Retrovirus receptors

Sommerfelt, Maja A.

doi:10.1099/0022-1317-80-12-3049

Cited by 70 publications

(67 citation statements)

References 125 publications

(143 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…These characteristics of the CAT1 protein may decrease the speed of evolution and cause a more complex evolutionary pathway. One of the reasons why most retroviral receptors have multiple membrane-spanning proteins such as mCAT1 (Sommerfelt, 1999) might be the reduced evolutionary rate of mutation among transporter proteins.…”

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%

See 1 more Smart Citation

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

View full text Add to dashboard Cite

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.

show abstract

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

View full text Add to dashboard Cite

show abstract

“…Many receptors for retroviruses have been identified that are either multiple or single membranespanning proteins (Sommerfelt, 1999). BLVRcp1, a cDNA encoding the candidate protein of the bovine leukaemia virus (BLV) receptor (BLVR), was cloned from an expression library of the bovine cell line MDBK, susceptible to BLV infection based on the binding property of bacterially expressed protein to BLV gp51 (Ban et al, 1993).…”

Section: Introductionmentioning

confidence: 99%

Evaluation of the δ subunit of bovine adaptor protein complex 3 as a receptor for bovine leukaemia virus

Suzuki

Matsubara

Kitani

et al. 2003

Journal of General Virology

View full text Add to dashboard Cite

“…One reported candidate (25) was later shown to correspond to the Ѩ subunit of the adaptor-protein complex AP3, involved in intracellular transport rather than cell surface binding (26). Notably, the unidentified receptor appears to be expressed in many tissues and across many species (27).…”

mentioning

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

View full text Add to dashboard Cite

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.

show abstract

Retrovirus receptors

Cited by 70 publications

References 125 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

Evaluation of the δ subunit of bovine adaptor protein complex 3 as a receptor for bovine leukaemia virus

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

Contact Info

Product

Resources

About