Document 0132
 DOCN  M9460132
 TI    Effect of sialic acid removal on the antibody response to the third
       variable domain of human immunodeficiency virus type-1 envelope
       glycoprotein.
 DT    9404
 AU    Benjouad A; Mabrouk K; Gluckman JC; Fenouillet E; Laboratoire de
       Biologie et Genetique des Pathologies; Immunitaires, CNRS URA, Faculte
       de Medecine; Pitie-Salpetriere, Paris, France.
 SO    FEBS Lett. 1994 Mar 21;341(2-3):244-50. Unique Identifier : AIDSLINE
       MED/94185803
 AB    The gp160 envelope glycoprotein of human immunodeficiency virus type-1
       (HIV-1) is an essential component of current vaccine trials. The glycans
       of gp160, part of which are highly sialylated, have been shown to
       influence gp160 immunogenicity. Here, using a panel of synthetic V3
       peptides, we characterized the anti-V3 antibodies generated in rabbits
       immunized by desialylated recombinant gp160LAI. Amino acid residues
       flanking the GPGR tip of V3 were necessary for the recognition by
       anti-V3 antibodies raised against either the native or desialylated
       gp160. Both types of antibodies reacted to V3 peptides of MN and SF2
       strains and with a North American/European V3 consensus peptide, while
       anti-desialylated gp160LAI antibodies reacted in addition to the V3 of
       CDC4, WMJ2 and NY5 strains. Yet, the V3 peptides did not significantly
       differ in their secondary structure, as determined by circular
       dichroism. The titer and avidity for V3MN of anti-desialylated gp160LAI
       antibodies were significantly lower than those of anti-native gp160LAI,
       which likely accounts for the inability of anti-desialylated gp160LAI
       sera to neutralize HIV-1MN-induced syncytia. These results indicate that
       V3 immunogenicity may be influenced by subtle directed changes in the
       gp160 glycosylation pattern.
 DE    Amino Acid Sequence  Animal  Antibodies, Viral/*IMMUNOLOGY  Circular
       Dichroism  Cross Reactions  Gene Products, env/CHEMISTRY/*IMMUNOLOGY
       Giant Cells  HIV Envelope Protein gp120/CHEMISTRY/*IMMUNOLOGY
       HIV-1/*IMMUNOLOGY/METABOLISM  Molecular Sequence Data  Peptide
       Fragments/CHEMISTRY/*IMMUNOLOGY  Peptide Mapping  Peptides/IMMUNOLOGY
       Protein Precursors/CHEMISTRY/*IMMUNOLOGY  Rabbits  Sequence Homology,
       Amino Acid  Sialic Acids/*IMMUNOLOGY  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).