Document 0131
 DOCN  M9650131
 TI    Evidence for distinct contributions of heavy and light chains to
       restriction of antibody recognition of the HIV-1 principal
       neutralization determinant.
 DT    9605
 AU    Watkins BA; Davis AE; Fiorentini S; di Marzo Veronese F; Reitz MS Jr;
       Laboratory of Tumor Cell Biology, National Cancer Institute,; National
       Institutes of Health, Bethesda, MD 20892, USA.
 SO    J Immunol. 1996 Feb 15;156(4):1676-83. Unique Identifier : AIDSLINE
       GENBANK/U33142
 AB    We have used phage Ab display technology to analyze two mAbs to HIV-1
       envelope proteins gp120 and gp41. From the data obtained we are able to
       demonstrate that the recognition of the principal neutralization
       determinant of different strains of HIV-1 by neutralizing mAb M77 is
       restricted by its heavy and light chains in different ways. Native M77
       is able to recognize and neutralize HIV-1 strain IIIB through binding to
       the gp120 V3 loop. M77 is unable to recognize strains of HIV-1 that
       differ on either the left or right side of the V3 loop tip. A
       chain-switched Fab fragment containing the M77 Fd fragment and a
       different light chain was able to recognize HIV-1 strains that differ
       from IIIB on the left side but not the right side of the V3 loop tip.
 DE    Amino Acid Sequence  Animal  Antibodies, Monoclonal  *Antibody
       Specificity  Base Sequence  Cloning, Molecular  Comparative Study
       *Genes, Immunoglobulin  HIV Antibodies/*CHEMISTRY  Immunoglobulins,
       Fab/CHEMISTRY  Immunoglobulins, Heavy-Chain/*CHEMISTRY  Immunoglobulins,
       Light-Chain/*CHEMISTRY  Mice  Molecular Sequence Data  Neutralization
       Tests  Sequence Alignment  Sequence Homology, Amino Acid  Sequence
       Homology, Nucleic Acid  JOURNAL ARTICLE

       SOURCE: National Library of Medicine.  NOTICE: This material may be
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