ArticleVirology2011
The interdomain linker region of HIV-1 capsid protein is a critical determinant of proper core assembly and stability.
Article in Virology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed.
- Atomistic characterization of the maturation mechanisms in the HIV-1 capsid domain.Nature communications · 2026Article
- HIV-1 Structural Proteins or Cell-Signaling Factors? That Is the Question!Current issues in molecular biology · 2024Review
- Nuclear Magnetic Resonance Spectroscopy to Study Virus Structure.Sub-cellular biochemistry · 2024Review
- Multidisciplinary studies with mutated HIV-1 capsid proteins reveal structural mechanisms of lattice stabilization.Nature communications · 2023Article
- HIV-1 capsid stability enables inositol phosphate-independent infection of target cells and promotes integration into genes.PLoS pathogens · 2023Article
- Human Immunodeficiency Virus Type 2 Capsid Protein Mutagenesis Reveals Amino Acid Residues Important for Virus Particle Assembly.Journal of molecular biology · 2022Article
- HIV-1 mutants that escape the cytotoxic T-lymphocytes are defective in viral DNA integration.PNAS nexus · 2022Article
- Mutation in the Disordered Linker Region of Capsid Disrupts Viral Kinetics of a Neuropathogenic SIV in Rhesus Macaques.Microbiology spectrum · 2022Article
- HIV Capsid Protein Genetic Diversity Across HIV-1 Variants and Impact on New Capsid-Inhibitor Lenacapavir.Frontiers in microbiology · 2022Article
- Rotten to the core: antivirals targeting the HIV-1 capsid core.Retrovirology · 2021Review
- HIV-1 capsid variability: viral exploitation and evasion of capsid-binding molecules.Retrovirology · 2021Review
- Curvature of the Retroviral Capsid Assembly Is Modulated by a Molecular Switch.The journal of physical chemistry letters · 2021Article
- Structure, Function, and Interactions of the HIV-1 Capsid Protein.Life (Basel, Switzerland) · 2021Review
- Intrinsic curvature of the HIV-1 CA hexamer underlies capsid topology and interaction with cyclophilin A.Nature structural & molecular biology · 2020Article
- Design, Synthesis, and Mechanism Study of Benzenesulfonamide-Containing Phenylalanine Derivatives as Novel HIV-1 Capsid Inhibitors with Improved Antiviral Activities.Journal of medicinal chemistry · 2020Article
- Allosteric Regulation of HIV-1 Capsid Structure for Gag Assembly, Virion Production, and Viral Infectivity by a Disordered Interdomain Linker.Journal of virology · 2019Article
- Article
- Role for Gag-CA Interdomain Linker in Primate Lentiviral Replication.Frontiers in microbiology · 2019Article
- Comparative genetic variability in HIV-1 subtype C p24 Gene in early age groups of infants.Virus genes · 2018Article
- The KT Jeang Retrovirology prize 2018: Eric Freed.Retrovirology · 2018Article
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Authors and funding
12 authors.
Funding
Abstract
The HIV-1 capsid protein consists of two independently folded domains connected by a flexible peptide linker (residues 146-150), the function of which remains to be defined. To investigate the role of this region in virus replication, we made alanine or leucine substitutions in each linker residue and two flanking residues. Three classes of mutants were identified: (i) S146A and T148A behave like wild type (WT); (ii) Y145A, I150A, and L151A are noninfectious, assemble unstable cores with aberrant morphology, and synthesize almost no viral DNA; and (iii) P147L and S149A display a poorly infectious, attenuated phenotype. Infectivity of P147L and S149A is rescued specifically by pseudotyping with vesicular stomatitis virus envelope glycoprotein. Moreover, despite having unstable cores, these mutants assemble WT-like structures and synthesize viral DNA, although less efficiently than WT. Collectively, these findings demonstrate that the linker region is essential for proper assembly and stability of cores and efficient replication.
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