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J. Biol. Chem., Vol. 278, Issue 5, 3131-3136, January 31, 2003
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From the The human immunodeficiency virus (HIV)
envelope (Env) glycoprotein (gp) 120 is a highly disulfide-bonded
molecule that attaches HIV to the lymphocyte surface receptors CD4 and
CXCR4. Conformation changes within gp120 result from binding and
trigger HIV/cell fusion. Inhibition of lymphocyte surface-associated
protein-disulfide isomerase (PDI) blocks HIV/cell fusion, suggesting
that redox changes within Env are required. Using a sensitive assay
based on a thiol reagent, we show that (i) the thiol content of gp120, either secreted by mammalian cells or bound to a lymphocyte surface enabling CD4 but not CXCR4 binding, was 0.5-1 pmol SH/pmol gp120 (SH/gp120), whereas that of gp120 after its interaction with a surface
enabling both CD4 and CXCR4 binding was raised to 4 SH/gp120; (ii) PDI
inhibitors prevented this change; and (iii) gp120 displaying 2 SH/gp120
exhibited CD4 but not CXCR4 binding capacity. In addition, PDI
inhibition did not impair gp120 binding to receptors. We
conclude that on average two of the nine disulfides of gp120 are
reduced during interaction with the lymphocyte surface after CXCR4
binding prior to fusion and that cell surface PDI catalyzes this
process. Disulfide bond restructuring within Env may constitute the
molecular basis of the post-receptor binding conformational changes
that induce fusion competence.
Protein-disulfide Isomerase-mediated Reduction of Two
Disulfide Bonds of HIV Envelope Glycoprotein 120 Occurs Post-CXCR4
Binding and Is Required for Fusion*
§,,
CNRS, Faculté de Médecine Nord,
Boulevard Pierre Dramard, Marseille, 13015 France and ¶ Animal
and Microbial Sciences, University of Reading, Reading RG6 6AJ, United
Kingdom
*
This work was supported by a grant from the Agence
Nationale de Recherche sur le SIDA (ANRS) (to E. F.) and a grant from
the Medical Research Council (to I. M. J).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed. Tel./Fax:
33-491-69-88-47; E-mail: fenouillet.e@jean-roche.univ-mrs.fr.
Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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