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Immunocomplexed Antigen Capture and Identification by Native Top-Down Mass Spectrometry.

John P McGee1, Rafael D Melani1, Ben Des Soye1

  • 1Departments of Chemistry and Molecular Biosciences and the Proteomics Center of Excellence, Northwestern University, Evanston, Illinois 60208, United States.

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Native mass spectrometry precisely characterizes antibody-antigen complexes, revealing how protein variations affect immune recognition. This method identifies specific antigen proteoforms and their binding sites, advancing allergy research.

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Area of Science:

  • Immunology
  • Analytical Chemistry
  • Biochemistry

Background:

  • Antibody-antigen interactions are crucial for the immune response.
  • Protein antigen variations (isoforms, PTMs) can alter antibody binding sites.
  • Understanding these variations is key to deciphering immune recognition.

Purpose of the Study:

  • To directly link protein antigen recognition to their molecular composition.
  • To characterize antibody-antigen complexes using native tandem mass spectrometry.
  • To investigate the peanut allergen Ara h 2 and its interaction with IgE.

Main Methods:

  • Native tandem mass spectrometry was employed to probe antibody-antigen complexes.
  • Immunocomplexes were isolated in the gas phase and activated.
  • Bound antigens were ejected, identified, and characterized as proteoforms.

Main Results:

  • Demonstrated antigen-induced dimerization of IgE antibodies.
  • Successfully isolated and fragmented ejected antigens to determine their chemical composition.
  • Identified specific proteoforms of the peanut allergen Ara h 2 bound by IgE.

Conclusions:

  • Native top-down mass spectrometry is a powerful platform for characterizing immunocomplexes.
  • This technique enables precise structure-function relationship determination.
  • Facilitates discovery of antigen proteoforms and their binding sites, crucial for allergy research.