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1996-02-27
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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).