Interaction of GB Virus C/Hepatitis G Virus Synthetic Peptides with Lipid Langmuir Monolayers and Large Unilamellar Vesicles

Pérez-López, Silvia; Vila-Romeu, Nuria; Esteller, Manel; Espina, Marta; Haro, Isabel; Mestres, C.

doi:10.1021/jp806938y

Cited by 16 publications

(18 citation statements)

References 45 publications

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“…Maxima pressures achieved are closely similar to those described in [12] for a 24 Aa peptide, although extrapolated area/ molecule values are smaller in our case, suggesting a random coil structure. Moreover, the shape and slope of isotherms are also similar to those described in previous papers [13][14][15]. The value of extrapolated area gives an indication of the cross-sectional area of the peptide chain lying at the interface.…”

Section: K-a Isotherms Of Mixed Monolayerssupporting

confidence: 83%

Physicochemical characterisation of four peptide sequences related to thrombospondin-1B

Reig

Ortiz²,

Alsina³

2011

Journal of Colloid and Interface Science

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Section: K-a Isotherms Of Mixed Monolayerssupporting

confidence: 83%

Physicochemical characterisation of four peptide sequences related to thrombospondin-1B

Reig

Ortiz²,

Alsina³

2011

Journal of Colloid and Interface Science

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“…Two E1 fusion peptides were also proposed as internal fusion peptides based on predicted lipid-interacting structures: 53–66 AGLAVRPGKSAAQL [65] and 145–162 WKVPFDFWRGVISLTPLL [66]. Further studies of the candidate fusion peptides in the context of viral particles are needed to determine if these domains are truly involved in fusion events.…”

Section: Gb Virus C Envelope Glycoproteinsmentioning

confidence: 99%

“…Recent studies examining peptide adsorption at air/water interfaces and their interaction with phospholipid monolayers identified other potential fusion peptides within GBV-C E2: 267-284 LLGTEVSEVLGGAGLTGG [63] and 347-363 VLLYLMKLAEARLVPLI [64]. Two E1 fusion peptides were also proposed as internal fusion peptides based on predicted lipid-interacting structures: 53-66 AGLAVRPGKSAAQL [65] and 145-162 WKVPFDFWRGVISLTPLL [66]. Further studies of the candidate fusion peptides in the context of viral particles are needed to determine if these domains are truly involved in fusion events.…”

Section: Fusion Peptidesmentioning

confidence: 99%

GB virus type C interactions with HIV: the role of envelope glycoproteins

Mohr

Stapleton

2009

Journal of Viral Hepatitis

110

180

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SUMMARY GB virus C/hepatitis G virus (GBV-C/HGV) is the most closely related human virus to hepatitis C virus (HCV). GBV-C is lymphotropic and not associated with any known disease, although it is associated with improved survival in HIV-infected individuals. In peripheral blood mononuclear cells, GBV-C induces the release of soluble ligands for HIV entry receptors (RANTES, MIP-1a, MIP-1b and SDF-1), suggesting that GBV-C may interact with lymphocytes to induce a chemokine and/or cytokine milieu that is inhibitory to HIV infection. Expression of GBV-C envelope glycoprotein E2 in CD4+ T cells or addition of recombinant E2 to CD4 cells recapitulates the HIV inhibition seen with GBV-C infection. Like HCV E2, GBV-C E2 is predicted to be post-translationally processed in the endoplasmic reticulum and is involved with cell binding. The C-termini of GBV-C E1 and E2 proteins contain predicted transmembrane domains sharing features with HCV TM domains. To date, cellular receptor(s) for GBV-C E2 have not been identified. GBV-C E2-mediated HIV inhibition is dose-dependent and HIV replication is blocked at the binding and/or entry step. In addition, a putative GBV-C E2 fusion peptide interferes with HIV gp41 peptide oligomerization required for HIV-1 fusion, further suggesting that GBV-C E2 may inhibit HIV entry. Additional work is needed to identify the GBV-C E2 cellular receptor, characterize GBV-C E2 domains responsible for HIV inhibition, and to examine GBV-C E2-mediated fusion in the context of the entire envelope protein or viral-particles. Understanding the mechanisms of action may identify novel approaches to HIV therapy.

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“…(347-363) VLLYLMKLAEARLVPLI (Perez-Lopez et al, 2009a). Two E1 fusion peptides were also proposed as internal fusion peptides based on predicted lipidinteracting structures: E1 (53-66) AGLAVRPGKSAAQL (Perez-Lopez et al, 2009b) and E1 (145-162) WKVPFDFWRGVISLTPLL (Sanchez-Martin et al, 2009). Further studies of the candidate peptides in the context of viral particles are needed to determine if these domains are truly involved in fusion events.…”

Section: Fusion Peptidesmentioning

confidence: 99%

GB virus C

Mohr¹

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GB virus C (GBV-C) is a nonpathogenic lymphotropic virus that replicates in B and T lymphocytes. Infection with GBV-C is documented worldwide and is common: between 1% and 5% of healthy blood donors are viremic at the time of donation. Antibodies to GBV-C proteins are not usually detected during viremia, and antibodies to the GBV-C envelope glycoprotein E2 develop following the clearance of viremia. Although GBV-C viremia may persist for decades, viremia usually clears within 2 years following infection in the majority of individuals infected by blood transfusion. A chimpanzee variant of GBV-C, designated GBV-C cpz , is found in captive and noncaptive chimpanzees and its prevalence and natural history are uncharacterized. HIV-infected individuals who are co-infected with GBV-C survive longer than those without GBV-C. GBV-C infection of PBMCs inhibits the replication of HIV isolates and one of the mechanisms for this is the downregulation of HIV coreceptors and secretion of the coreceptor ligands. Additional mechanisms of HIV inhibition by GBV-C are examined in this dissertation. The GBV-C envelope glycoprotein E2 contributes directly to the inhibition of HIV infection. Incubation of recombinant E2 with PBMCs at 4°C prior to HIV infection results in a decrease in HIV replication, and only HIV enveloped pseudoparticle transduction, not VSV-G enveloped pseudoparticle transduction, is inhibited by GBV-C E2. This suggests that GBV-C E2 inhibits HIV infection at an entry step when the HIV envelope proteins interact with cellular receptors and membranes. How GBV-C E2 interacts with cellular surfaces and which cellular proteins are utilized for GBV-C binding and entry are unknown. Here, we characterize GBV-C E2 binding to human PBMCs, murine cells, and multiple transformed cell lines to identify the PBMC subset to which E2 binds and to identify candidate cellular receptors involved in GBV-C binding and entry. Understanding how GBV-C E2 interacts with cellular surfaces is critical to determining how it inhibits HIV entry. v ABSTRACT GB virus C (GBV-C) is a nonpathogenic lymphotropic virus that replicates in B and T lymphocytes. Infection with GBV-C is documented worldwide and is common: between 1% and 5% of healthy blood donors are viremic at the time of donation. Antibodies to GBV-C proteins are not usually detected during viremia, and antibodies to the GBV-C envelope glycoprotein E2 develop following the clearance of viremia. Although GBV-C viremia may persist for decades, viremia usually clears within 2 years following infection in the majority of individuals infected by blood transfusion. A chimpanzee variant of GBV-C, designated GBV-C cpz , is found in captive and noncaptive chimpanzees and its prevalence and natural history are uncharacterized. GBV-C research was initially performed by viral hepatitis research groups because it was predicted to cause hepatitis. The realization that GBV-C did not cause hepatitis resulted in a marked reduction in research activity. Because Hepatitis C virus co-infection worsens the cl...

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Interaction of GB Virus C/Hepatitis G Virus Synthetic Peptides with Lipid Langmuir Monolayers and Large Unilamellar Vesicles

Cited by 16 publications

References 45 publications

Physicochemical characterisation of four peptide sequences related to thrombospondin-1B

Physicochemical characterisation of four peptide sequences related to thrombospondin-1B

GB virus type C interactions with HIV: the role of envelope glycoproteins

GB virus C

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