Abstract
The fine characterization of protective B cell epitopes plays a pivotal role in the development of novel vaccines. The development of epitope-based vaccines, in fact, cannot be possible without a clear definition of the antigenic regions involved in the binding between the protective antibody (Ab) and its molecular target. To achieve this result, different epitope-mapping approaches have been widely described (Clementi et al. Drug Discov Today 18(9–10):464–471, 2013). Nowadays, the best way to characterize an Ab bound region is still the resolution of Ab–antigen (Ag) co-crystal structure. Unfortunately, the crystallization approaches are not always feasible. However, different experimental strategies aimed to predict Ab–Ag interaction and followed by in silico analysis of the results may be good surrogate approaches to achieve this result. Here, we review few experimental techniques followed by the use of “basic” informatics tools for the analysis of the results.
Nicola Clementi and Nicasio Mancini contributed equally to the chapter.
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References
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Clementi, N., Mancini, N., Criscuolo, E., Cappelletti, F., Clementi, M., Burioni, R. (2014). Epitope Mapping by Epitope Excision, Hydrogen/Deuterium Exchange, and Peptide-Panning Techniques Combined with In Silico Analysis. In: Ossipow, V., Fischer, N. (eds) Monoclonal Antibodies. Methods in Molecular Biology, vol 1131. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-62703-992-5_26
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DOI: https://doi.org/10.1007/978-1-62703-992-5_26
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