Multiplex epitope mapping using bacterial surface display reveals both linear and conformational epitopes

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Multiplex epitope mapping using bacterial surface display reveals both linear and conformational epitopes

As antibody-based diagnosis and therapy grow at an increased pace, there is a need for methods which rapidly and accurately determine antibody-antigen interactions. Here, we report a method for the multiplex determination of antibody epitopes using bacterial cell-surface display. A protein-fragment library with 10(7) cell clones, covering 60 clinically-relevant protein targets, was created and ...

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Epitope Mapping: B-cell Epitopes

Immunoglobulin molecules are folded in a way that assembles sequences from the variable regions of both the heavy and light chains into a surface feature (comprised of up to six complementarity-determining regions (CDRs)) that is complementary in shape to a surface structure on the antigen. These two surface features, the ‘paratope’ on the antibody and the ‘epitope’ on the antigen, may have a c...

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Cell surface expression of protein has been widely used to display enzymes and antigens. Here we show that Pseudomonas syringae ice nucleation protein with a deletion of internal repeating domain (INC) can be used in Escherichia coli to display peptide in a conformationally active form on the outside of the folded protein by fusing to the C-terminus of INC. Diagnostic potential of this technolo...

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Automated Detection of Conformational Epitopes Using Phage Display Peptide Sequences

BACKGROUND Precise determination of conformational epitopes of neutralizing antibodies represents a key step in the rational design of novel vaccines. A powerful experimental method to gain insights on the physical chemical nature of conformational epitopes is the selection of linear peptides that bind with high affinities to a monoclonal antibody of interest by phage display technology. Howeve...

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ژورنال

عنوان ژورنال: Scientific Reports

سال: 2012

ISSN: 2045-2322

DOI: 10.1038/srep00706