Biosensor Characterization of Structure–Function Relationships in Viral Proteins

Publisher Summary This chapter discusses the biosensor characterization of structure–function relationships in viral proteins. The most widely used biosensor instrument is the BIACORE. The chapter discusses the mapping of viral epitopes. The regions of the viral proteins recognized by the antibody are usually described in terms of amino-acid residues although it is at the level of atomic interactions that the recognition takes place. As antigenic reactivity is usually ascribed to particular residues in a protein—this has led to the classification of epitopes as either continuous or discontinuous—depending on whether the residues involved in the epitopes are contiguous in the polypeptide chain or not. The mapping of epitopes on the surface of viral proteins is commonly done by double-sandwich enzyme-linked immunosorbent assays (ELISA) using all possible pairwise combinations of a panel of monoclonal antibodies (Mabs). Biosensors are useful for selecting diagnostic reagents suitable for viral diagnosis by high throughput immunoassays.

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