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Related Concept Videos

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Hybridoma Technology

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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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Proteins are involved in several cellular processes and biochemical reactions. Analyzing a specific protein of interest requires it to be isolated from the other proteins in the cell. This is achieved by overexpressing the specific gene in a suitable host to produce large quantities of the target protein. A tag or label is recombined with the gene to produce a fusion protein containing the target protein and the tag. The tags on these fusion proteins can then be used for easy detection and...
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Half-Life Extension of the IgG-Degrading Enzyme (IdeS) Using Fc-Fusion Technology.

Victoria Daventure1, Melissa Bou-Jaoudeh1, Emna Hannachi1

  • 1Institut National de la Santé et de la Recherche Médicale, Centre de Recherche des Cordeliers, CNRS, Sorbonne Université, Université Paris Cité, Paris, France.

European Journal of Immunology
|December 20, 2024
PubMed
Summary

Engineered imlifidase (IdeS) fused with Fc fragments demonstrated extended half-life and sustained IgG-depleting activity. This innovation could improve treatments for IgG-mediated diseases requiring prolonged therapeutic effects.

Keywords:
IdeSIgG eliminationImlifidasepharmacokinetics

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Area of Science:

  • Biochemistry
  • Immunology
  • Protein Engineering

Background:

  • Imlifidase (IdeS) is a bacterial protease that cleaves human IgG, reducing its half-life and Fc-mediated functions.
  • IdeS is used in kidney transplant rejection prevention and is evaluated for IgG-mediated autoimmune diseases.
  • The short half-life of IdeS limits its application in chronic conditions necessitating repeated dosing.

Purpose of the Study:

  • To engineer IdeS-Fc fusion proteins to prolong the IgG-depleting action of IdeS in vivo.
  • To evaluate the efficacy and pharmacokinetic properties of divalent (IdeS-Fcdiv) and monovalent (IdeS-Fcmonov) IdeS-Fc fusion proteins.

Main Methods:

  • Development of IdeS-Fc fusion proteins (divalent and monovalent heterodimers).
  • Assessment of IgG hydrolysis kinetics by IdeS-Fc fusion proteins.
  • In vivo half-life determination and residual IgG cleavage evaluation of IdeS-Fcmonov compared to IdeS.

Main Results:

  • Both IdeS-Fc fusion proteins effectively cleaved human IgG into F(ab')2 and Fc fragments, albeit with slower kinetics than native IdeS.
  • IdeS-Fcmonov showed a seven-fold extension in half-life compared to IdeS.
  • IdeS-Fcmonov demonstrated significantly better residual IgG cleavage at later time points post-injection.

Conclusions:

  • IdeS-Fc fusion proteins represent a viable strategy for extending the in vivo therapeutic duration of IdeS.
  • IdeS-Fcmonov offers a promising approach for sustained IgG hydrolysis, potentially benefiting chronic IgG-mediated diseases.
  • The developed IdeS-Fc fusion proteins provide proof of concept for enhanced IgG-depleting therapies with potential for rapid clinical translation.