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Peptide Scanning-assisted Identification of a Monoclonal Antibody-recognized Linear B-cell Epitope
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Published on: March 24, 2017

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

Elton P Hudson1, Mathias Uhlen, Johan Rockberg

  • 1School of Biotechnology, Alba Nova University Center, Royal Institute of Technology, Stockholm, Sweden.

Scientific Reports
|October 11, 2012
PubMed
Summary
This summary is machine-generated.

This study introduces a novel bacterial cell-surface display method for rapid and accurate antibody epitope mapping. The technique efficiently identifies antibody-antigen interactions, crucial for advancing antibody-based diagnostics and therapeutics.

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Area of Science:

  • Biotechnology
  • Immunology
  • Molecular Biology

Background:

  • Antibody-based diagnostics and therapeutics are rapidly advancing.
  • Accurate and rapid determination of antibody-antigen interactions is essential.
  • Current methods for epitope mapping can be time-consuming and lack multiplexing capabilities.

Purpose of the Study:

  • To develop and validate a novel method for multiplex antibody epitope determination.
  • To assess the method's ability to identify linear and structural epitopes.
  • To demonstrate the utility of the method in characterizing antibody cross-reactivity.

Main Methods:

  • Construction and characterization of a large-scale bacterial cell-surface display protein-fragment library (10^7 clones) against 60 clinically relevant targets.
  • Massively parallel sequencing for library analysis.
  • Application of the library to simultaneously map epitopes of monoclonal and polyclonal antibodies targeting PSMA, EGFR, and VEGF.

Main Results:

  • Simultaneous determination of antibody epitopes against multiple targets (PSMA, EGFR, VEGF).
  • Identification of off-target binding for one antibody, demonstrating cross-reactivity detection.
  • Successful mapping of structural epitopes, exemplified by the therapeutic antibody Avastin.

Conclusions:

  • The developed bacterial cell-surface display method enables rapid, multiplexed mapping of linear and structural antibody epitopes.
  • The method is suitable for characterizing monoclonal and polyclonal antibodies.
  • Potential applications include serum profiling and other protein-protein interaction studies.