Immunoglobulin M is the first isotype to be expressed by the adaptive immune system in response to a foreign pathogen, during B cell development. It is typically present as the antigen receptor on the naïve B-cell surface, allow for the B cell to associate with the polypeptides CD79a and CD79b, which play roles in IgM cell signaling.
IgM is monomeric when first produced by plasma cells but when secreted can link to other IgM units to form a pentameric configuration containing a polypeptide J-chain. This occurs during maturation and antigenic stimulation and increases IgM’s avidity since there would be ten antigen-binding sites per pentameric molecule. Through interactions with the antigen, IgM can then opsonize it for destruction.
The detection of IgM can be used to diagnose patients from acute exposure to a pathogen, since IgM is typically linked with a primary immune response. However, it does not indicate whether the patient still has that pathogen or if it had been eliminated, since memory plasma cells help form immunological memory to generate antibodies against a pathogen for many more months and years to come.1
In addition, several disorders can be connected with IgM, such as X-linked Hyper-IgM Syndrome. This is a rare primary immune deficiency disorder, characterized by elevated IgM levels but deficient levels of other immunoglobulin isotypes, as well as defects in cellular immunity. Other disorders linked to IgM include Selective IgM Deficiency, Cold Agglutinin Disease, and Monoclonal Gammopathies.2
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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
Sathe, A., & Cusick, J. K. (2022). Biochemistry, Immunoglobulin M. StatPearls. https://www.ncbi.nlm.nih.gov/books/NBK555995/
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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