Previous Article | Next Article ![]()
Journal of Virology, May 2001, p. 4528-4539, Vol. 75, No. 10
Department of Molecular Biology, The Scripps
Research Institute, La Jolla, California 92037
Received 16 November 2000/Accepted 13 February 2001
To address the role of CXCR4 in the cell-surface attachment of the
feline immunodeficency virus (FIV), a soluble fusion protein, gp95-Fc,
consisting of the surface glycoprotein (SU, gp95) of either
a primary (PPR) or cell line-adapted (34TF10) FIV strain was fused in
frame with the Fc domain of human immunoglobulin G1. The recombinant
SU-immunoadhesins were used as probes to investigate the cellular
binding of FIV SU. In agreement with the host cell range properties of
both viruses, binding of 34TF10 gp95-Fc was observed for all cell lines
tested, whereas PPR gp95-Fc bound only to primary feline T cells.
34TF10 gp95-Fc also bound to Jurkat and HeLa cells, consistent with the
ability of FIV to use human CXCR4 as a fusion receptor. As expected,
34TF10 gp95-Fc binding to Jurkat cells was blocked by addition of
stromal cell-derived factor 1
0022-538X/01/$04.00+0 DOI: 10.1128/JVI.75.10.4528-4539.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.
Binding of Recombinant Feline Immunodeficiency Virus Surface
Glycoprotein to Feline Cells: Role of CXCR4, Cell-Surface Heparans,
and an Unidentified Non-CXCR4 Receptor
(SDF-1
), as was binding to the 3201 feline lymphoma cell line. However, SDF-1
, RANTES, macrophage
inflammatory protein 1
, and heparin all failed to inhibit the
binding of either gp95-Fc to primary T cells, suggesting that a
non-CXCR4 receptor is involved in the binding of FIV SU. In this
regard, an unidentified 40-kDa protein species from the surface of
primary T cells but not Jurkat and 3201 cells specifically
coprecipitated with both gp95-Fc. Yet another type of binding of 34TF10
gp95-Fc to adherent kidney cells was noted. SDF-1
failed to block
the binding of 34TF10 gp95-Fc to either HeLa, Crandel feline leukemia,
or G355-5 cells. However, binding was severely impaired in the presence
of soluble heparin, as well as after enzymatic removal of surface
heparans or on cells deficient in heparan expression. These overall
findings suggest that in addition to CXCR4, a non-CXCR4 receptor and
cell-surface heparans also play an important role in FIV gp95 cell
surface interactions on specific target cells.
*
Corresponding author. Mailing address: The Scripps
Research Institute, Department of Molecular Biology MB-14, 10550 N. Torrey Pines Rd., La Jolla, CA 92037. Phone: (858) 784-9707. Fax: (858) 784-2750. E-mail: aymeric{at}scripps.edu.
This article has been cited by other articles:
| J. Bacteriol. | Mol. Cell. Biol. | Microbiol. Mol. Biol. Rev. |
|---|
| Clin. Vaccine Immunol. | ALL ASM JOURNALS |
|---|