Eight to eleven amino acid residues are the sizes of predominant peptides found to be associated with MHC class I molecules. Proteasomes have been implicated in antigen processing and generation of such peptides. Adva...
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Eight to eleven amino acid residues are the sizes of predominant peptides found to be associated with MHC class I molecules. Proteasomes have been implicated in antigen processing and generation of such peptides. Advanced methodologies in peptide elution together with sequence determination have led to the characterisation of MHC class I binding motifs. More recently, screening of random peptide phage display libraries and synthetic combinatorial peptide libraries have also been successfully used. This has led to the development and use of predictive algorithms to screen antigens for potential CTL epitopes. Not all predicted epitopes will be generated in vivo and the emerging picture suggests differential presentation of predicted CTL epitopes ranging from cryptic to immunodominant. The scope of this review is to discuss antigen processing by proteasomes, and to put forward a hypothesis that the molecular basis of immunogenicity can be a function of proteasomal processing. This may explain how pathogens and tumours are able to escape immunosurveillance by altering sequences required by proteasomes for epitope generation.
Overlapping heptapeptides derived from the MA16 Eimeria acervulina antigenic sequence (Castle et al., 1991) were synthesised on polypropylene pins ('pepskan' technique, Cambridge Research Biochemicals, UK), Bi...
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Overlapping heptapeptides derived from the MA16 Eimeria acervulina antigenic sequence (Castle et al., 1991) were synthesised on polypropylene pins ('pepskan' technique, Cambridge Research Biochemicals, UK), Binding of antibodies from chickens and rabbits infected and immunised respectively with various species of Eimeria oocysts (E. acervulina, E. tenella, E praecox, E. necatrix and E. maxima), was examined using the coated pins as the solid phase of an enzyme immunoassay (EIA). Antigenicity of the overlapping synthetic heptapeptides was then analysed using a number of algorithms based on the amino acid sequence to predict secondary protein structure, hydrophilicity, acrophilicity and chain flexibility profiles, The antigenicity of this sequence appears to be quite different from that found for the E. tenella GX3264 antigenic sequence (Bhogal et al., 1992) whose profile was similarly examined (Talebi and Mulcahy, 1994) using the same rabbit and chicken anti-Eimeria oocyst sera.
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