scholarly journals Antigen Binding to Secretory Immunoglobulin A Results in Decreased Sensitivity to Intestinal Proteases and Increased Binding to Cellular Fc Receptors

2009 ◽  
Vol 285 (2) ◽  
pp. 953-960 ◽  
Author(s):  
Mélanie Duc ◽  
Finn-Eirik Johansen ◽  
Blaise Corthésy
1996 ◽  
Vol 271 (27) ◽  
pp. 16300-16309 ◽  
Author(s):  
Elke Lüllau ◽  
Stephan Heyse ◽  
Horst Vogel ◽  
Ian Marison ◽  
Urs von Stockar ◽  
...  

Pharmacology ◽  
2021 ◽  
pp. 1-10
Author(s):  
Ekaterina N. Gorshkova ◽  
Shina Pashova ◽  
Ekaterina A. Vasilenko ◽  
Tatiana S. Tchurina ◽  
Elizaveta A. Razzorenova ◽  
...  

<b><i>Introduction:</i></b> 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. <b><i>Methods:</i></b> 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. <b><i>Results:</i></b> 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. <b><i>Conclusions:</i></b> 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.


Author(s):  
Claudia Seikrit ◽  
Oliver Pabst

AbstractAntibodies are key elements of protective immunity. In the mucosal immune system in particular, secretory immunoglobulin A (SIgA), the most abundantly produced antibody isotype, protects against infections, shields the mucosal surface from toxins and environmental factors, and regulates immune homeostasis and a peaceful coexistence with our microbiota. However, the dark side of IgA biology promotes the formation of immune complexes and provokes pathologies, e.g., IgA nephropathy (IgAN). The precise mechanisms of how IgA responses become deregulated and pathogenic in IgAN remain unresolved. Yet, as the field of microbiota research moved into the limelight, our basic understanding of IgA biology has been taking a leap forward. Here, we discuss the structure of IgA, the anatomical and cellular foundation of mucosal antibody responses, and current concepts of how we envision the interaction of SIgA and the microbiota. We center on key concepts in the field while taking account of both historic findings and exciting new observations to provide a comprehensive groundwork for the understanding of IgA biology from the perspective of a mucosal immunologist.


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