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The Journal of Immunology, Vol 142, Issue 5 1691-1695, Copyright © 1989 by American Association of Immunologists

ARTICLES

Characterization of an antibody-binding epitope from the 18-kDa protein on Mycobacterium leprae

TM Doherty, RJ Booth, SG Love, JJ Gibson, DR Harding and JD Watson
Department of Immunobiology, School of Medicine, Auckland University, New Zealand.

A murine mAb, designated L5, appears to be specific for an epitope on a protein from Mycobacterium leprae of restricted distribution within the mycobacteria. This protein, of Mr 18,000 (18 kDa) is of interest because monoclonal antibodies raised against it do not appear to cross- react with other mycobacterial pathogens. The L5 antibody-binding epitope has been mapped by two complementary methods; expression of gene fragments and synthesis of short peptides. This L5-binding region of the 18-kDa protein (amino acids 109 to 115) shows some homology to a region of the GroEL heat shock family of proteins. Characterization of this antibody-binding epitope may lead to a reagent of use in early diagnosis of infection.


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M. J. Linke, S. M. Sunkin, R. P. Andrews, J. R. Stringer, and P. D. Walzer
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[Abstract] [Full Text]


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