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Antibody Binding Specificity for Kappa (V&#954;) Light Chain-containing Human (IgM) Antibodies: Polysialic Acid (PSA) Attached to NCAM as a Case Study
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Induced antigen-binding polyreactivity in human serum IgA.

Ekaterina N Gorshkova1, Maxime Lecerf2, Irina V Astrakhantseva3

  • 1Center of Molecular Biology and Biomedicine, Institute of Biology and Biomedicine, National Research Lobachevsky State University of Nizhny Novgorod, 23 Gagarin Ave, Nizhny Novgorod 603022, Russian Federation.

Immunobiology
|April 16, 2022
PubMed
Summary
This summary is machine-generated.

Human IgA antibodies can acquire polyreactivity, increasing their ability to bind diverse viral and bacterial antigens. This newly discovered property suggests potential therapeutic applications for IgA in fighting infections.

Keywords:
Antibody specificityHuman serum IgAInduced polyreactivityMonoclonal IgA

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Area of Science:

  • Immunology
  • Biochemistry
  • Molecular Biology

Background:

  • Polyreactive antibodies are crucial for early defense against pathogens in hosts lacking prior immunity.
  • Antigen-binding polyreactivity can be intrinsic or acquired post-translationally.
  • While studied in IgG and IgE, the polyreactivity acquisition in human IgA has been minimally explored.

Purpose of the Study:

  • To investigate the capacity of human IgA to acquire antigen-binding polyreactivity.
  • To compare the antigen-binding profiles of native and modified human IgA antibodies.
  • To explore the potential therapeutic implications of induced IgA polyreactivity.

Main Methods:

  • Pooled human serum IgA and two human monoclonal IgA antibodies were treated with acidic pH, free heme, or ferrous ions.
  • Antigen-binding activity was assessed using immunoblot and ELISA assays.
  • Reactivity was compared between native and modified IgA against various viral and bacterial antigens.

Main Results:

  • Exposure to destabilizing agents (acidic pH) or pro-oxidative conditions (heme, ferrous ions) induced polyreactivity in human IgA.
  • A dose-dependent increase in IgA reactivity was observed against bacterial extracts and purified viral antigens.
  • This demonstrates a previously underappreciated ability of IgA to broaden its antigen-binding repertoire.

Conclusions:

  • Human IgA antibodies possess the ability to acquire antigen-binding polyreactivity upon exposure to specific environmental stressors.
  • This induced polyreactivity enhances IgA's binding to a range of microbial antigens.
  • The findings suggest that IgA polyreactivity could be harnessed for therapeutic strategies against infectious diseases.