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M9480082.TXT
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1994-08-09
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Document 0082
DOCN M9480082
TI Characteristics of HIV-1 gp120 glycoprotein binding to glycolipids.
DT 9410
AU McAlarney T; Apostolski S; Lederman S; Latov N; Department of Neurology,
College of Physicians and Surgeons,; Columbia University, New York, NY
10032.
SO J Neurosci Res. 1994 Mar 1;37(4):453-60. Unique Identifier : AIDSLINE
MED/94293356
AB We examined the binding of the gp120 envelope glycoprotein (gp120) of
the human immunodeficiency virus (HIV-1) to sulfatide (GalS),
galactocerebroside (GalC), and GM1-ganglioside (GM1). The gp120
glycoprotein bound to GalS but not to GalC or GM1 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 chromatography (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.
DE Cell Line Cell Membrane/METABOLISM Comparative Study Enzyme-Linked
Immunosorbent Assay G(M1) Ganglioside/METABOLISM
Galactosylceramides/METABOLISM Glycolipids/*METABOLISM Human HIV
Envelope Protein gp120/*METABOLISM HIV-1/*METABOLISM Immunoblotting
Lymphocytes/METABOLISM Protein Binding Receptors, Virus/*METABOLISM
Recombinant Proteins/METABOLISM Sulfatides/METABOLISM Support,
Non-U.S. Gov't JOURNAL ARTICLE
SOURCE: National Library of Medicine. NOTICE: This material may be
protected by Copyright Law (Title 17, U.S.Code).