Epitopes adjacent proteins

In order to model the effect of formalin fixation and antigen retrieval on antibody immunoreactivity, we used a peptide epitope array (Fig. 16.5). The peptide epitopes are derived from the exact sequences in the native proteins. In this experiment, the initial findings are similar to those shown in Figure 16.1, but they are then extended by allowing for the role of adjacent proteins. 

Figure 7.2 Schematic showing the relationship of the native antigen to the peptide mimic. The native antigen (a protein) is shown as a winding, twisted line, so as to represent a hypothetical three-dimensional structure. The peptide represents the antibody-binding epitope (shown in dotted lines) of the native antigen. The epitope can represent a linear sequence of the native protein. Alternatively, the epitope can be formed by amino acids that are not immediately adjacent to each other in the primary sequence but brought together by the three-dimensional folding of the protein. Adapted with permission from Sompuram et al.6...

Figure 2. Chondroitin sulfate chains covalently attach to a core protein via a carbohydrate linkage region. The native chondroitin sulfate epitopes for various anti-chondroitin sulfate monoclonal antibodies have been mapped to different regions of the chondroitin sulfate chains of embryonic chick aggrecan. The native 3B3 epitope [12, 48] appears at the non-reducing terminus. Interior domains contain epitopes for antibodies 4D3I6C3/CS-56 [62]. Epitopes for antibodies 4C3j7D4 are located adjacent to the linkage region [25, 62]. Figure modified from [62].

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