       Document 0537
 DOCN  M9630537
 TI    Human immunodeficiency virus type 1 infection of SK-N-MC cells: domains
       of gp120 involved in entry into a CD4-negative, galactosyl ceramide/3'
       sulfo-galactosyl ceramide-positive cell line.
 DT    9603
 AU    Harouse JM; Collman RG; Gonzalez-Scarano F; Department of Neurology,
       School of Medicine University of; Pennsylvania, Philadelphia 19104-6146,
       USA.
 SO    J Virol. 1995 Dec;69(12):7383-90. Unique Identifier : AIDSLINE
       MED/96078979
 AB    The primary receptor for human immunodeficiency virus (HIV) is the CD4
       molecule; however, in vitro evidence suggests that a neutral glycolipid,
       galactosyl ceramide (GalCer) or a derivative molecule, 3'
       sulfogalactosyl ceramide (GalS), may serve as an alternative receptor
       for HIV type 1 (HIV-1) in cells of neural and colonic origin.
       Biochemical studies have demonstrated that recombinant gp120 envelope
       protein binds to GalCer/GalS in both solid-phase enzyme-linked
       immunosorbent assay and high-performance thin-layer chromatography
       overlays. We have used the SK-N-MC cell line, a CD4-negative,
       GalCer/GalS-positive cell line previously characterized as susceptible
       to HIV-1 infection, to identify virus isolates with either a positive
       infection phenotype, HIVHxB2, or a negative infection phenotype,
       HIV-1(89.6). Using a solid-phase virus binding assay, we determined the
       level of restriction in HIV-1(89.6) infection to be at the level of
       virus-glycolipid binding. Furthermore, using HIV-1HxB2-HIV-1(89.6)
       chimeras, we have identified a 193-amino-acid fragment from the envelope
       region of HIV-1HxB2 containing the V3, V4, and V5 regions which confers
       a positive infection phenotype on the HIV-1(89.6) background.
       Recombinant viruses which separate this 193-amino-acid fragment into two
       distinct chimeras are each able to confer a positive infection phenotype
       on the background of HIV89.6, suggesting that a stable
       GalCer/GalS-envelope interaction is dependent on the conformation of the
       envelope protein in the context of the viral membrane. Alternatively,
       the GalCer/GalS-gp120 bond may involve multiple sites on the oligomeric
       envelope protein.
 DE    Antigens, CD/*GENETICS/PHYSIOLOGY  Antigens, CD4/*GENETICS/PHYSIOLOGY
       Base Sequence  Binding Sites  Cell Line  Chromatography, High Pressure
       Liquid  Comparative Study  DNA Primers  DNA, Viral/ANALYSIS/ISOLATION &
       PURIF  Enzyme-Linked Immunosorbent Assay
       Galactosylceramides/ANALYSIS/*PHYSIOLOGY  Hela Cells  Human  HIV
       Envelope Protein gp120/*METABOLISM  HIV-1/GENETICS/*PHYSIOLOGY  Kinetics
       Molecular Sequence Data  Neuroblastoma  Phenotype  Polymerase Chain
       Reaction  Receptors, Virus/ANALYSIS/*PHYSIOLOGY  Species Specificity
       Support, U.S. Gov't, P.H.S.  Tumor Cells, Cultured  JOURNAL ARTICLE

       SOURCE: National Library of Medicine.  NOTICE: This material may be
       protected by Copyright Law (Title 17, U.S.Code).

