In macrophages, HIV-1 assembles into an intracellular plasma membrane domain containing the tetraspanins CD81, CD9, and CD53

Deneka, Magdalena; Pelchen–Matthews, Annegret; Byland, Rahel; Ruiz‐Mateos, Ezequiel; Marsh, Mark

doi:10.1083/jcb.200609050

Cited by 295 publications

(343 citation statements)

References 47 publications

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“…HIV-1 Gag colocalized substantially with CD81 but was significantly reduced in regions labeled with lysosomal marker Lamp-1, consistent with the reported VCC-like location of virus ( Fig. 2A and B) (3,39,40).…”

Section: Efficient Contact-mediated Hiv-1 Infection From Mdm To T Cellssupporting

confidence: 76%

“…Long-lived HIV-1-infected macrophages resist viral cytopathic effects and shelter replicationcompetent virions in surface-accessible (3)(4)(5)(6), but antibody-occluding (7,8), virus-containing compartments (VCCs) (6) for several weeks (9), which strongly implicates macrophages in HIV-1 persistence (10,11). Moreover, by efficiently spreading HIV-1 to uninfected CD4 ϩ T cells through direct cell-to-cell contact (4,12), macrophages may actively contribute to viral pathogenesis (10).…”

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confidence: 99%

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High-Multiplicity HIV-1 Infection and Neutralizing Antibody Evasion Mediated by the Macrophage-T Cell Virological Synapse

Duncan

Williams

Schiffner

et al. 2014

J Virol

100

113

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Section: Efficient Contact-mediated Hiv-1 Infection From Mdm To T Cellssupporting

confidence: 76%

mentioning

confidence: 99%

High-Multiplicity HIV-1 Infection and Neutralizing Antibody Evasion Mediated by the Macrophage-T Cell Virological Synapse

Duncan

Williams

Schiffner

et al. 2014

J Virol

100

113

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“…S1). These endosomes were not deep invaginations of plasma membrane, as proposed in other systems (28,57), because they were negative for the plasma membrane marker CD44 (data not shown). In addition, endosomal Gag did not correspond to endocytosed virions produced by surrounding cells (supplemental Fig.…”

Section: Hiv-1 Gag Is Present In Late Endosomes-becausementioning

confidence: 82%

Endosomal Trafficking of HIV-1 Gag and Genomic RNAs Regulates Viral Egress

Molle

Segura-Morales

Camus

et al. 2009

Journal of Biological Chemistry

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HIV-1 Gag can assemble and generate virions at the plasma membrane, but it is also present in endosomes where its role remains incompletely characterized. Here, we show that HIV-1 RNAs and Gag are transported on endosomal vesicles positive for TiVamp, a v-SNARE involved in fusion events with the plasma membrane. Inhibition of endosomal traffic did not prevent viral release. However, inhibiting lysosomal degradation induced an accumulation of Gag in endosomes and increased viral production 7-fold, indicating that transport of Gag to lysosomes negatively regulates budding. This also suggested that endosomal Gag-RNA complexes could access retrograde pathways to the cell surface and indeed, depleting cells of TiVampreduced viral production. Moreover, inhibition of endosomal transport prevented the accumulation of Gag at sites of cellular contact. HIV-1 Gag could thus generate virions using two pathways, either directly from the plasma membrane or through an endosome-dependent route. Endosomal Gag-RNA complexes may be delivered at specific sites to facilitate cell-to-cell viral transmission.

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“…It is generally accepted that the assembly of MLV and HIV predominantly occurs at the PM or its invaginations (14)(15)(16)(17)(18)(19)(20). Both HIV Gag and MLV Gag have also been observed to associate with late endosomes and multivesicular bodies (MVBs) in HeLa, HEK293, and T cells and macrophages (21)(22)(23)(24)(25).…”

mentioning

confidence: 99%

Murine Leukemia Virus Gag Localizes to the Uropod of Migrating Primary Lymphocytes

Sewald

Jin

et al. 2014

J Virol

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B and CD4؉ T lymphocytes are natural targets of murine leukemia virus (MLV). Migrating lymphocytes adopt a polarized morphology with a trailing edge designated the uropod. Here, we demonstrate that MLV Gag localizes to the uropod in polarized B cells and CD4 ؉ T cells. The uropod localization of MLV Gag was dependent on plasma membrane (PM) association and multimerization of Gag but independent of the viral glycoprotein Env. Basic residues in MA that are required for MLV Gag recruitment to virological synapses between HEK293 and XC cells were dispensable for uropod localization in migrating B cells. Ultrastructural studies indicated that both wild-type and basic-residue mutant Gag localized to the outer surface of the PM at the uropod. Late-domain mutant virus particles were seen at the uropod in form of budding-arrested intermediates. Finally, uropods mediated contact between MLV-infected B cells and uninfected T cells to form virological synapses. Our results suggest that MLV, not unlike HIV, accumulates at the uropod of primary lymphocytes to facilitate viral spreading through the formation of uropodmediated cell-cell contacts. IMPORTANCEViruses have evolved mechanisms to coordinate their assembly and budding with cell polarity to facilitate their spreading. In this study, we demonstrated that the viral determinants for MLV Gag to localize to the uropod in polarized B cells are distinct from the requirements to localize to virological synapses in transformed cell lines. Basic residues in MA that are required for the Gag localization to virological synapses between HEK293 and XC cells are dispensable for Gag localization to the uropod in primary B cells. Rather, plasma membrane association and capsid-driven multimerization of Gag are sufficient to drive MLV Gag to the uropod. MLV-laden uropods also mediate contacts between MLV-infected B cells and uninfected T cells to form virological synapses. Our results indicate that MLV accumulates at the uropod of primary lymphocytes to facilitate viral spreading through the formation of uropod-mediated cell-cell contacts.

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In macrophages, HIV-1 assembles into an intracellular plasma membrane domain containing the tetraspanins CD81, CD9, and CD53

Cited by 295 publications

References 47 publications

High-Multiplicity HIV-1 Infection and Neutralizing Antibody Evasion Mediated by the Macrophage-T Cell Virological Synapse

High-Multiplicity HIV-1 Infection and Neutralizing Antibody Evasion Mediated by the Macrophage-T Cell Virological Synapse

Endosomal Trafficking of HIV-1 Gag and Genomic RNAs Regulates Viral Egress

Murine Leukemia Virus Gag Localizes to the Uropod of Migrating Primary Lymphocytes

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