E. Sally Ward

Ward was an undergraduate student at the University of Cambridge, where she studied the Natural Sciences Tripos with a focus on biochemistry. She remained at Cambridge for her doctoral research, working under the supervision of David J. Ellar at Gonville and Caius College, Cambridge.[4][5][6] Her PhD research investigated the genetics of delta endotoxin from Bacillus thuringiensis israelensis.[7]

Ward remained at Cambridge as a junior research fellow, working in both Gonville and Caius College and Sidney Sussex College, Cambridge.[8]

In 1990, Ward moved to the United States. She joined the University of Texas Southwestern Medical Center, where she was a member of the founding team of the Centre for Immunology. She was awarded various named chairs in Texas, including the Paul and Betty Meek-FINA Professorship. In 1996, Ward identified the Fc receptor, a regulator of Immunoglobulin G levels.[9] She moved to the Texas A&M University Health Sciences University in 2014.[9] In 2018, Ward returned to the United Kingdom, joining the University of Southampton as Professor of Molecular Immunology and Director of Translational Immunology.[10][11]

Ward works on antibody and protein engineering to treat autoimmune disease.[12] She makes use of in vivo studies to design novel anti-body therapies for the treatment of cancer. Her early identification of the Fc receptor has resulted in the development of FcRn antagonist technologies.[13][14] Ward has licensed these Abdegs (antibodies that enhance IgG degradation) to the pharmaceutical industry, resulting in anti-body therapeutics.[9][14][15]

Ward has developed advanced microscopies and image analysis techniques. She has demonstrated single molecule spectroscopy is capable of imaging single protein molecules at exceptional resolution. She uses multi-colour imaging to interrogate the cell surfaces. Using these approaches, Ward visualised the biological pathways intracellular endoscopes to the plasma membrane (and vice versa).[12] She has also pioneered open access software packages for miroscopy analysis.[12]

• Binding activities of a repertoire of single immunoglobulin variable domains secreted from Escherichia coli[16]
• Localization accuracy in single-molecule microscopy"[17]
• Multiple roles for the major histocompatibility complex class I- related receptor FcRn[18]
• Differences in promiscuity for antibody–FcRn interactions across species: implications for therapeutic antibodies[19]