Three Residues in HIV-1 Matrix Contribute to Protease Inhibitor Susceptibility and Replication Capacity

• Published in: Antimicrobial Agents and Chemotherapy Vol. 55; no. 3; pp. 1106 - 1113
• Main Authors: PARRY, Chris M, KOLLI, Madhavi, MYERS, Richard E, CANE, Patricia A, SCHIFFER, Celia, PILLAY, Deenan
• Format: Journal Article
• Language: English
• Published: Washington, DC American Society for Microbiology 01.03.2011; American Society for Microbiology (ASM)
• Subjects: 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; 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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