C and CRF02_AG I36 viruses exhibited higher levels of resistance to various PIs than their respective M36 counterparts, while the opposite was observed for subtype B viruses. Selections for resistance with each variant were performed with nelfinavir (NFV), lopinavir (LPV), and atazanavir (ATV). Sequence analysis of the protease gene at week 35 revealed that the major NFV resistance mutation D30N emerged in NFV-selected subtype B viruses and in I36 subtype C viruses, despite polymorphic variation. A unique mutational pattern developed in subtype C M36 viruses selected with NFV or ATV. The presence of I47A in LPV-selected I36 CRF02_AG virus conferred higher-level resistance than L76V in LPV-selected M36 CRF02_AG virus. Phenotypic analysis revealed a >1,000-fold increase in NFV resistance in I36 subtype C NFV-selected virus with no apparent impact on viral replication capacity. Thus, the position 36 polymorphism in the HIV-1 protease appears to have a differential effect on both drug susceptibility and the viral replication capacity, depending on both the viral subtype and the drug being evaluated. The amino acid at position 36 of the HIV-1 protease differs among various viral subtypes, in that methionine is usually found in subtype B viruses but isoleucine is common in other subtypes. This polymorphism is associated with higher rates of treatment failure involving protease inhibitors (PIs) in non-subtype B-infected patients. To investigate this, we generated genetically homogeneous wild-type viruses from subtype B, subtype C, and CRF02_AG full-length molecular clones and showed that subtype C and CRF02_AG I36 viruses exhibited higher levels of resistance to various PIs than their respective M36 counterparts, while the opposite was observed for subtype B viruses. Selections for resistance with each variant were performed with nelfinavir (NFV), lopinavir (LPV), and atazanavir (ATV). Sequence analysis of the protease gene at week 35 revealed that the major NFV resistance mutation D30N emerged in NFV-selected subtype B viruses and in I36 subtype C viruses, despite polymorphic variation. A unique mutational pattern developed in subtype C M36 viruses selected with NFV or ATV. The presence of I47A in LPV-selected I36 CRF02_AG virus conferred higher-level resistance than L76V in LPV-selected M36 CRF02_AG virus. Phenotypic analysis revealed a >1,000-fold increase in NFV resistance in I36 subtype C NFV-selected virus with no apparent impact on viral replication capacity. Thus, the position 36 polymorphism in the HIV-1 protease appears to have a differential effect on both drug susceptibility and the viral replication capacity, depending on both the viral subtype and the drug being evaluated.The amino acid at position 36 of the HIV-1 protease differs among various viral subtypes, in that methionine is usually found in subtype B viruses but isoleucine is common in other subtypes. This polymorphism is associated with higher rates of treatment failure involving protease inhibitors (PIs) in non-subtype B-infected patients. To investigate this, we generated genetically homogeneous wild-type viruses from subtype B, subtype C, and CRF02_AG full-length molecular clones and showed that subtype C and CRF02_AG I36 viruses exhibited higher levels of resistance to various PIs than their respective M36 counterparts, while the opposite was observed for subtype B viruses. Selections for resistance with each variant were performed with nelfinavir (NFV), lopinavir (LPV), and atazanavir (ATV). Sequence analysis of the protease gene at week 35 revealed that the major NFV resistance mutation D30N emerged in NFV-selected subtype B viruses and in I36 subtype C viruses, despite polymorphic variation. A unique mutational pattern developed in subtype C M36 viruses selected with NFV or ATV. The presence of I47A in LPV-selected I36 CRF02_AG virus conferred higher-level resistance than L76V in LPV-selected M36 CRF02_AG virus. Phenotypic analysis revealed a >1,000-fold increase in NFV resistance in I36 subtype C NFV-selected virus with no apparent impact on viral replication capacity. Thus, the position 36 polymorphism in the HIV-1 protease appears to have a differential effect on both drug susceptibility and the viral replication capacity, depending on both the viral subtype and the drug being evaluated. |
| Author | Susan M. Schader Irene Lisovsky Mark A. Wainberg Jorge-Luis Martinez-Cajas Daniela Moisi Maureen Oliveira |
| AuthorAffiliation | McGill University AIDS Centre, Lady Davis Institute, Jewish General Hospital, Montreal, Quebec, Canada, 1 Division of Experimental Medicine, McGill University, Montreal, Quebec, Canada, 2 Department of Microbiology and Immunology, McGill University, Montreal, Quebec, Canada, 3 Infectious Diseases Division, Department of Medicine, Queen's University, Kingston, Ontario, Canada 4 |
| AuthorAffiliation_xml | – name: McGill University AIDS Centre, Lady Davis Institute, Jewish General Hospital, Montreal, Quebec, Canada, 1 Division of Experimental Medicine, McGill University, Montreal, Quebec, Canada, 2 Department of Microbiology and Immunology, McGill University, Montreal, Quebec, Canada, 3 Infectious Diseases Division, Department of Medicine, Queen's University, Kingston, Ontario, Canada 4 |
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| Keywords | Antiretroviral agent Genetic variability HIV-1 virus Codon Nelfinavir Development Antiviral Immunopathology Atazanavir Typing Enzyme Lopinavir Enzyme inhibitor Retroviridae Genotype AIDS Immune deficiency Lentivirus Infection Virus Resistance Peptidases Viral disease Hydrolases Human immunodeficiency virus Subtype Protease inhibitor Polymorphism |
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Reddit... The amino acid at position 36 of the HIV-1 protease differs among various viral subtypes, in that methionine is usually found in subtype B viruses but... |
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| SubjectTerms | Anti-HIV Agents Anti-HIV Agents - pharmacology Anti-HIV Agents - therapeutic use Antibiotics. Antiinfectious agents. Antiparasitic agents Antiviral Agents Atazanavir Sulfate Biological and medical sciences Cell Line Cells, Cultured Codon Codon - genetics Genotype HIV Infections - drug therapy HIV Infections - genetics HIV Infections - virology HIV Protease HIV Protease - genetics HIV-1 HIV-1 - drug effects HIV-1 - enzymology HIV-1 - physiology Human immunodeficiency virus 1 Human viral diseases Humans Immunodeficiencies Immunodeficiencies. Immunoglobulinopathies Immunopathology Infectious diseases Lopinavir Medical sciences Nelfinavir - therapeutic use Oligopeptides - therapeutic use Pharmacology. Drug treatments Polymorphism, Genetic Polymorphism, Genetic - genetics Pyridines - therapeutic use Pyrimidinones - therapeutic use Viral diseases Viral diseases of the lymphoid tissue and the blood. Aids |
| Title | HIV-1 Protease Codon 36 Polymorphisms and Differential Development of Resistance to Nelfinavir, Lopinavir, and Atazanavir in Different HIV-1 Subtypes |
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