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Single-molecule imaging of HIV-1 envelope glycoprotein dynamics and Gag lattice association exposes determinants responsible for virus incorporation

Pezeshkian, Nairi ; Groves, Nicholas S. ; van Engelenburg, Schuyler B.

Proceedings of the National Academy of Sciences - PNAS, 2019-12, Vol.116 (50), p.25269-25277 [Revista revisada por pares]

United States: National Academy of Sciences

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Título:
Single-molecule imaging of HIV-1 envelope glycoprotein dynamics and Gag lattice association exposes determinants responsible for virus incorporation
Autor: Pezeshkian, Nairi ; Groves, Nicholas S. ; van Engelenburg, Schuyler B.
Materias: Assembling ; Assembly ; Biological Sciences ; Cell Membrane - virology ; Computed tomography ; env Gene Products, Human Immunodeficiency Virus - chemistry ; env Gene Products, Human Immunodeficiency Virus - genetics ; env Gene Products, Human Immunodeficiency Virus - metabolism ; gag Gene Products, Human Immunodeficiency Virus - chemistry ; gag Gene Products, Human Immunodeficiency Virus - genetics ; gag Gene Products, Human Immunodeficiency Virus - metabolism ; Gag protein ; Glycoproteins ; HIV ; HIV Infections - virology ; HIV-1 - chemistry ; HIV-1 - genetics ; HIV-1 - physiology ; Human immunodeficiency virus ; Humans ; Immune response ; Infectivity ; Membranes ; Physical Sciences ; PNAS Plus ; Protein Binding ; Protein Domains ; Proteins ; Single Molecule Imaging ; Trapping ; Trimers ; Virus Assembly ; Viruses
Es parte de: Proceedings of the National Academy of Sciences - PNAS, 2019-12, Vol.116 (50), p.25269-25277
Notas: ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
Edited by Malcolm A. Martin, NIH, Bethesda, MD, and approved October 30, 2019 (received for review June 11, 2019)
Author contributions: S.B.v.E. designed the study; N.P. and S.B.v.E. developed new reagents and probes; N.S.G. and S.B.v.E. developed analytical tools; N.P. performed imaging experiments; N.S.G. performed biochemical experiments; N.P., N.S.G., and S.B.v.E. analyzed data; and N.P., N.S.G., and S.B.v.E. wrote the paper.
Descripción: The HIV-1 envelope glycoprotein (Env) is sparsely incorporated onto assembling virus particles on the host cell plasma membrane in order for the virus to balance infectivity and evade the immune response. Env becomes trapped in a nascent particle on encounter with the polymeric viral protein Gag, which forms a dense protein lattice on the inner leaflet of the plasma membrane. While Env incorporation efficiency is readily measured biochemically from released particles, very little is known about the spatiotemporal dynamics of Env trapping events. Herein, we demonstrate, via high-resolution single-molecule tracking, that retention of Env trimers within single virus assembly sites requires the Env cytoplasmic tail (CT) and the L12 residue in the matrix (MA) domain of Gag but does not require curvature of the viral lattice. We further demonstrate that Env trimers are confined to subviral regions of a budding Gag lattice, supporting a model where direct interactions and/or steric corralling between the Env-CT and a lattice of MA trimers promote Env trapping and infectious HIV-1 assembly.
Editor: United States: National Academy of Sciences
Idioma: Inglés

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Single-molecule imaging of HIV-1 envelope glycoprotein dynamics and Gag lattice association exposes determinants responsible for virus incorporation

Pezeshkian, Nairi ; Groves, Nicholas S. ; van Engelenburg, Schuyler B.

United States: National Academy of Sciences

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