Glycoform-resolved FcɣRIIIa affinity chromatography-mass spectrometry

MAbs. 2019 Oct;11(7):1191-1196. doi: 10.1080/19420862.2019.1636602. Epub 2019 Aug 2.

Abstract

Determination of the impact of individual antibody glycoforms on FcɣRIIIa affinity, and consequently antibody-dependent cell-mediated cytotoxicity (ADCC) previously required high purity glycoengineering. We hyphenated FcɣRIIIa affinity chromatography to mass spectrometry, which allowed direct affinity comparison of glycoforms of intact monoclonal antibodies. The approach enabled reproduction and refinement of known glycosylation effects, and insights on afucosylation pairing as well as on low-abundant, unstudied glycoforms. Our method greatly improves the understanding of individual glycoform structure-function relationships. Thus, it is highly relevant for assessing Fc-glycosylation critical quality attributes related to ADCC.

Keywords: FT-ICR-MS; FcɣRIIIa affinity chromatography; IgG Fc glycosylation; Monoclonal antibody (mAb); immunoglobulin glycans; mass spectrometry; structure-function relationships.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Antibodies, Monoclonal / chemistry
  • Antibodies, Monoclonal / metabolism*
  • Antibody Affinity
  • Antibody-Dependent Cell Cytotoxicity
  • Chromatography, Affinity
  • Glycosylation
  • Humans
  • Immunoglobulin Fc Fragments / chemistry
  • Immunoglobulin Fc Fragments / metabolism*
  • Immunoglobulin G / chemistry
  • Immunoglobulin G / metabolism*
  • Mass Spectrometry
  • Polysaccharides / chemistry
  • Receptors, IgG / metabolism*
  • Structure-Activity Relationship

Substances

  • Antibodies, Monoclonal
  • FCGR3A protein, human
  • Immunoglobulin Fc Fragments
  • Immunoglobulin G
  • Polysaccharides
  • Receptors, IgG

Grants and funding

This work was supported by the Horizon 2020 [765502]; Nederlandse Organisatie voor Wetenschappelijk Onderzoek [731.017.202]; Roche Diagnostics; Nederlandse Organisatie voor Wetenschappelijk Onderzoek (NL) [722.016.008].