Self assembly of HIV-1 Gag protein on lipid membranes generates PI(4,5)P2/Cholesterol nanoclusters
| Autor: | Cyril Favard, Hanumant S. Tanwar, Catherine Picart, Delphine Muriaux, Quentin Lubart, Johnson Mak, Naresh Yandrapalli |
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| Přispěvatelé: | Laboratoire des matériaux et du génie physique (LMGP), Institut polytechnique de Grenoble - Grenoble Institute of Technology (Grenoble INP)-Centre National de la Recherche Scientifique (CNRS)-Institut National Polytechnique de Grenoble (INPG), Centre for Virology, Macfarlane Burnet Institute, Department of Microbiology, Department of Biochemistry and Molecular Biology, Monash University [Clayton], Virologie humaine, École normale supérieure - Lyon (ENS Lyon)-IFR128-Institut National de la Santé et de la Recherche Médicale (INSERM), Institut de Recherche en Infectiologie de Montpellier (IRIM), Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS), IMBM, Institut polytechnique de Grenoble - Grenoble Institute of Technology (Grenoble INP)-Centre National de la Recherche Scientifique (CNRS)-Institut National Polytechnique de Grenoble (INPG)-Institut polytechnique de Grenoble - Grenoble Institute of Technology (Grenoble INP)-Centre National de la Recherche Scientifique (CNRS)-Institut National Polytechnique de Grenoble (INPG), École normale supérieure - Lyon (ENS Lyon)-IFR128-Institut National de la Santé et de la Recherche Médicale (INSERM)-École normale supérieure - Lyon (ENS Lyon)-IFR128-Institut National de la Santé et de la Recherche Médicale (INSERM), Centre National de la Recherche Scientifique (CNRS)-Université de Montpellier (UM), Centre d’études d’Agents Pathogènes et Biotechologies pour la Santé (CPBS), Laboratoire des matériaux et du génie physique (LMGP ), Institut National Polytechnique de Grenoble (INPG)-Institut polytechnique de Grenoble - Grenoble Institute of Technology (Grenoble INP )-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Deakin University [Burwood], Institut polytechnique de Grenoble - Grenoble Institute of Technology (Grenoble INP )-Institut National Polytechnique de Grenoble (INPG)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Lmgp, Labo |
| Jazyk: | angličtina |
| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
viruses Membrane lipids [SDV]Life Sciences [q-bio] Cell Biology Matrix (biology) Virus Nanoclusters 03 medical and health sciences chemistry.chemical_compound Pi medicine ComputingMilieux_MISCELLANEOUS 030304 developmental biology 0303 health sciences Multidisciplinary Chemistry Cholesterol 030302 biochemistry & molecular biology 3. Good health Cell biology [SDV] Life Sciences [q-bio] [SDV.BBM.BP]Life Sciences [q-bio]/Biochemistry Molecular Biology/Biophysics 030104 developmental biology Membrane medicine.anatomical_structure lipids (amino acids peptides and proteins) Sphingomyelin |
| Zdroj: | Scientific Reports Scientific Reports, Nature Publishing Group, 2016, 6, ⟨10.1038/srep39332⟩ Scientific Reports, Nature Publishing Group, 2016, 6 (1), ⟨10.1038/srep39332⟩ Scientific Reports, Nature Publishing Group, 2016, 6, pp.39332. ⟨10.1038/srep39332⟩ Scientific Reports, 2016, 6, pp.39332. ⟨10.1038/srep39332⟩ |
| ISSN: | 2045-2322 |
| DOI: | 10.1038/srep39332⟩ |
| Popis: | The self-assembly of HIV-1 Gag polyprotein at the inner leaflet of the cell host plasma membrane is the key orchestrator of virus assembly. The binding between Gag and the plasma membrane is mediated by specific interaction of the Gag matrix domain and the PI(4,5)P2 lipid (PIP2). It is unknown whether this interaction could lead to local reorganization of the plasma membrane lipids. In this study, using model membranes, we examined the ability of Gag to segregate specific lipids upon self-assembly. We show for the first time that Gag self-assembly is responsible for the formation of PIP2 lipid nanoclusters, enriched in cholesterol but not in sphingomyelin. We also show that Gag mainly partition into liquid-disordered domains of these lipid membranes. Our work strongly suggests that, instead of targeting pre-existing plasma membrane lipid domains, Gag is more prone to generate PIP2/Cholesterol lipid nanodomains at the inner leaflet of the plasma membrane during early events of virus assembly. |
| Databáze: | OpenAIRE |
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