Therapeutic antibodies are increasingly used in several indications, such as oncology and autoimmunity. Antibodies with an unmodified Fc are increasingly being replaced with IgG antibodies with an engineered Fc domain. Alternative subclasses and isotypes are also being explored. The aim of these modifications are to influence the natural interactions with immune effector functions, such as Fc receptors and complement. These efforts ultimately hope to improve efficacy and safety of therapeutic antibodies.
The effector functions induced by Fc domains of the therapeutic antibodies represents complex interactions in vivo. The type and magnitude of these are influenced by a number of factors. However it is not well understood how in vitro results, and pre-clinical in vivo studies, translate into clinical efficacy. In vitro, often an isolated effector function is studied and the effector functions in pre-clinical mouse models differ from those present in humans. This Research Topic aims to collate articles exploring improvements in the predictive translational value of modified IgG Fc domains.
We welcome submissions on the Effector functions of therapeutic antibodies, with Original Research and Review articles focusing on, but not limited to, the following specific themes:
• IgG Fc domain modifications resulting in altered effector functions
• Effect of IgG Fc modifications in preclinical animal models
• IgG – Fc receptor interactions
• IgG – complement interactions
• IgG effector functions in mice vs men, lessons learned
• Association between antibody efficacy and polymorphisms in effector molecules in humans (clinical studies)
• Alternative isotypes and IgG subclasses
• IgG effector dead mutations
Dr. Peter Boross is an employee of Genmab BV, investigating the application of Antibody effector functions for drug therapy. The other Topic Editors declare no competing interests with relation to the Research Topic theme.
Therapeutic antibodies are increasingly used in several indications, such as oncology and autoimmunity. Antibodies with an unmodified Fc are increasingly being replaced with IgG antibodies with an engineered Fc domain. Alternative subclasses and isotypes are also being explored. The aim of these modifications are to influence the natural interactions with immune effector functions, such as Fc receptors and complement. These efforts ultimately hope to improve efficacy and safety of therapeutic antibodies.
The effector functions induced by Fc domains of the therapeutic antibodies represents complex interactions in vivo. The type and magnitude of these are influenced by a number of factors. However it is not well understood how in vitro results, and pre-clinical in vivo studies, translate into clinical efficacy. In vitro, often an isolated effector function is studied and the effector functions in pre-clinical mouse models differ from those present in humans. This Research Topic aims to collate articles exploring improvements in the predictive translational value of modified IgG Fc domains.
We welcome submissions on the Effector functions of therapeutic antibodies, with Original Research and Review articles focusing on, but not limited to, the following specific themes:
• IgG Fc domain modifications resulting in altered effector functions
• Effect of IgG Fc modifications in preclinical animal models
• IgG – Fc receptor interactions
• IgG – complement interactions
• IgG effector functions in mice vs men, lessons learned
• Association between antibody efficacy and polymorphisms in effector molecules in humans (clinical studies)
• Alternative isotypes and IgG subclasses
• IgG effector dead mutations
Dr. Peter Boross is an employee of Genmab BV, investigating the application of Antibody effector functions for drug therapy. The other Topic Editors declare no competing interests with relation to the Research Topic theme.
