Document 0046
 DOCN  M9470046
 TI    Jacalin, a lectin with anti-HIV-1 properties, and HIV-1 gp120 envelope
       protein interact with distinct regions of the CD4 molecule.
 DT    9409
 AU    Corbeau P; Haran M; Binz H; Devaux C; CRBM-UPR 9008 du CNRS, Institut de
       Biologie-Faculte de; Medecine, Montpellier, France.
 SO    Mol Immunol. 1994 Jun;31(8):569-75. Unique Identifier : AIDSLINE
       MED/94254890
 AB    Jacalin is a multimeric plant lectin able to interact with the
       lymphocyte cell-surface molecule CD4, a known receptor for the human
       immunodeficiency virus type 1 (HIV-1). Moreover, jacalin is able to
       block HIV-1 infection of CD4+ lymphoblastoid cells. Here we studied
       whether jacalin prevents HIV-1 gp120-CD4 interactions. We found (i) that
       jacalin did not inhibit HIV-1 Lai-induced syncytium formation that
       requires gp120-CD4 interactions; (ii) that jacalin prevented neither
       rgp120 binding to cell-surface CD4 nor sCD4 binding to viral envelope
       proteins expressed at the surface of HIV-1-infected lymphoblastoid
       cells; (iii) that jacalin did not compete for binding to CD4 with
       anti-CD4 mAb specific for the CDR2- or CDR3-like regions of the D1
       domain of CD4; (iv) that jacalin did not bind a recombinant soluble
       molecule containing the D1/D2 domains of CD4; and, (iv) that jacalin
       binding to CD4 is inhibited by sugars known to interact with the
       lectinic-site of jacalin. These data have implications for the
       understanding of the mechanism by which jacalin blocks HIV-1 infection
       of CD4+ cells.
 DE    Acetylgalactosamine/METABOLISM  Antigens, CD4/CHEMISTRY/*METABOLISM
       Antiviral Agents/*METABOLISM  Binding Sites  Binding, Competitive  Cell
       Line  Cell Line, Transformed  Comparative Study  Human  HIV Envelope
       Protein gp120/*METABOLISM  HIV-1/*DRUG EFFECTS  Lectins/*METABOLISM
       Nitrophenylgalactosides/METABOLISM  Support, Non-U.S. Gov't  JOURNAL
       ARTICLE

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