Fiche publication
Date publication
novembre 2025
Journal
BioEssays : news and reviews in molecular, cellular and developmental biology
Auteurs
Membres identifiés du Cancéropôle Est :
Pr MELY Yves
Tous les auteurs :
Tomishige N, Mély Y, Kobayashi T
Lien Pubmed
Résumé
Human immunodeficiency virus type 1 (HIV-1) possesses an envelope enriched with a specific set of host plasma membrane (PM) lipids, a composition that is critical for viral infectivity. Virus budding is initiated by the binding of the viral Gag protein to phosphatidylinositol-4,5-bisphosphate (PI(4,5)P) located in the inner leaflet of the PM. However, the mechanism by which inner leaflet-associated Gag protein contributes to the enrichment of specific outer leaflet lipids, such as sphingomyelin (SM) and cholesterol (Chol), remains poorly understood. Visualization of endogenous lipids using specific lipid probes and advanced microscopy has revealed that Gag multimerization reorganizes SM- and Chol-rich lipid domains in a curvature-dependent manner. To further elucidate the molecular mechanisms underlying Gag-induced selective lipid enrichment across the bilayer, two potential scenarios are discussed: one involving interdigitation and the other involving Chol enrichment through flip-flop. These models are considered in the context of existing literature describing the distribution and interactions of SM, PI(4,5)P, and Chol within the PM.
Mots clés
cholesterol, human immunodeficiency virus type 1, lipid asymmetry, lipid domains, lipid imaging, phosphatidylinositol‐4,5‐bisphosphate, sphingomyelin
Référence
Bioessays. 2025 11 20;:e70090
