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<https://archiv.ub.uni-heidelberg.de/volltextserver/id/eprint/36287> <http://purl.org/dc/terms/title> "Super-resolution microscopy of HIV-1 Gag \r\nassembly-induced lipid domains"^^<http://www.w3.org/2001/XMLSchema#string> .
<https://archiv.ub.uni-heidelberg.de/volltextserver/id/eprint/36287> <http://purl.org/ontology/bibo/abstract> "Assembly of Gag, the main structural polyprotein of HIV-1, drives virion \r\nbiogenesis by recruiting and assembling the necessary factors at the plasma \r\nmembrane (PM) of infected cells. Lipid rafts, microdomains rich in Cholesterol and \r\nSphingomyelin (SM), are believed to serve as platforms for HIV-1 assembly and \r\nrelease. However, the localization, arrangement, composition, interactions, and \r\ndiversity of these lipid domains remain poorly understood. In this work, I combined \r\nlabeling of native Cholesterol and SM using recombinant fluorescence probes with \r\nstimulated emission depletion (STED) microscopy, to investigate lipid distribution at \r\nindividual HIV-1 assembly sites within the plasma membrane of cells.  \r\nGag assembly sites highly colocalized with Cholesterol- and SM-rich domains. \r\nNotably, one third of Gag domains were associated with a distinct ring-shaped lipid \r\ndomain localized at the border of Gag assembly sites – coinciding with the extended \r\nring-shaped envelope glycoprotein (Env) domain. Gag oligomerization at the PM in \r\nabsence of all other viral proteins, including Env, was sufficient to induce formation \r\nof this lipid ring. Semi-automated image analyses and classification of Gag assembly \r\nsites based on their fluorescence intensity indicated a progressive recruitment of \r\nlipid microdomains. Punctate lipid domains more often associated with low-intensity \r\nGag sites while half-ring and full-ring domains associated with respectively higher \r\nintensity and larger Gag domains. The Env ring domain largely overlapped with the \r\nlipid ring, but quantitative image analyses revealed the lipid ring to be on average \r\n~15 nm closer towards the center of assembly. Punctate Cholesterol signal was also \r\ndetected in released virus-like particles (VLPs), indicating that a portion of the lipid \r\nring domain gets incorporated during budding. GagCA3, a mutant that is unable to \r\ngenerate PM curvature, lacked recruitment of Cholesterol-rich domains while Env \r\nrecruitment was retained. However, only punctate Env domains were observed in \r\nGagCA3, which may result from altered interaction with the GagCA3 lattice compared \r\nto Gag wild type.  \r\nTogether these data indicate that the induction of negative curvature of the PM \r\nduring Gag immature lattice formation and assembly is essential for the recruitment \r\nof punctate lipid microdomains, which transition into a distinct ring-shaped domain \r\nsurrounding Gag. In conclusion, this study deepened our mechanistic understanding \r\nof HIV-1 assembly and provided a basis for further investigations of lipid-protein \r\ninteractions in viral assembly and in a broader context, vesicle-mediated release \r\nevents."^^<http://www.w3.org/2001/XMLSchema#string> .
<https://archiv.ub.uni-heidelberg.de/volltextserver/id/eprint/36287> <http://purl.org/dc/terms/date> "2025" .
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