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Antibody Structure01:10

Antibody Structure

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Overview
Antibodies, also known as immunoglobulins (Ig), are essential players of the adaptive immune system. These antigen-binding proteins are produced by B cells and make up 20 percent of the total blood plasma by weight. In mammals, antibodies fall into five different classes, which each elicits a different biological response upon antigen binding.
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Hybridoma technology is used for the large-scale production of monoclonal antibodies. Monoclonal antibodies bind to only a single antigenic determinant or epitope. Such antibodies are used in research, diagnostics, and disease therapy. The hybridoma technology established in 1975 by Georges Köhler and Cesar Milstein was awarded the Nobel Prize in Medicine in 1984 for revolutionizing research and therapy.
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Antibodies, also known as immunoglobulins, are produced by B cells in response to foreign substances, such as bacteria and viruses. These proteins are critical for recognizing and neutralizing these substances, protecting the body from potential harm.
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Stellabody: A novel hexamer-promoting mutation for improved IgG potency.

Clarissa A Whitehead1,2, Bruce D Wines1,2, Anna M Davies3

  • 1Immune Therapies Group, Burnet Institute, Melbourne, Victoria, Australia.

Immunological Reviews
|October 4, 2024
PubMed
Summary

New antibody engineering strategies enhance IgG hexamerisation for more potent immunotherapeutics. Stellabody technology, by modifying the H429 residue, enables on-target or pH-sensitive hexamerisation for improved therapeutic effects.

Keywords:
Fc mutationFc receptorsIgGStellabodycomplementhexamerisationmonoclonal antibodies

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Area of Science:

  • Immunology
  • Biotechnology
  • Protein Engineering

Background:

  • Immunoglobulin G (IgG) hexamerisation is a natural process influencing antibody function.
  • Existing mutations enhancing IgG hexamerisation primarily target surface residues.
  • Enhanced hexamerisation can significantly improve antibody-dependent cellular cytotoxicity (ADCC) and antigen binding.

Purpose of the Study:

  • To explore novel strategies for engineering IgG hexamerisation.
  • To investigate the impact of modifying the buried H429 residue in the CH3 domain.
  • To introduce Stellabody technology for controlled IgG hexamerisation.

Main Methods:

  • Engineering of the H429 residue within the CH3 domain of IgG.
  • Development of Stellabody technology with distinct amino acid substitutions (H429F, H429Y).
  • Assessment of hexamerisation outcomes, including on-target and pH-sensitive mechanisms.

Main Results:

  • H429F mutation leads to monomeric IgG that hexamerises upon target binding ('on-target' hexamerisation).
  • H429Y mutation results in pH-sensitive hexamers forming in solution before antigen binding.
  • Stellabody technology demonstrates broad applicability across various antibody formats and therapeutic targets.

Conclusions:

  • Engineering the H429 residue offers a unique approach to control IgG hexamerisation.
  • Stellabody technology provides distinct mechanisms for enhanced antibody potency and function.
  • This technology has wide-ranging applications in developing next-generation antibody-based immunotherapeutics.