Epitope identification

Yao, Z.-J., Kao, M. C. C., and Chung, M. C. M. (1995). Epitope identification by polyclonal antibody from phage-displayed random peptide library. J. Protein Chem. 14, 161-166. 

Reuhs, B.L., Stephens, S.B., Geller, D.P., Kim, J.S., Glenn, J., Przytycki, J., Ojanen-Reuhs, T. Epitope identification for a panel of unli-Sinoritizobium meliloti monoclonal antibodies and application to the analysis of K antigens and lipopolysaccharides from bacteroids. Appl Environ Microbiol 65 (1999) 5186-5191. 

DIFFERENTIAL EPITOPE IDENTIFICATION OF ANTIBODIES AGAINST INTRACELLULAR DOMAINS OF ALZHEIMER S AMYLOID PRECURSOR PROTEIN USING HIGH RESOLUTION AFFINITY-MASS SPECTROMETRY... 

Epitope Identification and Immunological Characterisation of a Monoclonal Anti-C-APP... 

Epitope Identification of a Polyclonal Anti-cAPP Antibody (36BO)... 

Differential Epitope Identification of Antibodies Against Intracellnlar Domains of Alzheimer s Amyloid Precursor... 

D Suckau, J Kohl, G Karwath, K Schneider, M Casaretto, D Bitter-Sauermann, M Przybylski. Molecular epitope identification by limited proteolysis of a immobilized antigen-anitbody complex and mass spectrometric peptide mapping. Proc Natl Acad Sci USA 87 9848 9852, 1990. 

Wang, L.F. and Yu, M., 2004. Epitope identification and discovery using phage display libraries applications in vaccine development and diagnostics, Curr. Drug Targets, 5, pp. 1-15. 

To verify the immunogenic potential of the peptides identified via MAPPs, candidate epitopes are routinely screened in a T cell activation assay which involves human blood-derived APCs and autologous T cells from the same blood donor. In comparison to in silico tools described above, MAPPs has several advantages in T cell epitope identification (i) it narrows down the number of potentially relevant epitopes, as predictable by in silico tools, to a few immunodominant epitopes so that the potency of the drug can be retained more easily (ii) it takes into account post-translational modifications of biologies that may change the pattern of relevant epitopes and (iii) it can be done with fully formulated biologies—a feature not covered by any of the other approaches described above. 

There are two general methods for identifying antibody epitopes (1) evaluate peptides whose composition is based on the sequence of the native protein, or (2) evaluate peptides that are selected from a random combinatorial peptide library. The former is only effective if the epitope is composed of a linear sequence of amino acids in the native protein sequence. If it is, then analysis of overlapping peptides from the native protein is a simple method for identifying antibody epitopes. Each peptide is tested for immunoreactivity to the antibody. Those peptides that are immunoreactive contain the epitope. The other method of epitope identihcation, selection from a random combinatorial library, will identify peptides that represent both linear and conformationally dependent epitopes. The drawback of this method is that biopanning from a random combinatorial peptide library is more time consuming. Phage-displayed peptide libraries have previously been used for epitope identification in this context. ... 

Suckau, D., Kohl, J., Karwath, G., et al. (1990) Molecular Epitope Identification by Limited Proteolysis of an Immobilized Antigen-Antibody Complex and Mass Spectrometric Peptide Mapping. Proceedings of the National Academy of Sciences of the United States of America, 87 (24), 9848-9852. 

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