Immunoglobulin A is the dominant antibody for mucosal homeostasis in the gastrointestinal, respiratory, and genitourinary tracts. This means they can be found in body secretions such as tears, saliva, respiratory and intestinal secretions, and makes up 50% of the protein in colostrum. IgA gets produced by class switching of Ig and protects against pathogens by neutralization or prevention from binding to the mucosal surfaces.
Researchers are still debating the exact mechanisms and functions of IgA, as there may be large differences between IgA in different mucosal tissues. For instance, a paper by Pabst & Slack (2020) details the disagreement about the relevancy of T cell-dependent versus T cell-independent IgA in both microbiota and infection control.1,2
When in serum, IgA is usually a monomer, but in mucosa, secretory IgA takes a dimeric form with a J-chain and a secretory component. Secretory IgA is produced through the functions of plasma cells producing multimeric IgA and epithelial cells producing pIgR. Which form IgA takes does have interesting consequences, for instance, with how polymeric IgA is more effective than monomeric IgA in preventing Clostridium difficile toxins.
IgA can also be further classified into IgA1 and IgA2. IgA1 has a longer hinge region than IgA2, with a duplicated section of amino acids, making it more susceptible to cleavage from bacterial proteases. This may explain why IgA2 is dominant in many mucosal secretions and the colon, while approximately 90% of total IgA in serum is comprised of IgA1.3
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Schroeder, H. W., & Cavacini, L. (2010). Structure and Function of Immunoglobulins. The Journal of Allergy and Clinical Immunology, 125(2 0 2), S41. https://doi.org/10.1016/J.JACI.2009.09.046
Pabst, O., & Slack, E. (2019). IgA and the intestinal microbiota: the importance of being specific. Mucosal Immunology 2019 13:1, 13(1), 12–21. https://doi.org/10.1038/s41385-019-0227-4
Stubbe, H., Berdoz, J., Kraehenbuhl, J.-P., & Corthésy, B. (2000). Polymeric IgA is superior to monomeric IgA and IgG carrying the same variable domain in preventing Clostridium difficile toxin A damaging of T84 monolayers. Journal of Immunology (Baltimore, Md. : 1950), 164(4), 1952–1960. https://doi.org/10.4049/JIMMUNOL.164.4.1952
Antibody specificity refers to an antibody's ability to selectively bind to a unique epitope on a target antigen while avoiding interactions with unrelated antigens. This property arises from the highly specialized antigen-binding site located in the variable region of the antibody, which determines its unique binding characteristics.
Antibody affinity refers to the strength of the binding interaction between a single antigen epitope and the paratope (binding site) of an antibody. This interaction is a fundamental measure of how well an antibody recognizes its specific antigen target.
Recombinant antibodies are produced using genetic engineering techniques, unlike traditional antibody production, where the immune system generates antibodies without direct control over their sequence. By introducing genes encoding antibody fragments into host cells, such as bacteria or mammalian cells, recombinant antibodies can be expressed, purified, and deployed for applications including research, diagnostics, and therapeutics.
Recombinant antibody expression is a biotechnological process that involves engineering and producing antibodies outside their natural context using recombinant DNA technology.
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