B-epitopes

Figure 3 Design of a diepitope liposomal construct. Small unilamellar liposomes (PC/PG/Chol 55/25/50 molar ratio diameter 100nm) containing 10mol% of bromo-acetyl l,2-dipalmitoyl-sn-glycero-3-phosphoethanolamine and 10mol% of the thiol-reactive lipopeptide adjuvant anchor Pam3CysAlaGly-Mal were reacted, at 25°C successively at pH 6.5, with the T-helper epitope QYI, derivatized with a C-linker at its N-terminus, followed at pH 9.0 by the B-epitope TPE derivatized with a CG linker at its N-terminus. Abbreviations PC, phosphatidylcholine PE, phosphatidylethanolamine SUV, small unilamellar vesicles. Source From Refs. 11, 20, 21.

Reynolds, S.R., Dahl, C.E. and Harn, D.A. (1 994)T and B epitope determination and analysis of multiple antigenic peptides for the Schistosoma mansoni experimental vaccine triose-phosphate isomerase. The Journal of Immunology 1 52, 1 93-200. 

Gargiulo, V., Garozzo, D., Lanzetta, R., Molinaro, A., Sturiale, L., Castro, C.D., Parrilli, M. Rhizobium rubi A gram-negative phytopathogenic bacterium expressing the Lewis B epitope on the outer core of its lipoohgosaccharide fraction. ChemBioChem 9 (2008) 1830-1835. 

Burritt JB, Quinn MT, Jutila MA, Bond CW, Jesaitis AJ, Topological mapping of neutrophil cytochrome b epitopes with phage-display libraries, J. Biol. Chem., 270(28) 16974-16980, 1995. 

F. Belot, C. Guerreiro, F. Baleux, and L. A. Mulard, Synthesis of two linear PADRE conjugates bearing a deca- or pentadecasaccharide B epitope as potential synthetic vaccines against Shigella flexneri serotype 2a infection, Eur. J. Chem., 11 (2005) 1625-1635. 

Fig. 10. Tlie O-chain of H. pylori strain P466 carrying a type-2 Le (A), or a type-2 sialyl Ixi" (B) epitope at the nonreducing tenninus of a Le" O-chain.

Vaccines need to be designed to take account of variations in human genome in regard to HLA, and also variations in our own proteins to avoid autoimmune disease. The theory of attack is to make vaccines that contain B-epitopes (bone immune system) that generate antibodies, T-epitopes (thymus immune system) that will stimulate antibody and T-cell response respectively, plus some other stimulants of immune response (e.g., molecular adjuvant ). Briefly and crudely, the antibodies deal with the molecules, and the T response with whole cells. 

A or O person receives a transfusion of type B blood, antibodies against the B epitope will bind to the introduced red cells and trigger their destruction. To prevent such harmful reactions, blood-group typing and appropriate matching of blood donors and recipients are required in all transfusions (Table 5-2). ... 

The sensitivity to trypsin of the epitopes from the entire cyt protein as well as those at the NH2- and COOH-termini was measured in thylakoids and ISO membranes relative to that of proteins known to be located on the lumen side of the membrane. Cyt /, as well as the OEC 16 and 33 kDa proteins (not shown), were found to be more resistant in thylakoids to trypsin than the cyt b epitopes (Fig. 3), whereas the trypsin-resistant epitopes in ISO membranes were those to the NH2- and COOH-termini (not shown). Thus, epitopes from the NH2- and COOH-termini show an accessibility to trypsin that is inversely related to that of cyt / and the OEC proteins, implying that the cyt b termini are both exposed to the stroma, as in the model of Fig. 1. 

Rudolf MP, Vogel M, Kricek F, Ruf C, Zurcher AW, Reushcel R, Auer M, Miescher S, Stadler B. Epitope-specific antibody response to IgE by mimotope immunization. J Immunol 1998 160 3315-3321. 

Figure 2. A comparison of the relative efficiencies of different T-cell epitopes to provide help in the induction of antibody responses and the relative stabilities of branched and linear immunogens to proteolysis. The left hand panel shows the abilities of two immunogens constructed with the same B cell epitope but with different helper T cell qpitopes. T1 or T2, to elicit antibody. The right hand panel demonstrates that an immunogen c< npased of the T2 and B epitopes in a branched configuration is more resistant to proteolysis following exposure to serum than the same epitopes when assembled as a tandem linear arrangement.

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