Plasma membrane is the site of productive HIV-1 particle assembly

Recently proposed models that have gained wide acceptance posit that HIV-1 virion morphogenesis is initiated by targeting the major structural protein (Gag) to late endosomal membranes. Thereafter, late endosome-based secretory pathways are thought to deliver Gag or assembled virions to the plasma m...

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Bibliographic Details
Published in:PLoS biology 2006-12, Vol.4 (12), p.e435-e435
Main Authors: Jouvenet, Nolwenn, Neil, Stuart J D, Bess, Cameron, Johnson, Marc C, Virgen, Cesar A, Simon, Sanford M, Bieniasz, Paul D
Format: Article
Language:English
Subjects:
Actins - metabolism
Biological Transport
Cell Biology
Cell Membrane - metabolism
Cell membranes
Cells, Cultured
Cellular biology
Endocytosis
Endosomes - metabolism
Gene Products, gag - genetics
Gene Products, gag - metabolism
Gene Products, gag - ultrastructure
Genetic aspects
HIV (Viruses)
HIV-1 - genetics
HIV-1 - metabolism
HIV-1 - ultrastructure
Humans
Infectious Diseases
Kinases
Leukemia
Macrophages - metabolism
Membranes
Microscopy, Electron, Transmission
Microtubules - metabolism
Plasma
Proteins
Virion - genetics
Virion - metabolism
Virion - ultrastructure
Virology
Virus Assembly
Viruses
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Summary:Recently proposed models that have gained wide acceptance posit that HIV-1 virion morphogenesis is initiated by targeting the major structural protein (Gag) to late endosomal membranes. Thereafter, late endosome-based secretory pathways are thought to deliver Gag or assembled virions to the plasma membrane (PM) and extracellular milieu. We present several findings that are inconsistent with this model. Specifically, we demonstrate that HIV-1 Gag is delivered to the PM, and virions are efficiently released into the extracellular medium, when late endosome motility is abolished. Furthermore, we show that HIV-1 virions are efficiently released when assembly is rationally targeted to the PM, but not when targeted to late endosomes. Recently synthesized Gag first accumulates and assembles at the PM, but a proportion is subsequently internalized via endocytosis or phagocytosis, thus accounting for observations of endosomal localization. We conclude that HIV-1 assembly is initiated and completed at the PM, and not at endosomal membranes.
ISSN:1545-7885
1544-9173
1545-7885
DOI:10.1371/journal.pbio.0040435