Mapping of the T and B cell epitopes of the Mycobacterium bovis protein, MPB70

Summary A clone coding for the entire gene for the Mycobacterium bovis protein antigen MPB70 was used to produce a series of overlapping subclones by making a series of deletions from the 3′ end of the gene. The subclones expressed incomplete MPB70 proteins as fusions with glutathione‐S‐transferase....

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Bibliographic Details
Published in:Immunology and cell biology 2017-12, Vol.68 (6), p.359-365
Main Authors: Billman‐Jacobe, H., Radford, A. J., Rothel, J. S., Wood, P. R.
Format: Article
Language:English
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Summary:Summary A clone coding for the entire gene for the Mycobacterium bovis protein antigen MPB70 was used to produce a series of overlapping subclones by making a series of deletions from the 3′ end of the gene. The subclones expressed incomplete MPB70 proteins as fusions with glutathione‐S‐transferase. The insert DNA was sequenced to determine the extent of the deletion and the proteins expressed by the clones were examined for the presence of T cell and B cell epitopes. T cell epitopes were mapped by measuring the ability of recombinant antigens to stimulate gamma interferon (γ‐IFN) production in a whole blood culture system. γ‐IFN production was measured using a sandwich enzyme immunoasssay specific for bovine γ‐IFN. B cell epitopes were mapped with a series of anti‐MPB70 monoclonal antibodies using an indirect enzyme immunoassay.
ISSN:0818-9641
1440-1711
DOI:10.1038/icb.1990.49