Cell Surface Receptors for Gammaretroviruses

Tailor, Chetankumar S.; Lavillette, Dimitri; Marin, Mariana; Kabat, David

doi:10.1007/978-3-642-19012-4_2

Cited by 60 publications

(76 citation statements)

References 354 publications

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“…All of the gammaretrovirus receptors identified to date employ glycosylated carrier facilitator proteins as receptors (Tailor et al, 2003); therefore, it is not surprising that the cell-specific addition of N-linked sugars to receptor proteins has evolved as a method for restricting efficient infection by gammaretroviruses (Overbaugh et al, 2001;Tailor et al, 2000). The ASCT1, Pit1 and Pit2 receptors have all been reported to be inactivated by glycosylation in some types of cell and hence fail to facilitate entry by the feline endogenous retrovirus RD114, gibbon ape leukemia virus and amphotropic MLV, respectively.…”

Section: Mechanism Of Glycosylation-mediated Loss Of Receptor Functiomentioning

confidence: 99%

“…The CAT1 protein is a 14-transmembrane multi-spanning molecule comprised of seven extracellular and six cytoplasmic loops with two conserved N-linked glycosylation sites (Asn 223 and Asn 229). The third extracellular loop (ECL3) appears to be critical for ecotropic retrovirus receptor function (Albritton et al, 1989;Overbaugh et al, 2001;Sommerfelt, 1999;Tailor et al, 2003). Previous studies have shown that the integrity of the 235 YGE 237 motif in ECL3 is essential for MLV receptor function (Albritton et al, 1993;Yoshimoto et al, 1993).…”

Section: Introductionmentioning

confidence: 99%

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Mechanisms underlying glycosylation-mediated loss of ecotropic receptor function in murine MDTF cells and implications for receptor evolution

Yoshii

Kamiyama

Arima

et al. 2008

Journal of General Virology

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A Mus dunni tail fibroblast (MDTF) cell line is highly resistant to infection by ecotropic Moloney murine leukemia virus (Mo-MLV). The cationic amino acid transporter type 1 (CAT1) paralogues of murine NIH 3T3 and MDTF cells (mCAT1 and dCAT1, respectively) contain two conserved N-linked glycosylation sites in the third extracellular loop (ECL3, the putative Mo-MLV binding site). Glycosylation of dCAT1 inhibits Mo-MLV infection, but that of mCAT1 does not. Compared with mCAT1, dCAT1 possesses an Ile-to-Val substitution at position 214 and a Gly insertion at position 236 in the ECL3. To determine the residues responsible for the loss of dCAT1 receptor function, mutants of mCAT1 were constructed. The mCAT1/insG receptor (with a Gly residue inserted at mCAT1 position 236) had greatly reduced Mo-MLV receptor function compared with mCAT1. Treatment of mCAT1/insG-expressing cells with tunicamycin, an N-linked glycosylation inhibitor, increased the transduction titre. In addition, the reduced susceptibility to Mo-MLV observed with mCAT1/insG-expressing cells correlated with impaired binding of Mo-MLV. These results show that a single amino acid insertion confers mCAT1 receptor properties on dCAT1 and provide an important insight into the co-evolution of virus-host interactions.

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Section: Mechanism Of Glycosylation-mediated Loss Of Receptor Functiomentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Mechanisms underlying glycosylation-mediated loss of ecotropic receptor function in murine MDTF cells and implications for receptor evolution

Yoshii

Kamiyama

Arima

et al. 2008

Journal of General Virology

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“…Mammalian gammaretroviruses use nutrient transporters as receptors Gammaretrovirus receptors identified to date are either multimembrane-spanning nutrient transporters or, for those of unknown function, have a structure that is compatible with nutrient transport functions (Tailor et al, 2003) (Table 1). The closely related structural organization of HTLV and gammaretrovirus Env (Figure 2) led us to predict that the HTLV receptor would also be a member of this family of molecules (Kim et al, 2000).…”

Section: Htlv Receptor and Coreceptor Candidatesmentioning

confidence: 99%

“…Thus, it is possible that upon 'capture' of an env gene, intracellular interactions between Env and its cell receptor foster the routing of the virus out of the cell (Kim et al, 2004a). Therefore, evaluating the contribution of Env-receptor interactions in viral egress might provide additional clues on the exclusive selection by gammaretroviruses and HTLV of nutrient transporters as Env receptors (Tailor et al, 2003).…”

Section: Htlv Receptor and Coreceptor Candidatesmentioning

confidence: 99%

HTLV-1 tropism and envelope receptor

et al. 2005

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The identification of CD4 as the primary receptor for HIV followed shortly after the discovery of the virus, but the HTLV receptor remained long elusive, until its recent identification as the GLUT1 glucose transporter. In the present review, we describe the status of the literature that surrounded this discovery as well as the in vitro and in vivo observations that led to the identification of GLUT1. Also, we will explore a few tracks to conciliate the in vitro and in vivo data on HTLV-1 tropism within the context of the HTLV literature that has accumulated over the past 25 years. A close examination of these data leads us to conclude that the preferential detection of HTLV-1 in CD4 þ T lymphocyte subsets in vivo, even in the absence of leukemia, is not likely to be directly related to envelope receptor interactions, but rather to an array of postentry selection bottlenecks in vivo. Furthermore, we propose that infection of other hematopoietic and nonhematopoietic cells is likely to take place during the lifetime of an individual, with a burst early during the infection. Oncogene (2005) 24, 6016-6025.

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“…Using a soluble-tagged construct encompassing this region (H RBD ), we were able to track HTLV receptor expression in lymphocyte subsets (28) and identified Glut1, the ubiquitous vertebrate glucose as a receptor for HTLV-1 and -2 Env (19, 29 -31). It is of particular interest that Glut1, a deltaretrovirus receptor, like all other identified gammaretrovirus receptors, is a multimembrane-spanning nutrient transporter (19,24,32).…”

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confidence: 99%

Cell Surface Expression of the Bovine Leukemia Virus-Binding Receptor on B and T Lymphocytes Is Induced by Receptor Engagement

Lavanya

Kinet

Montel‐Hagen

et al. 2008

The Journal of Immunology

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Bovine leukemia virus (BLV), one of the most common infectious viruses of cattle, is endemic in many herds. Approximately 30–40% of adult cows in the United States are infected by this oncogenic C-type retrovirus and 1–5% of animals will eventually develop a malignant lymphoma. BLV, like the human and simian T cell leukemia viruses, is a deltaretrovirus but, in contrast with the latter, the BLV receptor remains unidentified. In this study, we demonstrate that the amino-terminal 182 residues of the BLV envelope glycoprotein surface unit encompasses the receptor-binding domain. A bona fide interaction of this receptor-binding domain with the BLV receptor was demonstrated by specific interference with BLV, but not human T cell leukemia virus, envelope glycoprotein-mediated binding. We generated a rabbit Ig Fc-tagged BLV receptor-binding domain construct and ascertained that the ligand binds the BLV receptor on target cells from multiple species. Using this tool, we determined that the BLV-binding receptor is expressed on differentiating pro/pre-B cells in mouse bone marrow. However, the receptor was not detected on mature/quiescent B cells but was induced upon B cell activation. Activation of human B and T lymphocytes also induced surface BLV-binding receptor expression and required de novo protein synthesis. Receptor levels were down-regulated as activated lymphocytes returned to quiescence. In the human thymus, BLV-binding receptor expression was specifically detected on thymocytes responding to the IL-7 cytokine. Thus, expression of the BLV-binding receptor is a marker of enhanced metabolic activity in B cells, T cells, and thymocytes.

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Cell Surface Receptors for Gammaretroviruses

Cited by 60 publications

References 354 publications

Mechanisms underlying glycosylation-mediated loss of ecotropic receptor function in murine MDTF cells and implications for receptor evolution

Mechanisms underlying glycosylation-mediated loss of ecotropic receptor function in murine MDTF cells and implications for receptor evolution

HTLV-1 tropism and envelope receptor

Cell Surface Expression of the Bovine Leukemia Virus-Binding Receptor on B and T Lymphocytes Is Induced by Receptor Engagement

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