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J. Biol. Chem., Vol. 280, Issue 32, 29025-29029, August 12, 2005

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Human T Cell Leukemia Virus Envelope Binding and Virus Entry Are Mediated by Distinct Domains of the Glucose Transporter GLUT1^*

Nicolas Manel, Jean-Luc Battini, Supported by the INSERM, and Marc Sitbon, Supported by the INSERM¶

From the Institut de Génétique Moléculaire de Montpellier, CNRS UMR 5535, IFR 122, 1919 route de Mende, F-34293 Montpellier Cedex 5, France

The glucose transporter GLUT1, a member of the multimembrane-spanning facilitative nutrient transporter family, serves as a receptor for human T cell leukemia virus (HTLV) infection. Here, we show 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. Glutamate residue 426 in ECL6 was identified as critical for binding. However, binding to ECL6 was not sufficient for HTLV envelope-driven infection. Infection required two additional determinants located in ECL1 and ECL5, which otherwise did not influence HTLV envelope binding. Moreover the single N-glycosylation chain located in ECL1 was not required for HTLV infection. Therefore, binding involves a discrete determinant in the carboxyl terminal ECL6, whereas post-binding events engage extracellular sequences in the amino and carboxyl terminus of GLUT1.

Received for publication, April 26, 2005 , and in revised form, June 8, 2005.

^* This work was supported in part by grants from the Association pour la Recherche sur le Cancer (Nos. 5989 and 3424), Fondation de France (Nos. 2291 and 2138), and the Association Française contre les Myopathies (No. 7706) (to M. S.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Supported by a graduate student fellowship from the Ministère del' Education Nationale de la Recherche et de la Technologie.

To whom correspondence may be addressed. Tel.: 33-467-613-640; Fax: 33-467-040-231; E-mail: jean-luc.battini{at}igmm.cnrs.fr. ¶ To whom correspondence may be addressed. Tel.: 33-467-613-640; Fax: 33-467-040-231; E-mail: marc.sitbon{at}igmm.cnrs.fr.

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