Basic Residues in Human Immunodeficiency Virus Type 1 Nucleocapsid Promote Virion Assembly via Interaction with RNA
| Autor: | Cimarelli, A., Sandin, S., Höglund, S, Luban, J., Hoglund, S. |
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| Přispěvatelé: | Centre International de Recherche en Infectiologie - UMR (CIRI), Institut National de la Santé et de la Recherche Médicale (INSERM)-École normale supérieure - Lyon (ENS Lyon)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS), Centre International de Recherche en Infectiologie (CIRI), École normale supérieure de Lyon (ENS de Lyon)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Université Jean Monnet - Saint-Étienne (UJM)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS) |
| Rok vydání: | 2000 |
| Předmět: |
viruses
Molecular Sequence Data Immunology Gene Products gag RNA-binding protein Biology Virus Replication Microbiology Cell Line 03 medical and health sciences Virology Humans Inner membrane Amino Acid Sequence Nucleocapsid Peptide sequence DNA Primers 030304 developmental biology Alanine Zinc finger 0303 health sciences Base Sequence Sequence Homology Amino Acid Virus Assembly Structure and Assembly 030302 biochemistry & molecular biology Virion RNA-Binding Proteins RNA Zinc Fingers biochemical phenomena metabolism and nutrition 3. Good health Cell biology Viral replication Virion assembly Insect Science [SDV.MP.VIR]Life Sciences [q-bio]/Microbiology and Parasitology/Virology Mutation HIV-1 RNA Viral |
| Zdroj: | Journal of Virology Journal of Virology, American Society for Microbiology, 2000, 74 (7), pp.3046-3057. ⟨10.1128/jvi.74.7.3046-3057.2000⟩ Journal of Virology, 2000, 74 (7), pp.3046-3057. ⟨10.1128/jvi.74.7.3046-3057.2000⟩ |
| ISSN: | 1098-5514 0022-538X |
| DOI: | 10.1128/jvi.74.7.3046-3057.2000 |
| Popis: | Retroviral Gag polyproteins drive virion assembly by polymerizing to form a spherical shell that lines the inner membrane of nascent virions. Deletion of the nucleocapsid (NC) domain of the Gag polyprotein disrupts assembly, presumably because NC is required for polymerization. Human immunodeficiency virus type 1 NC possesses two zinc finger motifs that are required for specific recognition and packaging of viral genomic RNA. Though essential, zinc fingers and genomic RNA are not required for virion assembly. NC promiscuously associates with cellular RNAs, many of which are incorporated into virions. It has been hypothesized that Gag polymerization and virion assembly are promoted by nonspecific interaction of NC with RNA. Consistent with this model, we found an inverse relationship between the number of NC basic residues replaced with alanine and NC's nonspecific RNA-binding activity, Gag's ability to polymerize in vitro and in vivo, and Gag's capacity to assemble virions. In contrast, mutation of NC's zinc fingers had only minor effects on these properties. |
| Databáze: | OpenAIRE |
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