The Ubiquitous Glucose Transporter GLUT-1 Is a Receptor for HTLV

@article{Manel2003TheUG,
  title={The Ubiquitous Glucose Transporter GLUT-1 Is a Receptor for HTLV},
  author={Nicolas Manel and Felix J. Kim and Sandrina Kinet and Naomi Taylor and Marc Sitbon and Jean-Luc Battini},
  journal={Cell},
  year={2003},
  volume={115},
  pages={449-459}
}

Figures from this paper

HTLV envelopes and their receptor GLUT1, the ubiquitous glucose transporter: a new vision on HTLV infection?
TLDR
Several molecular, viral, cellular and physiological aspects of HTLV infection in relation to the in vivo and in vitro properties of GLUT1 are reviewed and new schemes that emphasize the potential metabolic alterations caused in different cellular compartments are proposed.
Expression of Glucose Transporter 1 Confers Susceptibility to Human T-Cell Leukemia Virus Envelope-Mediated Fusion
TLDR
It is shown that expression of glut-1 in relatively resistant MDBK cells conferred increased susceptibility to both HTLV-1- andHTLV-2-pseudotyped particles, and this results provide additional evidence that glut- 1 is a receptor for HTLV.
Human T Cell Leukemia Virus Envelope Binding and Virus Entry Are Mediated by Distinct Domains of the Glucose Transporter GLUT1*
TLDR
It is shown that the 7 amino acids of the extracellular loop 6 of GLUT1 (ECL6) placed in the context of the related GLUT3 transporter were sufficient for HTLV envelope binding.
Isolated receptor binding domains of HTLV-1 and HTLV-2 envelopes bind Glut-1 on activated CD4+ and CD8+ T cells
TLDR
Transfection of Glut-1 directly correlates with the capacities ofHTLV-1 and HTLV-2 envelope-derived ligands to bind cells, and is induced by TCR engagement, resulting in massive increases in glucose uptake and binding of HTLV1 and -2 envelopes to both CD4 and CD8 T lymphocytes.
GLUT1 Is Not the Primary Binding Receptor but Is Associated with Cell-to-Cell Transmission of Human T-Cell Leukemia Virus Type 1
TLDR
Although increasing cell surface levels of GLUT1 enhanced HTLV-I transfer, efficient virus spread correlated largely with heparan sulfate proteoglycan (HSPG) expression on target cells, indicating thatGLUT1 and HSPGs are important for efficient cell-to-cell transmission of HTLV -1 but raise concerns on the role of GLut1 as theHTLV-1 primary binding receptor.
Separate Cellular Localizations of Human T-Lymphotropic Virus 1 (HTLV-1) Env and Glucose Transporter Type 1 (GLUT1) Are Required for HTLV-1 Env-Mediated Fusion and Infection
TLDR
It is found that a large amount of GLUT1 or translocation ofGLUT1 to the plasma membrane from intracellular compartments in virus-producing cells enhances the colocalization and interaction of GLut1 with HTLV-1 Env, leading to the inhibition of cell fusion activity and infectivity.
Interaction between the HTLV-1 envelope and cellular proteins: impact on virus infection and restriction.
TLDR
The first human retrovirus, human T-lymphotropic virus 1 (HTLV-1), was discovered 30 years ago and its interactions with cellular proteins, enabling the virus to traffic by exploiting cellular delivery pathways, are reviewed.
Neuropilin-1 Is Involved in Human T-Cell Lymphotropic Virus Type 1 Entry
TLDR
It is shown that Neuropilin-1 (NRP1), the receptor for semaphorin-3A and VEGF-A165 and a member of the immune synapse, is also a physical and functional partner of HTLV-1 envelope (Env) proteins.
...
...

References

SHOWING 1-10 OF 109 REFERENCES
The HTLV receptor is a widely expressed protein.
TLDR
The receptor for human T-cell leukemia virus type 1 (HTLV-1) was found to be expressed on a broad range of cell lines derived from multiple species and was partially resistant to ammonium chloride.
The HTLV receptor is an early T-cell activation marker whose expression requires de novo protein synthesis.
TLDR
Up-regulation of the HTLV receptor, via signals transmitted through the IL-7 cytokine receptor as well as the TCR, is likely to contribute to the mother-to-infant transmission and spreading of HTLV-1.
HTLV-1-induced cell fusion is limited at two distinct steps in the fusion pathway after receptor binding.
TLDR
HTLV-1 fusion is a multistep process which is susceptible to inhibition at two seperate stages of the fusion pathway post receptor binding, and the inefficient infection by cell-free virions may explain the poor infectivity of HTLV- 1 in vivo and suggests strategies for preventative therapy.
Human T-Cell Leukemia Virus Type 1 Receptor Expression among Syncytium-Resistant Cell Lines Revealed by a Novel Surface Glycoprotein-Immunoadhesin
TLDR
It is suggested that for some HTLV-1-resistant cell lines the block to viral entry occurs at a late post-receptor-binding step of the entry process, which will be of value in developing new strategies to identify the cellular receptor used by HTLV -1.
Protein interactions with the glucose transporter binding protein GLUT1CBP that provide a link between GLUT1 and the cytoskeleton.
TLDR
The identification and characterization of a protein, GLUT1 C-terminal binding protein (GLUT1CBP), that binds via a PDZ domain to the C terminus of GLut1 that implicate GLUT 1CBP in cellular mechanisms for targeting GLUT2 to specific subcellular sites either by tethering the transporter to cytoskeletal motor proteins or by anchoring theporter to the actin cytoskeleton.
Facilitative glucose transporters.
TLDR
This review summarizes recent advances concerning the structure, function, and regulation of the Glut proteins.
Regulation of the cell-surface expression of an HTLV-I binding protein in human T cells during immune activation.
TLDR
Results indicate that cell-surface expression of the HTLV SU binding protein is up-regulated during in vitro activation and suggest a role for theHTLV-I SU binding proteins in the immunobiology of CD4(+) T cells.
Analysis of Functional Conservation in the Surface and Transmembrane Glycoprotein Subunits of Human T-Cell Leukemia Virus Type 1 (HTLV-1) and HTLV-2
TLDR
Although they recognize the same receptor, the HTLV-1 andHTLV-2 SU subunits have slightly different ways of transducing the conformational information that primes a common fusion mechanism effected by similar TM subunits, suggesting that the glycoproteins function in broadly similar ways.
Changes in glucose transport and transporter isoforms during the activation of human peripheral blood lymphocytes by phytohemagglutinin.
TLDR
It is concluded that PHA stimulation increases glucose transport partly by inducing the expression of GLUT-1 instead ofGLUT-3 and that GLut-1 expression is induced by signals generated by IL-2 binding to its high affinity receptors.
Influence of transmembrane domains on the fusogenic abilities of human and murine leukemia retrovirus envelopes.
TLDR
The results indicate that these two domains in F-MuLV and HTLV-1 constitute structural entities with similar fusogenic properties, however, in the absence of a cytoplasmic domain, the F- MuLV membrane-spanning domain appeared to confer weaker fUSogenic properties than the HT LV-1 membrane- spanning domain.
...
...