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J. Biol. Chem., Vol. 276, Issue 16, 13433-13441, April 20, 2001
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From the Department of Human Retrovirology, Academic Medical
Center, University of Amsterdam, Meibergdreef 15, 1105 AZ Amsterdam, The Netherlands
The variable V1V2 and V3 regions of the human
immunodeficiency virus type-1 (HIV-1) envelope glycoprotein (gp120) can
influence viral coreceptor usage. To substantiate this we generated
isogenic HIV-1 molecularly cloned viruses that were composed of the
HxB2 envelope backbone containing the V1V2 and V3 regions from viruses isolated from a patient progressing to disease. We show that the V3
amino acid charge per se had little influence on altering
the virus coreceptor phenotype. The V1V2 region and its
N-linked glycosylation degree were shown to confer CXCR4
usage and provide the virus with rapid replication kinetics. Loss of an
N-linked glycosylation site within the V3 region had a
major influence on the virus switching from the R5 to X4 phenotype in a
V3 charge-dependent manner. The loss of this V3
N-linked glycosylation site was also linked with the
broadening of the coreceptor repertoire to incorporate CCR3. By
comparing the amino acid sequences of primary HIV-1 isolates, we
identified a strong association between high V3 charge and the loss of
this V3 N-linked glycosylation site. These results demonstrate that the N-linked glycosylation pattern of the
HIV-1 envelope can strongly influence viral coreceptor utilization and the R5 to X4 switch.
N-Linked Glycosylation of the HIV Type-1 gp120
Envelope Glycoprotein as a Major Determinant of CCR5 and CXCR4
Coreceptor Utilization*
*
This work was supported by Nederlands AIDS Fond Grant 4019, a grant from the Royal Dutch Academy for Arts and Sciences (to W. A. P.), and a grant from the European Union (QLK2-CT-1999-01321 "EuroVac").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.: 31 20 566 4739;
Fax: 31 20 691 6531; E-mail: w.a.paxton@amc.uva.nl.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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