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  • 1Hotung Molecular Immunology Laboratory, Institute for Infection and Immunity, School of Health and Medical Sciences, City St. George's University of London, London, UK.

Biotechnology Journal
|May 28, 2026
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Secretory IgA (SIgA) antibodies are crucial for mucosal immunity. Engineering SIgA with Protein A-binding IgG Fc domains enables efficient purification, unlocking SIgA biologics potential.

Area of Science:

  • Immunology
  • Biotechnology
  • Protein Engineering

Background:

  • Secretory IgA (SIgA) is vital for mucosal defense.
  • Monoclonal SIgA antibodies offer novel therapeutic potential but face purification challenges.
  • Current purification methods are hindered by IgA's low affinity for Protein A.

Purpose of the Study:

  • To develop a method for efficient affinity purification of SIgA monoclonal antibodies (mAbs).
  • To engineer a secretory component (SC) with Protein A binding capabilities.
  • To assess the impact of engineered SC on SIgA assembly and antigen-binding functionality.

Main Methods:

  • Engineered chimaeric SC by replacing domains with IgG Fc (CH2-CH3) regions.
  • Expressed recombinant monoclonal SIgA containing the engineered SC.
Keywords:
Protein Aantibody engineeringsecretory component

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  • Utilized Protein A affinity chromatography for SIgA purification.

    • Main Results:

    • Engineered SC enabled Protein A affinity purification of SIgA.
    • SIgA assembly and antigen-binding functionality were preserved.
    • Purification successfully separated SIgA from assembly intermediates like dimeric IgA.

    Conclusions:

    • SC-Fc fusions provide a viable strategy for SIgA mAb purification.
    • This approach streamlines manufacturing and could unlock clinical applications for SIgA biologics.