CD16a is encoded by the FCGR3A gene and is expressed on the surface of natural killer (NK) cells, macrophages, and a subset of T cells. It is a transmembrane protein that consists of an extracellular domain, a transmembrane domain, and a cytoplasmic tail. The extracellular domain is responsible for binding to the Fc region of IgG, while the cytoplasmic tail is involved in signal transduction .
There are two isoforms of CD16: CD16a and CD16b. CD16a is expressed on NK cells and macrophages, while CD16b is expressed on neutrophils. The two isoforms differ in their membrane anchoring; CD16a is anchored via a transmembrane domain, whereas CD16b is anchored via a glycosylphosphatidylinositol (GPI) linkage .
CD16a plays a pivotal role in the immune response by mediating ADCC, a mechanism through which NK cells lyse target cells that are coated with antibodies. When CD16a binds to the Fc region of IgG on the surface of target cells, it triggers the release of cytotoxic granules from NK cells, leading to the destruction of the target cells .
Additionally, CD16a is involved in the phagocytosis of antibody-coated pathogens by macrophages. Upon binding to immune complexes, CD16a activates signaling pathways that result in the engulfment and degradation of the pathogens .
Recombinant CD16a is a laboratory-produced version of the natural receptor, created using recombinant DNA technology. It is typically produced in mammalian cell lines, such as Chinese hamster ovary (CHO) cells, to ensure proper folding and post-translational modifications. Recombinant CD16a is used in various research applications, including studies on ADCC, immune complex clearance, and receptor-ligand interactions .
Recombinant CD16a is widely used in immunological research to study the mechanisms of ADCC and other Fc receptor-mediated processes. It is also employed in the development of therapeutic antibodies, as understanding the interaction between CD16a and IgG can help optimize antibody design for enhanced efficacy .