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Originally published In Press as doi:10.1074/jbc.M504549200 on June 13, 2005

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{ddagger}, 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

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


   ABSTRACT
TOP
 ABSTRACT
INTRODUCTION
 MATERIALS AND METHODS
 RESULTS
 DISCUSSION
 REFERENCES
 
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.


   INTRODUCTION
TOP
 ABSTRACT
 INTRODUCTION
MATERIALS AND METHODS
 RESULTS
 DISCUSSION
 REFERENCES
 
Interactions of retroviral envelope glycoproteins (Env)1 with cell surface receptors govern the first steps of retroviral infection. Env mediates both virus binding to the cell surface and fusion of the viral and cellular membranes allowing productive viral entry. Env consists of an extracellular surface component (SU) and an associated transmembrane subunit (TM) harboring an amino-terminal fusion peptide (1). SU and TM are derived from the same polyprotein precursor (1), and it is generally accepted that initial interactions between SU and the receptor are sufficient to induce post-binding conformational changes of Env that unmask the TM fusion peptide (2).

Several Env determinants of gammaretroviruses distinctively involved in binding and post-binding events have been described (3–8). From the context of the cellular Env receptors, little is known concerning potential post-binding determinants and receptor conformational changes that follow SU binding (9, 10). In the case of HIV and other related lentiviruses, it has been shown that post-binding events involve the recruitment of additional molecules, co-receptors, that belong to the seven membrane-spanning chemokine receptor family (11). No such co-receptors have yet been reported for a non-lentiviral Env (12).

Human T cell leukemia virus (HTLV) is a complex deltaretrovirus characterized by several multispliced mRNAs that encode for regulatory proteins. However, despite the large phylogenetic distance (13) between HTLV and simple gammaretroviruses, HTLV and murine leukemia viruses (MLVs) share a common general organization of Env (14–16). Their respective SU are composed of an amino-terminal RBD (14–18) followed by a central proline-rich region (15, 19) and a carboxyl-terminal domain that harbors a conserved (20) and highly reactive CXXC motif (6, 8). Furthermore, the HTLV Env receptor, the glucose transporter 1 (GLUT1) (21), is a multimembrane-spanning molecule, like all identified gammaretrovirus receptors (22).

In this context, we sought to identify GLUT1 determinants that are involved in the different steps of HTLV Env-mediated viral entry. GLUT1, a member of the class I family of glucose transporters, together with GLUT2, GLUT3, and GLUT4 (23) and GLUT14 (24), is a uniport carrier that passively facilitates glucose transport across membranes by switching between two conformational states (25). Biochemical data and modelization indicate that GLUT1 is a type 2 integral membrane protein composed of 12 transmembrane domains that delineate 6 extracellular loops (ECL) (26) (Fig. 1A). GLUT3, the closest isoform of GLUT1, has a similar predicted structure with six ECL but does not allow HTLV Env-mediated binding and infection. All six GLUT1 and GLUT3 ECL sequences present extensive residue differences and their carboxyl-terminal cytoplasmic tails confer different cell trafficking properties to the two transporters (27). Using GLUT1-GLUT3 chimeras and single residue mutants, we identified 7 amino acids in the GLUT1 ECL6 as the sole determinant able to confer HTLV Env binding properties to GLUT3. However, this determinant was not sufficient to mediate viral entry. Indeed, we found that GLUT1 harbors other non-binding determinants whose concomitant presence in GLUT3 was required for viral entry, thereby demonstrating the dual importance of GLUT1 binding and post-binding events for HTLV infection.


   MATERIALS AND METHODS
TOP
 ABSTRACT
 INTRODUCTION
 MATERIALS AND METHODS
RESULTS
 DISCUSSION
 REFERENCES
 
Plasmids—All chimeric and point mutant constructs were derived from pCHIX.GLUT1 and pCHIX.GLUT3, each harboring two COOH-terminal HA tags (21). The fragments encompassing the extracellular loops were exchanged using the following restriction sites (positions refer to GLUT1 coding sequence): MscI (206), ApaI (461), SacI (781), StuI (1017), and ApaI (1188). The ApaI sites at position 461 in GLUT1 and position 1188 in GLUT3, the SacI site in GLUT1, as well as point mutations N45Q, E426A, Q427A, and L428A in GLUT1 were introduced by the QuikChange site-directed mutagenesis protocol. PCR-amplified regions and ligation boundaries were checked by automated DNA sequencing. pLXSN.NotI was obtained by inserting a NotI linker in place of the HpaI site of pLXSN (28). The GLUT1-HA, GLUT3-HA, and the chimeric constructs were subcloned in pLXSN.NotI using the flanking NotI-BamHI restriction sites.

Cells—Human 293T and bovine MDBK cells were grown in DMEM with high glucose (4.5 g/liter) with 10% fetal bovine serum at 37 °C and 5% CO2. MDBK cells were provided by P. Mangeat (Centre de Recherche en Biochimie Macromoléculaire, Montpellier, France) and O. Schwartz (Institut Pasteur, Paris). Transient transfection of 293T was performed by the calcium phosphate method.

Protein Expression and Immunoblots—293T cells were transfected and lysed as described (21). Unboiled lysates were loaded on a 12.5% SDS-PAGE and transferred onto polyvinylidene difluoride membranes after migration. Membranes were blocked in PBS containing 5% powdered milk and 0.5% Tween 20, probed with a 1:5000 dilution of a 12CA5 anti-HA mouse antibody (Roche Applied Science) for 1 h at room temperature, washed three times with PBS, 0.1% Tween 20, followed by incubation with a 1:20,000 dilution of a horseradish peroxidase-conjugated anti-mouse immunoglobulin for 1 h at room temperature. Immunoblots were subsequently washed three times with PBS, 0.1% Tween 20 and revealed by chemiluminescence (ECL+, Amersham Biosciences).

Binding Assay—5 x 105 cells were detached with PBS containing 1 mM EDTA and centrifuged at 4 °C, and the cell pellet was resuspended in cold DMEM containing 10% FBS. Cells were further incubated with either control supernatant obtained from pCDNA-transfected 293T cells or HRBD surpernatant obtained from 293T cells transfected with a vector encoding the HRBD-EGFP fusion protein (29). Following incubation at 37 °C for 30 min, cells were harvested by centrifugation, washed one time with 1 ml of PBS, 2% fetal bovine serum, 0.01% sodium azide, and resuspended in 500 µl of the same buffer. Cells were analyzed with a FACSCalibur (BD Biosciences).

Infections—A replication-defective LacZ retroviral vector was pseudotyped with either HTLV-2 or VSV-G envelopes as described previously (30). Stable MDBK cell lines were plated at 75,000 cells per well (12-well plates), and infections were performed in triplicate with two viral dilutions. Viral dilutions ranged between 1/2 and 1/200, depending on the titer of the original viral stock. Fresh medium was added 24 h later, and 5-bromo-4-chloro-3-indolyl-{beta}-D-galactopyranoside staining was performed at 48 h. Infection foci were counted under conditions where the viral dilution showed at least two foci but not more than 1000 for all wells.

Glucose Uptake—The hexose uptake assay was adapted from Manel et al. (21) using 2-deoxy-D-[1-3H]glucose (Amersham Biosciences). 105 MDBK stably expressing the panel of chimeric constructs were seeded in 6-well plates. The next day, cells were washed in PBS, incubated in serum-free DMEM, washed in serum/glucose-free DMEM, and incubated for 20 min in 500 µl of serum/glucose-free DMEM. Uptake was initiated by adding labeled deoxyglucose to a final concentration of 0.1 mM (2 µCi/ml), and cells were incubated for an additional 10 min. Cells were then washed three times in PBS and solubilized in 400 µl of 0.1% SDS. Three µl were used for Bradford normalization, and 3H incorporation in the remainder of the samples was counted.

Transductions—Retroviral vector particles were obtained by transfecting 293T cells with a VSV-G expression vector (31), a gag-pol expression vector (30), and a control or GLUT1-expressing pLXSN.NotI vector. MDBK cells stably expressing these vectors were obtained by transduction using viral supernatants followed by selection in G418 (1 g/liter).


   RESULTS
TOP
 ABSTRACT
 INTRODUCTION
 MATERIALS AND METHODS
 RESULTS
DISCUSSION
 REFERENCES
 
The Sixth Extracellular Loop of GLUT1 Mediates HTLV Env Binding—GLUT1 and GLUT3 share 63% amino acid sequence identity. Based on secondary structure predictions (26), we delineated six homologous fragments, each containing a single ECL (Fig. 1A), by either natural or introduced restriction sites and generated a series of GLUT1-GLUT3 chimeric molecules. Chimeras referred to by the parental origin of each ECL (1 or 3) were evaluated for HTLV Env binding (Fig. 1C). Most chimeras, with the exception of 133311 and 331333, were expressed at similar levels as parental constructs (Fig. 1B). HTLV Env binding was measured using soluble HTLV Env RBD protein fused to GFP (HRBD) (15, 29). An increase in HRBD binding, as revealed by the appearance of a new peak of highly fluorescent cells, was only observed upon expression of 333311, 333331, and 133311, to levels similar to that observed in GLUT1-transfected cells (Fig. 1C). These chimeras have the GLUT1 sixth fragment that harbors ECL6 in common. We derived two additional chimeric constructs in which all residues were those of GLUT3 with the exception of either 12 residues (residues 420–431) or the 7 residues (residues 423–429) that constitute the GLUT1 ECL6 (Fig. 2A). Both chimeras, designated 333331 (12) and 333331 (7), respectively, were expressed at similar levels (Fig. 2B) and increased HRBD binding (Fig. 2C). Therefore, the 7 amino acids of GLUT1 ECL6 were sufficient to confer HTLV Env binding activity to GLUT3.



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  		FIG. 1.
The COOH-terminal domain of GLUT1 is responsible for HTLV Env binding. A, schematic topological representation of GLUT1 (adapted from Hruz et al. (26)). Arrowheads indicate the boundaries of the six GLUT fragments as used for allelic exchanges, each containing a single ECL. The single N-glycosylation on residue 45 is indicated. B, expression of the HA-tagged chimeric molecules in transfected 293T cells as revealed by an anti-HA antibody. Cells were transfected with an empty vector (control) or a vector encoding HA-tagged parental GLUT1 and GLUT3 or a panel of GLUT1-GLUT3 chimeric molecules. Chimeras are identified according to the presence of parental GLUT1 ("1") or GLUT3 ("3") ECL by a six-letter code corresponding to the six fragments delineated above. C, Binding of the HTLV Env to control and transfected cells was assessed using HRBD-EGFP fusion protein. Fluorescence-activated cell sorter analyses showing binding to HRBD (solid histograms) or to control supernatant (open histograms) are presented.

 
Glu426, Gln427, and Leu428 are found only in GLUT1 ECL6 (Fig. 3A). Individual mutation of E426A, but not Q427A or L428A, dramatically reduced HRBD binding as compared with wild-type GLUT1 (Fig. 3B), despite similar levels of expression of all three mutants (Fig. 3C). These data indicate the crucial role of a single residue, Glu426, in HTLV Env binding to GLUT1.

Determinants of HTLV Env-mediated Infection on GLUT1— We next sought to determine whether ECL6-dependent HTLV Env binding to GLUT1-GLUT3 chimeras was sufficient to lead to subsequent viral entry and infection. Since most cell lines, including 293T cells, are readily infectable by HTLV Env-harboring virions, we used bovine MDBK cells that are relatively resistant to HTLV Env-mediated infection (32, 33). Indeed, it has been shown recently that ectopic expression of GLUT1 in MDBK cells significantly increases HTLV Env-mediated infection (34). MDBK cells were stably transduced with GLUT1, GLUT3, chimeric retroviral vectors, or a control empty vector. Infection of these cells with HTLV Env-pseudotyped virions consistently demonstrated titers that were 1–2 logs higher on GLUT1-expressing MDBK cells than on control or GLUT3-expressing cells (Fig. 4). In contrast, control VSV-G-pseudotyped virions had similar titers on all MDBK populations.



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  		FIG. 2.
Seven amino acids of the GLUT1 ECL6 constitute the HTLV Env binding determinant. A, alignment between GLUT1 and GLUT3 in a region that includes parts of the transmembrane 11 and 12 domains (TM 11 and TM 12) as well as ECL6. The sequences of the two minimal chimeric molecules tested, 333331 (12) and 333331 (7), harboring 12 and 7 amino acids from ECL6 of GLUT1, respectively, are indicated. Residues that are identical to GLUT1 sequence are indicated by dashes. B, expression of the chimeric HA-tagged molecules in total 293T cell extracts using an anti-HA antibody. C, HRBD binding to 293T cells transfected with a control vector or vectors encoding GLUT1, 333331 (12) or 333331 (7), was monitored by flow cytometry.

 



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  		FIG. 3.
Glu426 in GLUT1 ECL6 is a critical residue for HTLV Env binding. A, alignement of the extracellular loop 6 (ECL6) from the five members of the class I glucose transporter family and GLUT1 mutants. Residues identical to GLUT1 sequence in other GLUT isoforms are indicated by dashes. B, binding of HRBD to control 293T or 293T cells overexpressing wild-type GLUT1 or E426A, Q427A, and L428A mutants. C, expression of the wild-type and HA-tagged GLUT1 mutants in total cell extracts as assessed with an anti-HA antibody.

 



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  		FIG. 4.
Susceptibility of MDBK cells to HTLV Env-mediated infection requires GLUT1 ECL 1, 5, and 6. Titers of virions pseudotyped with HTLV-2 Env or VSV-G were measured on control MDBK cells or MDBK cells stably expressing a panel of chimeric GLUT molecules after retroviral transduction. Chimeras are the same as described in the legends for Figs. 1 and 2.

 
Interestingly, MDBK cells expressing a GLUT3 construct harboring the GLUT1 HTLV Env binding domain, namely 333331 and 333331 (12) and 333331 (7), did not show increased susceptibility to HTLV Env-mediated infection (Fig. 4). This indicated that GLUT1 ECL6 was not sufficient to mediate HTLV entry and prompted us to evaluate whether other precise GLUT1 determinants were involved in post-binding events. Indeed, ectopic expression of 333311 and 133331 led to slight increases in HTLV Env-mediated infection (p < 0.001), and cells expressing a GLUT chimera that combined fragments 1, 5, and 6 (133311) showed infection levels similar to that mediated by GLUT1 (Fig. 4).

As these data pointed to the role of ECL1 and -5 in post-binding events, it was important to assess whether Env binding was necessary for infection. To this end, ECL6 point mutants (E426A, Q427A, and L428A) were evaluated for HTLV Env-mediated infection. Only E426A, which was not able to bind HRBD, showed a quasi-complete drop of HTLV Env-mediated infection (Fig. 5A). The Q427A mutation, which did not affect Env binding, led to less important, albeit significant, decreases in HTLV titers (Fig. 5A; p < 0.02). The L428A mutation had no effect on HTLV titers. Thus, as binding via Glu426 is required for infection, residue Gln427 in ECL6 is likely to be involved in post-binding events.

Irrespective of HTLV Env binding properties, all chimeras increased deoxyglucose uptake. Expression of both 333311 and 333331 (12) chimeras led to an increase in uptake similar to that observed for parental GLUT1 (Table I). The E426A mutant significantly increased glucose uptake but to a lesser extent when compared with wild-type GLUT1. These data confirm correct targeting, folding, and transport function of these chimeras.


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  		TABLE I
Functional properties of GLUT1, GLUT3, GLUT1-GLUT3 chimeras, and GLUT1 mutants

 
Since post-binding events may involve distinct interactions of GLUT1 and GLUT3 with cytoplasmic factors, we further evaluated the contribution of the NH2-terminal intracellular tail adjacent to GLUT1 ECL1 in viral entry, as both motifs were present in 133311. Additional chimeric molecules that harbored GLUT1 ECL6 in combination with either the GLUT1 amino-terminal intracellular tail (residues 1–12) or ECL1 alone (residues 34–66) were generated. Increased viral titers were observed only with the latter construct (data not shown), demonstrating that post-binding events mediated by the first fragment of GLUT1 in the GLUT3 context were solely due to the extracellular loop.



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  		FIG. 5.
The Glu426 residue in GLUT1, and not N-glycosylation, is required for HTLV Env-mediated infection of MDBK cells. Titers of virions pseudotyped with HTLV-2 Env were measured on control MDBK cells or MDBK cells stably expressing wild-type GLUT1 or the E426A, Q427A, and L428A mutants (A) or the N45Q N-glycosylation mutant in ECL1 (B).

 
GLUT1 N-Glycosylation Is Not Required for HTLV Env-mediated Infection—N-Glycosylation of several retroviral receptors has previously been shown to inhibit viral entry (35–39). Since GLUT1 has a N-glycosylation site at Asn45 in ECL1, we evaluated the influence of this site on HTLV Env-mediated infection. The GLUT1 N45Q mutant had the expected increased electrophoretic migration as compared with wild-type GLUT1, due to suppression of this N-glycosylation site (data not shown). However, neither HTLV Env-mediated binding (data not shown) nor infection were affected (Fig. 5B). Therefore, the requirement of HTLV ECL1 in HTLV Env-mediated infection does not depend on its N-linked glycosylated chain.


   DISCUSSION
TOP
 ABSTRACT
 INTRODUCTION
 MATERIALS AND METHODS
 RESULTS
 DISCUSSION
REFERENCES
 
The binding of HTLV-1 and HTLV-2 Env to GLUT1 could be conferred to the heterologous GLUT3 glucose transporter by substitution of 7 amino acids constituting the sixth extracellular loop of GLUT1 (ECL6). However, productive viral entry required the presence of additional determinants located in loops 1 and 5, neither of which appeared to influence binding. This functional dichotomy of GLUT1 with regard to HTLV Env binding and subsequent viral entry steps was further supported by results obtained with the Q427A mutation in ECL6. Indeed, although GLUT1 Q427A exhibited full binding abilities, this mutant had a significant decrease in HTLV Env-mediated viral entry. Elucidation of the interactions between Gln427 in ECL6 and ECL5 in addition to those with the more remote amino-terminal ECL1 will likely provide further clues with regard to the conformational changes that contribute to both the glucose transporter and HTLV Env receptor and possibly other cellular functions (40) of GLUT1.

Disruption of GLUT1 single N-glycosylation had no effect on HTLV Env binding and infection. Nevertheless, various patterns of GLUT1 glycosylation have been described (41). The impact of these modifications as well as other post-translational modifications of GLUT1 on HTLV Env binding and HTLV Env-mediated infection remains to be determined.

Mutation of Glu426 in GLUT1 strongly reduced HTLV Env binding and infection; however, it only mildly affected glucose uptake (Table I). Furthermore, disruption of the glucose uptake activity of GLUT1 by introducing the Q161C mutation did not alter HTLV Env binding and infection (data not shown). This indicates that these different activities are mediated by distinct domains on GLUT1. It will thus be of interest to determine the mechanism involved in the inhibition of GLUT1 activity by HTLV Env (21).

The distinct trafficking properties of GLUT1 and GLUT3, previously documented in an epithelial cell line, depend on their COOH-terminal intracellular domains (27). In agreement with this report, we also observed that the COOH-terminal intracellular domain of GLUT1 and GLUT3 was responsible for differences in localization, with GLUT1 accumulating mainly into cytoplasmic vesicles and GLUT3 present predominantly at the plasma membrane (data not shown). However, these differences in overall compartmentation did not appear to influence HTLV Env binding and post-binding events in all constructs we tested. For example, introduction of the GLUT3 cytoplasmic tail in the GLUT1 background did not modify HTLV Env binding (data not shown). Similarly, 133311 and 333331 chimeras, which shared the same major vesicular localization as GLUT1, showed comparable HTLV Env binding due to the presence of the GLUT1 ECL6, while only 133311 allowed HTLV Env-mediated infection.

Mapping of viral entry or binding determinants on gammaretrovirus receptors has also made use of chimeric molecules (10, 42–45), but the presence of receptor determinants that distinctively control Env binding and post-binding viral entry has not been reported. In contrast, binding and post-binding entry determinants located within the viral Env have been characterized for an increasing number of gammaretroviruses (22). In the case of MLV, a disulfide bond-mediated association of SU and TM is isomerized upon binding into an intrasubunit disulfide bond in the SU. This event, which is dependent on a highly conserved CXXC (CWLC) motif in the MLV SU (20), is further controlled in cis or in trans by the amino-terminal RBD of the SU (3, 4). Interestingly, HTLV-Env also harbors a similar motif in its SU (CIVC). It is therefore tempting to propose that a similar isomerization occurs in HTLV Env, following binding to GLUT1 ECL6. It remains to be determined whether the post-binding events controlled by GLUT1 determinants are involved in the SU isomerization process. In addition, although no co-receptor has been formally identified for GLUT1, it will be of interest to determine whether these post-binding determinants act through the recruitment of co-receptors or co-factors or alternatively through conformational changes in GLUT1 that favor membrane fusion and productive virion entry.


   FOOTNOTES
 
* 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. Back

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

§ 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.

1 The abbreviations used are: Env, envelope glycoprotein; SU, surface component; TM, transmembrane subunit; HTLV, human T cell leukemia virus; MLV, murine leukemia virus; RBD, receptor binding domain; ECL, extracellular loop; HA, hemagglutinin; MDBK, Madin-Darby bovine kidney; DMEM, Dulbecco's modified Eagle's medium; PBS, phosphate-buffered saline; GFP, green fluorescent protein; EGFP, enhanced GFP; VSV-G, vesicular stomatitis virus G protein. Back


   ACKNOWLEDGMENTS
 
We thank S. Perkovska and G. Boissonnet for their help with the generation of some of the constructs, N. Taylor for insightful discussion and critical reading of the manuscript, and all the members of our laboratory for stimulating input.



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 ABSTRACT
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 MATERIALS AND METHODS
 RESULTS
 DISCUSSION
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