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Mapping epitopes of monoclonal antibodies against HIV‐1 integrase with limited proteolysis and matrix‐assisted laser desorption ionization time‐of‐flight mass spectrometry
Author(s) -
Yi Jizu,
Skalka Anna Marie
Publication year - 2000
Publication title -
peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/1097-0282(2000)55:4<308::aid-bip1004>3.0.co;2-2
Subject(s) - chemistry , integrase , mass spectrometry , monoclonal antibody , epitope , matrix assisted laser desorption/ionization , human immunodeficiency virus (hiv) , proteolysis , desorption , chromatography , antibody , biochemistry , virology , organic chemistry , enzyme , immunology , adsorption , biology , gene
Abstract Monoclonal antibodies (mAbs) have been used extensively in the biochemical analysis of proteins. Molecular identification of a specific epitope can enhance our understanding of the relationship between the structure and function of a protein. We recently developed a protein footprint technique for mapping mAb epitopes that employs limited proteolysis followed by peptide analysis with matrix‐assisted laser desorption ionization time‐of‐flight mass spectrometry (MALDI‐TOF MS). Here we describe the rational for the technique and illustrate its use in mapping the epitopes of two mAbs that bind to the C‐terminal domain of human immunodeficiency virus type‐1 integrase. The results provide a plausible explanation for the fact that one mAb inhibits enzyme activity while the second does not. © 2001 John Wiley & Sons, Inc. Biopolymers (Pept Sci) 55: 308–318, 2000