       Document 0074
 DOCN  M9640074
 TI    An antibody that binds domain 1 of CD4 inhibits replication of HIV-1,
       but not HTLV-I, in a CD4-positive/p56lck-negative HTLV-I-transformed
       cell line.
 DT    9604
 AU    Lemasson I; Briant L; Hague B; Coudronniere N; Heron L; David C;
       Rebouissou C; Kindt T; Devaux C; Laboratory of Immunology for Retroviral
       Infections, INSERM U249,; Institute of Biology, Montpellier, France.
 SO    J Immunol. 1996 Jan 15;156(2):859-65. Unique Identifier : AIDSLINE
       MED/96133018
 AB    mAbs that bind to the Ig CDR3-like region in D1 domain of the CD4
       molecule can inhibit the HIV-1 life cycle in CD4-positive T cells and
       lymphoblastoid cell lines at the stage of transcription. This antiviral
       effect requires the integrity of the cytoplasmic tail of CD4, which acts
       as a signal transduction region through its association with protein
       tyrosine kinases such as p56Ick. Here we investigated the role of p56Ick
       in the cascade of molecular events that control HIV-1 transcription in
       cells treated with anti-CD4 mAb directed against the Ig CDR3-like
       region. The Ig CDR3-like region-specific mAb, 13B8-2, blocked HIV-1
       production in CD4-positive/p56Ick-negative HTLV-I-producing MT2 cells
       superinfected by HIV-1Lai, but had no effect on HTLV-I production,
       although it did inhibit Tax-induced NF-kappa B translocation. These
       results raise the possibility that an as yet unidentified tyrosine
       kinase may be capable of associating with CD4 and mediating
       intracellular signaling.
 DE    beta 2-Microglobulin/IMMUNOLOGY  src-Family
       Kinases/ANALYSIS/DEFICIENCY/*PHYSIOLOGY  Antibodies,
       Monoclonal/IMMUNOLOGY/*PHARMACOLOGY  Antigens,
       CD4/BIOSYNTHESIS/CHEMISTRY/*IMMUNOLOGY  Antiviral Agents/*PHARMACOLOGY
       Base Sequence  Cell Line, Transformed  Comparative Study
       Epitopes/CHEMISTRY/IMMUNOLOGY  Gene Products, tax/METABOLISM  Human
       HIV-1/DRUG EFFECTS/*IMMUNOLOGY/PHYSIOLOGY  HTLV-I/*PHYSIOLOGY  Molecular
       Sequence Data  NF-kappa B/METABOLISM  Polymerase Chain Reaction  Protein
       Structure, Tertiary  Protein-Tyrosine Kinase/*PHYSIOLOGY  Recombinant
       Fusion Proteins/METABOLISM  *Signal Transduction  Support, Non-U.S.
       Gov't  Virus Replication/*DRUG EFFECTS  JOURNAL ARTICLE

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

