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Your search keyword '"Hanumant S, Tanwar"' showing total 2 results
Start Over Author "Hanumant S, Tanwar" Topic lipids (amino acids, peptides, and proteins)
2 results on '"Hanumant S, Tanwar"'

1. Self assembly of HIV-1 Gag protein on lipid membranes generates PI(4,5)P

Author

Naresh, Yandrapalli, Quentin, Lubart, Hanumant S, Tanwar, Catherine, Picart, Johnson, Mak, Delphine, Muriaux, and Cyril, Favard

Subjects
Phosphatidylinositol 4,5-Diphosphate, Cholesterol, viruses, Virus Assembly, Lipid Bilayers, HIV-1, lipids (amino acids, peptides, and proteins), gag Gene Products, Human Immunodeficiency Virus, Article
Abstract

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.

Published
2016

2. Self assembly of HIV-1 Gag protein on lipid membranes generates PI(4,5)P2/Cholesterol nanoclusters

Author

Cyril Favard, Hanumant S. Tanwar, Catherine Picart, Delphine Muriaux, Quentin Lubart, Johnson Mak, Naresh Yandrapalli, 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), and Lmgp, Labo

Subjects
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
Abstract

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.

Published
2016

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