The envelope glycoprotein of human endogenous retrovirus type W uses a divergent family of amino acid transporters/cell surface receptors

Dimitri Lavillette, Mariana Marin, Alessia Ruggieri, François Mallet, François Loïc Cosset, David Kabat

Research output: Contribution to journalArticle

134 Citations (Scopus)

Abstract

The human endogenous retrovirus type W (HERV-W) family includes proviruses with intact protein-coding regions that appear to be under selection pressure, suggesting that some HERV-W proviruses may remain active in higher primates. The envelope glycoprotein (Env) encoded by HERV-W is highly fusogenic, is naturally expressed in human placental syncytiatrophoblasts, and has been reported to function as a super-antigen in lymphocyte cultures. Recent evidence suggested that HERV-W Env can mediate syncytium formation by interacting with the human sodium-dependent neutral amino acid transporter type 2 (hASCT2; gene name, SLC1A5) (J.-L. Blond, D. Lavillette, V. Cheynet, O. Bouton, G. Oriol, S. Chapel-Fernandez, B. Mandrand, F. Mallet, and F.-L. Cosset, J. Virol. 74:3321-3329, 2000) and that it can pseudotype human immunodeficiency virus cores (D. S. An, Y. Xie, and I. S. Y. Chen, J. Virol. 75:3488-3489, 2001). By using cell-cell fusion and pseudotype virion infection assays, we found that HERV-W Env efficiently uses both hASCT2 and the related transporter hASCT1 (gene name, SLC1A4) as receptors. In addition, although HERV-W Env mediates only slight syncytium formation or infection of mouse cells, it utilizes the mouse transporters mASCT1 and mASCT2 when their sites for N-linked glycosylation are eliminated by mutagenesis. Consistent with their role as a battlefield in host-virus coevolution, the viral recognition regions in ASCT1 and ASCT2 of humans and mice are highly divergent compared with other regions of these proteins, and their ratios of nonsynonymous to synonymous nucleotide sequence changes are extremely large. The recognition of ASCT1 and ASCT2 despite this divergence of their sequences strongly suggests that the use of both receptors has been highly advantageous for survival and evolution of the HERV-W family of retroviruses.

Original languageEnglish (US)
Pages (from-to)6442-6452
Number of pages11
JournalJournal of Virology
Volume76
Issue number13
DOIs
StatePublished - 2002

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Retroviridae
amino acid transporters
Endogenous Retroviruses
Amino Acid Transport Systems
Cell Surface Receptors
glycoproteins
Glycoproteins
receptors
Proviruses
cells
Giant Cells
proviruses
Names
Neutral Amino Acid Transport Systems
giant cells
env Gene Products
transporters
Cell Fusion
mice
Infection

ASJC Scopus subject areas

  • Immunology

Cite this

The envelope glycoprotein of human endogenous retrovirus type W uses a divergent family of amino acid transporters/cell surface receptors. / Lavillette, Dimitri; Marin, Mariana; Ruggieri, Alessia; Mallet, François; Cosset, François Loïc; Kabat, David.

In: Journal of Virology, Vol. 76, No. 13, 2002, p. 6442-6452.

Research output: Contribution to journalArticle

Lavillette, Dimitri ; Marin, Mariana ; Ruggieri, Alessia ; Mallet, François ; Cosset, François Loïc ; Kabat, David. / The envelope glycoprotein of human endogenous retrovirus type W uses a divergent family of amino acid transporters/cell surface receptors. In: Journal of Virology. 2002 ; Vol. 76, No. 13. pp. 6442-6452.
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