Alteration of intracellular potassium and sodium concentrations correlates with induction of cytopathic effects by human immunodeficiency virus

Voss, Thomas G.; Fermin, César D.; Levy, Jay A.; Vígh, S.; Choi, Bok Kyoung; Garry, Robert F.

doi:10.1128/jvi.70.8.5447-5454.1996

Cited by 38 publications

(23 citation statements)

References 62 publications

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“…These data indicate that during acute infection of RH9 cells, there was a marked decrease in pH i coincident with the appearance of HIV-specific CPE. As previously described, HIV-1 LAI infection of RH9 cells results in an increase in [K ϩ ] i (54). [K ϩ ] i in acutely infected RH9 cells peaked at about 400 mM at 2 days postinfection, as determined using PBFI, a K ϩ -sensitive fluorescent probe.…”

Section: Alterations Of Ph I In T-lymphoblastoid Cells Acutely Infectmentioning

confidence: 56%

“…Alterations in plasma membrane function induced by several cytolytic viruses result in changes in the intracellular content of ions and other small molecules. Previously we and others have shown that infection by HIV alters the intracellular concentrations of several ions, including Na ϩ and K ϩ (54). Cytopathic strains of HIV-1 increased intracellular Na ϩ and K ϩ concentrations ([Na ϩ ] i and [K ϩ ] i ) to a greater extent than HIV-1 strains with lower cytopathic potential.…”

mentioning

confidence: 88%

“…Therefore, the ratio of emission intensity at Ͻ535 to that at Ͼ575 nm can be used to eliminate signal errors caused by variations in concentration, path length, leakage, and photobleaching. [K ϩ i ] in HIV-infected RH9 cells was measured by similar methods, using the K ϩ -sensitive probe potassium-binding benzofuran isophthalate-acetoxymethyl ester (PBFI-AM) as previously described (54). After addition of BCECF-AM or PBFI-AM at a final concentration of 20 or 10 M, cells were incubated for 2.0 h. Cells were then washed and examined by using a fluorescence concentration analyzer (Idexx Laboratories, Westbrook, Maine) or fluorescence microscopy and video imaging.…”

Section: Cells and Virusesmentioning

confidence: 99%

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Human immunodeficiency virus infection of T-lymphoblastoid cells reduces intracellular pH

Makutonina

Voss

Plymale

et al. 1996

J Virol

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Alterations in plasma membrane function are induced by many cytopathic viruses, including human immunodeficiency virus type 1 (HIV-1). These alterations can result in changes in the intracellular content of ions and other small molecules and can contribute to cytolysis and death of the infected cell. The pH-sensitive fluorescent probe 2,7-bis(2-carboxyethyl)-5,6-carboxyfluorescein-acetoxymethyl ester was used to quantitate intracellular pH (pH i ) in HIV-1-infected T cells. Infection of cells from the CD4 ؉ T-lymphoblastoid line HUT-78 (RH9 subclone) with HIV-1 strain LAI resulted in a significant decrease of pH i , from approximately 7.2 in mock-infected cells to below 6.7 by day 4 after infection, when cells were undergoing acute cytopathic effects. The pH i in persistently infected cells that survived the acute cytopathic effects of HIV-1 was approximately 6.8 to 7.0. Studies with amiloride, an inhibitor of the Na ؉ /H ؉ exchange system, suggest that HIV-1induced intracellular acidification in lymphocytes is due, in part, to dysfunction of this plasma membrane ion transport system. The alterations in pH i may mediate certain cytopathic effects of HIV-1, thereby contributing to depletion of CD4 ؉ T lymphocytes in patients with AIDS.

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Section: Alterations Of Ph I In T-lymphoblastoid Cells Acutely Infectmentioning

confidence: 56%

mentioning

confidence: 88%

Section: Cells and Virusesmentioning

confidence: 99%

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Human immunodeficiency virus infection of T-lymphoblastoid cells reduces intracellular pH

Makutonina

Voss

Plymale

et al. 1996

J Virol

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“…How does the BEC1/gp120 interaction fit into this scenario? Notably, HIV-infection of human PBMC caused an increase of intracellular K + levels that correlated with HIV-1-induced cytopathic effects [17]. Since BEC1 transports K + out of the cell, BEC1 inhibition is likely to cause increased intracellular K + concentration.…”

Section: Discussionmentioning

confidence: 99%

Interaction of human immunodeficiency virus gp120 with the voltage‐gated potassium channel BEC1

Herrmann¹,

Ruprecht²,

Sauter³

et al. 2010

FEBS Letters

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a b s t r a c tRetrovirus replication critically depends on a dynamic interplay between retroviral and host proteins. We report on the binding of the surface subunit (glycoprotein 120 (gp120)) of the human immunodeficiency virus type 1 (HIV-1) envelope protein (Env) to the cytoplasmic C-terminus of the voltage-gated potassium channel BEC1 (brain-specific ether-a-go-go-like channel 1), an interaction that can result in the repression of BEC's activity and the inhibition of HIV-1 particle-release. BEC1 protein was found to be expressed in T cells and macrophages, the major target cells of HIV-1. Thus, gp120/BEC1 interaction may be involved in HIV-1 life cycle and/or pathogenesis. Structured summary:MINT-7968695: BEC1 (uniprotkb:Q9ULD8) physically interacts (MI:0915) with gp160 (uniprotkb:P04578) by anti bait coimmunoprecipitation (MI:0006) MINT-7968714: BEC1 (uniprotkb:Q9ULD8) physically interacts (MI:0915) with gp160 (uniprotkb:P04578) by anti tag coimmunoprecipitation (MI:0007) MINT-7968675: BEC1 (uniprotkb:Q9ULD8) physically interacts (MI:0915) with gp160 (uniprotkb:P04578) by pull down (MI:0096)

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“…. On a FACSCalibur, the green fluorescent cells were gated at FL1, and their PBFI intensities were collected at the FL5 channel (excitation/emission: 350/500 nm) [40,41]. Membrane potentials were calculated with the measured [K ? ]…”

Section: Exosome/exovesicle Characterization By Flow Cytometrymentioning

confidence: 99%

Background K2P Channels KCNK3/9/15 Limit the Budding of Cell Membrane-derived Vesicles

Chi

Chen

Lee

et al. 2011

Cell Biochem Biophys

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The main function of background two-pore potassium (K(2P)) channels KCNK3/9/15 is to stabilize the cell membrane potential. We previously observed that membrane potential depolarization enhances the release of HIV-1 viruses. Because membrane polarization affects the biomembrane directly, here we examined the effects of KCNK3/9/15 on the budding of nonviral vesicles. We found that depolarization by knocking down endogenous KCNK3/9/15 promoted secretion of cell-derived vesicles. We further used Vpu (an antagonist of KCNK3) as a model for the in vivo study of depolarization-stimulated secretion. Vpu is a HIV-1-encoded, ion channel-like protein (viroporin) capable of enhancing virus release and depolarizing the cell membrane potential. We found that Vpu could also promote nonviral vesicle release, perhaps through a similar mechanism that Vpu utilizes to promote viral particle release. Notably, T cells expressing Vpu alone became pathologically low in intracellular K(+) and insensitive to extracellular K(+) or membrane potential stimulation. In contrast, heterologous expression of KCNK3 in T cells stabilized the cell potentials by maintaining intracellular K(+). We thus concluded that KCNK3/9/15 expression limits membrane depolarization and depolarization-induced secretion at least in part by maintaining intracellular K(+).

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Alteration of intracellular potassium and sodium concentrations correlates with induction of cytopathic effects by human immunodeficiency virus

Cited by 38 publications

References 62 publications

Human immunodeficiency virus infection of T-lymphoblastoid cells reduces intracellular pH

Human immunodeficiency virus infection of T-lymphoblastoid cells reduces intracellular pH

Interaction of human immunodeficiency virus gp120 with the voltage‐gated potassium channel BEC1

Background K2P Channels KCNK3/9/15 Limit the Budding of Cell Membrane-derived Vesicles

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