Document 0185
 DOCN  M95A0185
 TI    alpha 1-Acid glycoprotein binds human immunodeficiency virus type 1
       (HIV-1) envelope glycoprotein via N-linked glycans.
 DT    9510
 AU    Rabehi L; Ferriere F; Saffar L; Gattegno L; Laboratoire de Biologie
       Cellulaire, Faculte de Medecine; Paris-Nord, Bobigny, France.
 SO    Glycoconj J. 1995 Feb;12(1):7-16. Unique Identifier : AIDSLINE
       MED/95315749
 AB    In the present study, we demonstrate a specific low-affinity interaction
       between recombinant precursor gp160 (rgp160) or surface unit gp120
       (rgp120) of human immunodeficiency virus type 1 (HIV-1) and alpha 1-acid
       glycoprotein (AGP), a human glycoprotein displaying complex type
       N-glycans. Binding of rgp160/rgp120 to agarose-coupled AGP was
       dose-dependent, saturable, calcium-, pH- and temperature-dependent.
       Binding was inhibited by soluble AGP, asialo-AGP, fetuin,
       beta-D-GlcNAc47-BSA, alpha-D-Man20-BSA, mannan, complex-type
       asialo-agalacto-tetraanternary precursor oligosaccharide from human AGP
       and oligomannose 9 from porcine thyroglobulin; fully deglycosylated AGP
       was not inhibitory. The three AGP glycoforms separated on immobilized
       ConA bound rgp160 to the same extent as did unfractionated AGP. These
       findings extend our previous results on the carbohydrate-binding
       properties of HIV-1 envelope (Env) glycoprotein in that they demonstrate
       the involvement of AGP glycan moieties in the binding to rgp160/rgp120.
       Preincubation of rgp160 with AGP or mannan significantly reduced its
       binding to monocyte-derived macrophages (MDM), suggesting that AGP may
       play a role in preventing binding of soluble or virus-bound Env
       glycoprotein to CD4+ monocytic cells.
 DE    Binding, Competitive  Carbohydrate Sequence
       Carbohydrates/CHEMISTRY/METABOLISM  Comparative Study  CD4-Positive
       T-Lymphocytes/METABOLISM/VIROLOGY  Human  HIV Envelope Protein
       gp120/DRUG EFFECTS/GENETICS/*METABOLISM  HIV-1/*CHEMISTRY  Molecular
       Sequence Data  Orosomucoid/CHEMISTRY/*METABOLISM/PHARMACOLOGY
       Recombinant Proteins/METABOLISM  Sepharose/CHEMISTRY  Substrate
       Specificity  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).