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Updated: Jul 17, 2026
Assessment of Human Natural Killer Cell Events Driven by FcγRIIIa Engagement in the Presence of Therapeutic Antibodies
Published on: May 22, 2020
Antibodies, Fc receptors and cancer
Falk Nimmerjahn1, Jeffrey V Ravetch
1Laboratory of Molecular Genetics and Immunology, The Rockefeller University, 1230 York Avenue, New York, NY 10021, USA.
Since the first report of the successful use of a monoclonal antibody for the treatment of human B cell lymphoma in 1982, several antibodies have become incorporated into standard treatment protocols for cancer. One of the most important factors that determine antibody activity in vivo is the efficient interaction with cellular Fc-receptors on innate immune effector cells. It has become clear that the outcome of this interaction is influenced by several factors, such as the antibody isotype-specific affinity to activating and inhibitory receptors, the level of inhibitory FcgammaRIIB expression, and the composition of the sugar side chain attached to the antibody Fc-portion. These novel insights into antibody FcR interactions might be useful to produce the next generation of improved immunotherapeutic molecules.
Since the first report of the successful use of a monoclonal antibody for the treatment of human B cell lymphoma in 1982, several antibodies have become incorporated into standard treatment protocols for cancer. One of the most important factors that determine antibody activity in vivo is the efficient interaction with cellular Fc-receptors on innate immune effector cells. It has become clear that the outcome of this interaction is influenced by several factors, such as the antibody isotype-specific affinity to activating and inhibitory receptors, the level of inhibitory FcgammaRIIB expression, and the composition of the sugar side chain attached to the antibody Fc-portion. These novel insights into antibody FcR interactions might be useful to produce the next generation of improved immunotherapeutic molecules.
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