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Stability Engineering of Recombinant Secretory IgA.

Kathrin Göritzer1,2, Richard Strasser1, Julian K-C Ma2

  • 1Department of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences, 1190 Vienna, Austria.

International Journal of Molecular Sciences
|July 13, 2024
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Summary
This summary is machine-generated.

Engineered secretory IgA2 antibodies show improved expression and stability for mucosal immunotherapy. Specific mutations enhance production and thermal stability, overcoming challenges for topical delivery applications.

Keywords:
IgAaerosolizationantibody engineeringmonoclonal antibodyplant molecular pharmingprotein assemblyprotein stabilitysecretory immunoglobulin A

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Area of Science:

  • Immunology
  • Biotechnology
  • Protein Engineering

Background:

  • Secretory IgA (SIgA) is a key immunotherapy candidate for mucosal surfaces.
  • Challenges in SIgA expression, purification, and stability hinder its therapeutic application.
  • IgA1 and IgA2 isotypes, along with IgA2 allotypes (IgA2m(1), IgA2m(2)), possess distinct structural and functional properties.

Purpose of the Study:

  • To engineer stable secretory IgA2 (SIgA2) variants for enhanced mucosal immunotherapy.
  • To address production and stability issues associated with the IgA2m(1) allotype.
  • To compare engineered SIgA2 with SIgA1 for SARS-CoV-2 topical delivery.

Main Methods:

  • Introduction of specific mutations to facilitate disulfide bond formation in IgA2.
  • Expression and purification of engineered SIgA2 variants in *Nicotiana benthamiana*.
  • Comparative analysis of expression levels, assembly efficacy, thermal stability, and aerosolization potential.

Main Results:

  • Engineered SIgA2 (P221R) demonstrated significantly improved expression and assembly in *Nicotiana benthamiana*.
  • Enhanced SIgA2 variants exhibited increased thermal stability under physiological and acidic conditions.
  • Engineered SIgA2 proved suitable for aerosolization via a mesh nebulizer.

Conclusions:

  • Stability-enhancing mutations effectively overcome hurdles in SIgA expression and stability.
  • Engineered SIgA2 represents a promising platform for developing stable and effective mucosal immunotherapies.
  • These findings pave the way for improved topical delivery of SIgA antibodies, including against SARS-CoV-2.