Journal of Virology, June 1999, p. 5244-5248, Vol. 73, No. 6
0022-538X/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
Laboratoire de Biochimie et Biologie de la
Nutrition,
Received 26 October 1998/Accepted 5 March 1999
Glycosphingolipids from human erythrocytes mediate CD4-dependent
fusion with cells expressing human immunodeficiency virus type 1 (HIV-1) envelope glycoproteins. To identify the glycosphingolipid(s) which participates in the fusion process, we have analyzed the interaction of HIV-1 gp120 (X4 and R5X4 isolates) with reconstituted membrane microdomains of human erythrocyte glycosphingolipids. We
identified globotriaosylceramide (Gb3) and ganglioside GM3 as the main
glycosphingolipids recognized by gp120. In the presence of CD4, Gb3
interacted preferentially with the X4 gp120, whereas GM3 interacted
exclusively with the R5X4 gp120. These data suggest that
glycosphingolipid microdomains are required in CD4-dependent fusion and
that Gb3 and/or GM3 may function as alternative entry cofactors for
selected HIV-1 isolates.
*
Corresponding author. Mailing address: Laboratoire de
Biochimie et Biologie de la Nutrition, ESA-CNRS 6033, Faculté des
Sciences de St Jérôme, 13397 Marseille cedex 20, France.
Phone: 33 491-288-761. Fax: 33 491-288-440. E-mail:
JACQUES.FANTINI{at}LBBN.u-3mrs.fr.
This article has been cited by other articles:
| J. Bacteriol. | Mol. Cell. Biol. | Microbiol. Mol. Biol. Rev. |
|---|
| Clin. Vaccine Immunol. | ALL ASM JOURNALS |
|---|