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SELECTBIO Conferences High-Content and Phenotypic Screening Europe 2018

E. Sally Ward's Biography

E. Sally Ward, Professor, Texas A&M University Health Science Center

Sally Ward completed her Ph.D. research in the Department of Biochemistry, Cambridge University in 1985 in the laboratory of Professor David Ellar. From 1985-1988 she was a Research Fellow at Gonville and Caius College whilst working at the Department of Biochemistry, Cambridge University. From 1988 to 1990, she held the Stanley Elmore Senior Research Fellowship at Sidney Sussex College whilst carrying out research in Sir Greg Winter’s laboratory at the MRC Laboratory of Molecular Biology, Cambridge. In 1990 she joined UT Southwestern Medical Center, Dallas, as an Assistant Professor. From 2002-2014, she was a Professor in the Department of Immunology at UT Southwestern and in 2004 was appointed to the Paul and Betty Meek-FINA Professorship in Molecular Immunology. Since 2014, she has been a Professor at Texas A&M University Health Science Center. Her current research includes the use of a combination of fluorescence imaging, protein engineering and in vivo studies to develop therapeutics to treat cancer and autoimmunity. She was a founding co-organizer of the Gordon Research Conference ‘Antibody Biology and Engineering’ in 2010. She is a member of the Board of Distinguished Advisors in the Antibody Society and serves on the editorial boards of mAbs and Protein Engineering, Design and Selection.

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Exploiting the Multiple Functions of FcRn for Therapy

Friday, 25 May 2018 at 14:00

Add to Calendar ▼2018-05-25 14:00:002018-05-25 15:00:00Europe/LondonExploiting the Multiple Functions of FcRn for TherapyHigh-Content and Phenotypic Screening Europe 2018 in Cambridge, UKCambridge,

The central role of FcRn in regulating 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 pH dependence of the IgG-FcRn interaction is retained. Conversely, engineered IgGs with increased affinity for FcRn at both acidic and near neutral pH act as potent inhibitors of FcRn. Consequently, such antibodies (‘Abdegs’, for antibodies that enhance IgG degradation) can lower the levels of endogenous IgG. Recent studies in our laboratory have also resulted in the generation of engineered Fc-fusions that selectively clear antigen-specific antibodies (‘Seldegs’, for selective degradation). Recent developments related to the modulation of IgG dynamics will be presented.  We have demonstrated that the loss of expression of FcRn in tumor cells results in increased intracellular albumin accumulation and tumor growth in mouse models. These observations have implications for tumor immunotherapy and indicate a novel function for FcRn as a metabolic regulator.

Add to Calendar ▼2018-05-24 00:00:002018-05-25 00:00:00Europe/LondonHigh-Content and Phenotypic Screening Europe 2018High-Content and Phenotypic Screening Europe 2018 in Cambridge, UKCambridge,