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About The Speaker

Sally Ward

Director of Translational Immunology at the Centre for Cancer Immunology in the University of Southampton

Sally Ward

Sally Ward completed her Ph.D. research in the Department of Biochemistry at Cambridge University in 1985 under the mentorship of Professor David Ellar. She subsequently carried out research on antibody repertoire technology in Sir Greg Winter’s laboratory at the MRC Laboratory of Molecular Biology in Cambridge. In 1990 she joined the University of Texas Southwestern Medical Center, Dallas, as an Assistant Professor. From 2002-2014, she was a Professor in the Department of Immunology at the same institution and in 2004 was appointed to the Paul and Betty Meek-FINA Professorship in Molecular Immunology. In 2014, shebecame a Professor at Texas A&M University Health Science Center, and in 2018 was appointed as Director of Translational Immunology and Professor of Molecular Immunology at the Centre for Cancer Immunology in Southampton, U.K.

Her interdisciplinary research involves the use of a combination of fluorescence imaging, protein engineering and in vivo studies to develop antibody-based therapeutics to treat autoimmunity, cancer and infectious disease. This has led to several technologies (half-life extension and the FcRn antagonist, efgartigimod) that have been licensed to biopharma. Efgartigimod (Vyvgart) has been developed by argenx, and has recently been approved to treat myasthenia gravis with ongoing late stage trials for multiple other antibody-mediated autoimmune diseases. Sally was a founding co-organiser of the Gordon Research Conference ‘Antibody Biology and Engineering’ (2010). She is past President of the Antibody Society (2022-2023) and was elected as a Fellow of the Royal Society in 2022.

Targeting FcRn for the therapy of autoimmune disease

The central role of FcRn in regulating immunoglobulin G (IgG) persistence and transport provides opportunities for targeting this receptor in multiple different diagnostic and therapeutic situations. The engineering of IgGs with higher affinity for FcRn can be used to produce antibodies with longer in vivo half-lives, but only if the low affinity of the IgG-FcRninteraction at near neutral pH is retained. Conversely, an engineered IgG or Fc fragmentwith increased affinity for FcRn at both acidic and near neutral pH acts as a potent inhibitor of FcRn. Consequently, such an antibody (‘Abdeg’, for antibody that enhancesIgG degradation) can lower the levels of endogenous IgG and has led to the FcRn antagonist, efgartigimod, that has been developed by argenx and recently approved for the treatment of myasthenia gravis. Our recent work has also resulted in the generation of engineered Fc-fusions that selectively clear antigen-specific antibodies (‘Seldegs’, for selective degradation). Developments related to the modulation of the dynamic behavior of IgG in the bodywill be presented.

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