Chapter 26 : Specificity and Function of T- and B-Cell Recognition in Tuberculosis

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This chapter talks about the progress in the study of immune reactions mainly to antigens of that have been firmly identified and the largely characterized protein structure. An important breakthrough in the characterization of antigens was achieved initially by the production of monoclonal antibodies to mycobacterial antigens and particularly by the development of recombinant DNA systems for efficient expression of mycobacterial genes in . Heat shock proteins (hsp) have highly conserved amino acid sequences. Their functions as molecular chaperones in the assembly and disassembly of proteins into oligomers during transport through the cell or as proteases that degrade misfolded or foreign proteins are vital for each cell. The significance of lipoproteins for the immune response to mycobacteria has been in focus in view of reports that acylation of proteins enhances their ability to induce delayed-type hypersensitivity (DTH) and that synthetic lipopeptides have the ability to prime cytotoxic T cells. Proteins secreted from viable bacteria could be available for immune recognition at an early stage of infection and may therefore play a special role in protective immune mechanisms. Antibody levels following immunization with soluble extracts of tubercle bacilli in adjuvant demonstrated the codominant control by the IA locus of the response to individual epitopes. Analysis of the specificity of T-cell responses to the mycobacterial 65-kDa heat shock protein has so far attracted more attention in relation to its potential role in autoimmunity than in respect to tuberculosis.

Citation: Ivanyi J, Thole J. 1994. Specificity and Function of T- and B-Cell Recognition in Tuberculosis, p 437-458. In Bloom B (ed), Tuberculosis. ASM Press, Washington, DC. doi: 10.1128/9781555818357.ch26
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