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1996-02-26
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Document 0523
DOCN M9620523
TI Mapping the Ig superantigen-binding site of HIV-1 gp120.
DT 9602
AU Goodglick L; Zevit N; Neshat MS; Braun J; Department of Pathology and
Laboratory Medicine, Jonsson; Comprehensive Cancer Center, UCLA School
of Medicine 90095, USA.
SO J Immunol. 1995 Dec 1;155(11):5151-9. Unique Identifier : AIDSLINE
MED/96072787
AB The envelope glycoprotein, gp120, of HIV-1 has recently been identified
as a member of the new family of Ig superantigens (Ig-SAg). This
classification is based on the selective binding of gp120 to an
unusually high proportion of endogenous, nonimmune Ig, and the selective
activation of nonimmune B cells by gp120 in vitro. Many, if not all of
the nonimmune Ig that bind to gp120 are members of the VH3 Ig gene
family. The aim of this study was to determine the epitope on gp120 that
was responsible for its Ig-SAg binding activity. To do this, we utilized
a panel of 30 peptides derived from gp160 in a competition-binding
assay. For five Igs that were tested, as well as for polyclonal serum
IgM, two overlapping peptides (each 20 amino acids in length) were
identified that were potent inhibitors of gp120 binding. Similarly, the
10 amino acid overlap region of these two peptides had inhibitory
activity. Thus, this decamer sequence represented the optimal Ig-SAg
epitope or mimotope. The amino acid residue at position 1 of the
decamer, and to a lesser extent at position 10, was critical for peptide
binding. In addition to this decamer peptide, other peptides that shared
modest sequence homology were also selectively inhibitory for specific
Ig samples. These findings provide the first definition of an Ig-SAg
ligand at the peptide level and will facilitate further structural and
biologic characterization of this new class of pathogenic Ags.
DE Amino Acid Sequence Antibodies, Monoclonal/IMMUNOLOGY *Epitope Mapping
Human HIV Envelope Protein gp120/*METABOLISM HIV-1/*IMMUNOLOGY
IgM/IMMUNOLOGY/METABOLISM Molecular Sequence Data Peptides/IMMUNOLOGY
Superantigens/*METABOLISM Support, Non-U.S. Gov't Support, U.S. Gov't,
P.H.S. JOURNAL ARTICLE
SOURCE: National Library of Medicine. NOTICE: This material may be
protected by Copyright Law (Title 17, U.S.Code).