Insights into the IgG heavy chain engineering patent landscape as applied to IgG4 antibody development

MAbs. 2019 Nov-Dec;11(8):1341-1350. doi: 10.1080/19420862.2019.1664365. Epub 2019 Sep 26.

Abstract

Despite being the least abundant immunoglobulin G in human plasma, IgG4 are used therapeutically when weak effector functions are needed. The increase in engineered IgG4-based antibodies on the market led us to study the patent landscape of IgG4 Fc engineering, i.e., patents claiming modifications in the heavy chain. Thirty-seven relevant patent families were identified, comprising hundreds of IgG4 Fc variants focusing on removal of residual effector functions (since IgG4s bind to FcγRI and weakly to other FcγRs), half-life enhancement and IgG4 stability. Given the number of expired or soon to expire major patents in those 3 areas, companies developing blocking antibodies now have, or will in the near future, access to free tools to design silenced, half-life extended and stable IgG4 antibodies.

Keywords: Fc; IgG4; engineering; patents.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Humans
  • Immunoglobulin Fc Fragments / chemistry
  • Immunoglobulin Fc Fragments / genetics
  • Immunoglobulin G / chemistry
  • Immunoglobulin G / genetics*
  • Immunoglobulin Heavy Chains / chemistry
  • Immunoglobulin Heavy Chains / genetics*
  • Patents as Topic
  • Protein Engineering*

Substances

  • Immunoglobulin Fc Fragments
  • Immunoglobulin G
  • Immunoglobulin Heavy Chains

Grants and funding

This work was supported by the Investissments d’avenir [LabEx MAbImprove ANR_10_53_01].