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Induced Polyspecificity of Human Secretory Immunoglobulin A Antibodies: Is It Possible to Improve Their Ability to Bind Pathogens? | LitMetric

AI Article Synopsis

  • Researchers studied how different substances can change how well a specific protein in our body, called secretory immunoglobulin A (sIgA), can grab onto germs like viruses and bacteria.
  • They tested sIgA by exposing it to things like acidic solutions, free heme, and some metal ions to see how these affected its ability to bind to germs.
  • They found that acidic solutions made sIgA bind better to various germs, more than the other treatments, which means it could help our body respond to infections more effectively.

Article Abstract

Introduction: As has been shown previously, various protein-modifying agents can change the antigen-binding properties of immunoglobulins. However, induced polyspecificity of human secretory immunoglobulin A (sIgA) has not been previously characterized in detail.

Methods: In the present study, human secretory immunoglobulin A (IgA) was exposed to buffers with acidic pH, to free heme, or to pro-oxidative ferrous ions, and the antigen-binding behavior of the native and modified IgA to viral and bacterial antigens was compared using Western blotting and enzyme-linked immunosorbent assay. The ability of these agents to modulate the antigen-binding properties of human sIgA toward a wide range of pathogen peptides was investigated using an epitope microarray.

Results: We have shown that acidic pH, heme, and pro-oxidative ferrous ions influenced the binding of secretory IgA in opposite directions (either increasing or decreasing); however, the strongest effect was observed when using buffers with low pH. This fraction had the highest number of affected reactivities; most of them were increased and most of the new ones were toward common pathogens.

Conclusions: Thus, it was shown that all investigated treatments can alter to some degree the antigen-binding of secretory IgA, but acidic pH has the most potentially beneficial effect by increasing binding to a largest number of common pathogens' antigens.

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Source
http://dx.doi.org/10.1159/000520343DOI Listing

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