HIV-1 requires Arf6-mediated membrane dynamics to efficiently enter and infect T lymphocytes

García-Expósito, Laura; Barroso-González, Jonathan; Puigdomènech, Isabel; Machado, José David; Blanco, Julià; Valenzuela-Fernández, Agustı́n

doi:10.1091/mbc.e10-08-0722

Cited by 41 publications

(78 citation statements)

References 91 publications

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“…5D and E). The magnitude of this effect was similar to that previously reported to occur with ARF silencing (16). Under these conditions, ARF-6 knockdown did not inhibit HLA-A2 downmodulation in HIV-infected (Gag ϩ ) cells (Fig.…”

Section: Resultssupporting

confidence: 89%

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ADP Ribosylation Factor 1 Activity Is Required To Recruit AP-1 to the Major Histocompatibility Complex Class I (MHC-I) Cytoplasmic Tail and Disrupt MHC-I Trafficking in HIV-1-Infected Primary T Cells

Wonderlich

Leonard

Kulpa

et al. 2011

J Virol

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HIV-1-infected cells are partially resistant to anti-HIV cytotoxic T lymphocytes (CTLs) due to the effects of the HIV Nef protein on antigen presentation by major histocompatibility complex class I (MHC-I), and evidence has been accumulating that this function of Nef is important in vivo. HIV Nef disrupts the normal expression of MHC-I by stabilizing a protein-protein interaction between the clathrin adaptor protein AP-1 and the MHC-I cytoplasmic tail. There is also evidence that Nef activates a phosphatidylinositol 3 kinase (PI3K)-dependent GTPase, ADP ribosylation factor 6 (ARF-6), to stimulate MHC-I internalization. However, the relative importance of these two pathways is unclear. Here we report that a GTPase required for AP-1 activity (ARF-1) was needed for Nef to disrupt MHC-I surface levels, whereas no significant requirement for ARF-6 was observed in Nef-expressing T cell lines and in HIV-infected primary T cells. An ARF-1 inhibitor blocked the ability of Nef to recruit AP-1 to the MHC-I cytoplasmic tail, and a dominant active ARF-1 mutant stabilized the Nef-MHC-I-AP-1 complex. These data support a model in which Nef and ARF-1 stabilize an interaction between MHC-I and AP-1 to disrupt the presentation of HIV-1 epitopes to CTLs.

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Section: Resultssupporting

confidence: 89%

“…ARF-6 is known to regulate cellular entry by several microorganisms, including HIV, and ARF-6 silencing has been shown to inhibit HIV infection (16). Therefore, we used inhibition of HIV infection as a positive control for ARF-6 silencing.…”

Section: Resultsmentioning

confidence: 99%

ADP Ribosylation Factor 1 Activity Is Required To Recruit AP-1 to the Major Histocompatibility Complex Class I (MHC-I) Cytoplasmic Tail and Disrupt MHC-I Trafficking in HIV-1-Infected Primary T Cells

Wonderlich

Leonard

Kulpa

et al. 2011

J Virol

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“…It was reported that ARF6 depletion does not affect cell infection by HIV-1 vectors pseudotyped with the VSV-G protein 33 . To determine whether ESCRT machinery involved in viral budding was functionally affected or not by ARF6 depletion, we infected MCF-7 cells, depleted or not for ARF6, with VSVpseudotyped replication competent HIV-1.…”

Section: Arf6 Regulates Exosomesmentioning

confidence: 98%

Syntenin-ALIX exosome biogenesis and budding into multivesicular bodies are controlled by ARF6 and PLD2

et al. 2014

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“…Since actin remodeling should help the released HIV core to penetrate the cortical actin layer [26,36] (Fig. 3), the requirement for signaling and actin dynamics has been interpreted as evidence for HIV fusion with the PM [13,34,37]. The regulation of actin dynamics through CXCR4 signaling is particularly important for HIV infection of resting CD4 + T cells [37,38].…”

Section: Fusion With the Plasma Membranementioning

confidence: 99%

HIV entry: a game of hide-and-fuse?

Melikyan

2014

Current Opinion in Virology

101

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Human Immunodeficiency Virus (HIV) initiates infection by fusing its envelope membrane with the cell membrane through a process which is triggered through interactions with the cellular receptor and coreceptor. While the mechanism of HIV fusion has been extensively studied, the point of its entry into cells remains controversial. HIV has long been thought to fuse directly with the cell plasma membrane. However, several lines of evidence suggest that endocytic entry of HIV can lead to infection and, moreover, that endocytosis could be the predominant HIV entry pathway into different cell types. This review discusses recent findings pertinent to HIV entry routes and novel approaches to pinpoint the sites of virus entry.

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HIV-1 requires Arf6-mediated membrane dynamics to efficiently enter and infect T lymphocytes

Cited by 41 publications

References 91 publications

ADP Ribosylation Factor 1 Activity Is Required To Recruit AP-1 to the Major Histocompatibility Complex Class I (MHC-I) Cytoplasmic Tail and Disrupt MHC-I Trafficking in HIV-1-Infected Primary T Cells

ADP Ribosylation Factor 1 Activity Is Required To Recruit AP-1 to the Major Histocompatibility Complex Class I (MHC-I) Cytoplasmic Tail and Disrupt MHC-I Trafficking in HIV-1-Infected Primary T Cells

Syntenin-ALIX exosome biogenesis and budding into multivesicular bodies are controlled by ARF6 and PLD2

HIV entry: a game of hide-and-fuse?

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