FcγRIII, synonymously also referred to CD16, is a type III Fcγ receptor which has other two identified members: a high-affinity receptor FcγRI (CD64) and a low-affinity one FcγRII (CD32). This transmembrane protein, FcγRIII, contains two extracellular immunoglobulin (Ig)-like domains with low-affinity for IgG. It is responsible for antibody-dependent cellular cytotoxicity. FcγRIII is expressed on large granular lymphocytes of both nature killer (NK)- and T-cell types. There are two different isoforms of it in humans named FcγRIIIa and FcγRIIIb, sharing 96% sequence identity in extracellular Ig binding regions. FcγRIIIa is a transmembrane receptor found on macrophages, mast and NK cells. FcγRIIIb is expressed exclusively on neutrophils and functions as the only Fc receptor anchored via a glycosyl-phosphatidylinositol (GPI) linker to the cell membrane. GD2 is a kind of disialoganglioside expressed on tumor cells of neuroectodermal origin, including melanoma, glioma and neuroblastoma. Ganglioside GD2 is a sialic acid-containing glycosphingolipid involved in cell attachment to the extracellular matrix. Its expression is highly restricted in normal tissues, principally to the central nervous system, peripheral nerves, skin melanocytes, and mesenchymal stem cells of humans. The relatively specific tumor expression of GD2 makes it a suitable target for clinical therapy with monoclonal antibodies or artificial T cell receptors. Recently, GD2 has been proposed as a marker for some cancer cells and targeting ganglioside GD2 with immunotherapy has resulted in an improved outcome for patients suffering neuroblastoma.