HIV-2 genome dimerization is required for the correct processing of gag: A second-site reversion in matrix can restore both processes in dimerization-impaired mutant viruses

• Main Authors: L'Hernault, A, Weiss, E.U, Greatorex, J.S, Lever, A.M
• Other Authors: MEDICINE
• Format: Article
• Published: 2020
• Subjects: Gag protein; matrix protein; mutant protein; purine; stem loop 1 protein; unclassified drug; virus protein; virus RNA; article; controlled study; genetic analysis; genetic parameters; genome dimerization; human; human cell; Human immunodeficiency virus 1; Human immunodeficiency virus 2; packaging signal; priority journal; protein assembly; protein motif; protein processing; protein structure; revertant; viral phenomena and functions; virus examination; virus infectivity; virus mutant; virus replication; Amino Acid Motifs; Cell Line; Dimerization; gag Gene Products, Human Immunodeficiency Virus; Genome, Viral; HIV Infections; HIV-2; Humans; Inverted Repeat Sequences; Molecular Sequence Data; Mutation; Nucleic Acid Conformation; Protein Processing, Post-Translational; Virus Replication
• Online Access: https://scholarbank.nus.edu.sg/handle/10635/180837
• Institution: National University of Singapore

10.1128/JVI.00124-12