Premium
Characteristics of HIV‐1 gp120 glycoprotein binding to glycolipids
Author(s) -
McAlarney T.,
Apostolski S.,
Lederman S.,
Latov N.
Publication year - 1994
Publication title -
journal of neuroscience research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.72
H-Index - 160
eISSN - 1097-4547
pISSN - 0360-4012
DOI - 10.1002/jnr.490370404
Subject(s) - galactocerebroside , glycolipid , nitrocellulose , glycoprotein , immunofluorescence , chemistry , human immunodeficiency virus (hiv) , receptor , antibody , membrane , biochemistry , biology , virology , immunology , myelin , neuroscience , oligodendrocyte , central nervous system
Abstract We examined the binding of the gp120 envelope glycoprotein (gp120) of the human immunodeficiency virus (HIV‐1) to sulfatide (GalS), galactocerebroside (GalC), and GMI‐ganglioside (GMI). The gp120 glycoprotein bound to GalS but not to GalC or GMI by enzyme‐linked immunosorbent assay (ELISA) and by an immunospot assay on nitrocellulose paper. However, it bound to all three glycolipids by an immunospot assay on thin layer chromotography (TLC) plates. In studies to determine whether GalS could be a receptor for gp120 on the surface of cells, gp120 bound to GalS incorporated into the plasma membrane of lymphoid cells as determined by cytofluorometric analysis and immunofluorescence microscopy. These studies indicate that GalS may function as a receptor for gp120 and HIV‐1. © 1994 Wiley‐Liss, Inc.