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Epitope mapping of rat neutralizing monoclonal antibody against human immunodeficiency virus type-1 by a phage peptide library: comparison with ELISA using synthetic peptides.
Ichiyama K; Ishikawa D; Tanaka Y; Kashiwa T; Koyanagi Y; Handa S;
September 30, 1999
Viral Immunol. 1999;12(1):57-66. Unique Identifier : AIDSLINE

We generated a rat monoclonal antibody (mAb W#10) with the ability to neutralize human immunodeficiency virus type 1IIIB (HIV-1IIIB) infection. The epitope recognized by mAb W#10 was defined as R-I-Q-R-G-P-G by enzyme-linked immunosorbent assay (ELISA) with the use of synthetic peptides. The filamentous phage clones displaying random 15-amino-acid peptides on the amino terminus of the pIII coat protein reacting with mAb W#10 were identified with affinity and immunological selection procedures. Thirteen out of 16 selected phage clones contained the G-X-G-R-X-F sequence in the coat protein region representing significant homology to a part of conserved G-P-G-R-A-F sequence in the V3 loop of various HIV-1 strains. In addition, the phage clones included the G-X-G sequence in the sequence detected by synthetic peptides as the recognition site. The selected phage clones were stained by mAb W#10 specifically and were able to compete with mAb binding to cells expressing viral antigens.

JOURNAL ARTICLE Amino Acid Sequence Animal Antibodies, Monoclonal/*CHEMISTRY Binding Sites, Antibody Cells, Cultured Coliphages/GENETICS/IMMUNOLOGY Comparative Study Enzyme-Linked Immunosorbent Assay/METHODS Epitope Mapping/*METHODS Human HIV-1/*IMMUNOLOGY Kidney Molecular Sequence Data Neutralization Tests *Peptide Library Peptide Mapping Peptides/ANALYSIS/*CHEMICAL SYNTHESIS/*IMMUNOLOGY Rats Support, Non-U.S. Gov't