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

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