Open AccessMonoclonal antibody epitopes of mycobacterial 65‐kD heat‐shock protein defined by epitope scanning
Author(s) -
HAJEER A. H.,
WORTHINGTON J.,
MORGAN K.,
BERNSTEIN R. M.
Publication year - 1992
Publication title -
clinical & experimental immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.329
H-Index - 135
eISSN - 1365-2249
pISSN - 0009-9104
DOI - 10.1111/j.1365-2249.1992.tb06888.x
Subject(s) - epitope , monoclonal antibody , mycobacterium tuberculosis , epitope mapping , biology , linear epitope , antibody , tuberculosis , virology , immunology , medicine , pathology
SUMMARY The binding sites for MoAbs to the 65‐kD heat‐shock protein (hsp65) of mycobacteria have been investigated by epitope scanning. Five hundred and twenty‐six 8‐mer peptides representing the complete sequence of Mycobacterium tuberculosis hsp65 were synthesised in duplicate using the Epitope Scanning Kit (CRB Ltd.). The epitopes of six MoAbs raised to the hsp65 of M. tuberculosis or M. leprae were investigated. We have identified the epitope of a new MoAb (DC 16); this epitope is continuous, hydrophilic in nature and 11 amino acids long. We have also confirmed the location of the epitopes of three MoAbs (IIH9, ML30 and IIC8). Thus the epitope scanning technique has proved suitable for the detection of continuous epitopes of hsp65.