Gemma Seabright

I joined the biotechnology team at D Young & Co in 2019. My background is in biology and biochemistry and I am particularly excited to work on new developments in the fields of vaccinology and immunotherapy.

Since joining the firm, I have gained experience in patent prosecution and opposition for a variety of clients, including multinational companies, SMEs and academic institutions.

Prior to joining D Young & Co, I studied biology at undergraduate level before completing my PhD in biochemistry at the University of Oxford. My research related to HIV vaccine design, in particular using mass spectrometry to analyse the glycans on the viral Envelope protein. I also have experience in the production and analysis of monoclonal antibodies.

Publications

• Seabright, G. E. et al., 2020. Networks of HIV-1 envelope glycans maintain antibody epitopes in the face of glycan additions and deletions. bioRxiv 2020.02.21.959981.
• Watanabe, Y. et al., 2020. Vulnerabilities in coronavirus glycan shields despite extensive glycosylation. bioRxiv 2020.02.20.957472.
• Dubrovskaya, V. et al. 2019. Vaccination with Glycan-Modified HIV NFL Envelope Trimer-Liposomes Elicits Broadly Neutralizing Antibodies to Multiple Sites of Vulnerability. Immunity. 51(5):915-929.e7.
• Seabright, G. E. et al., 2019. Protein and Glycan Mimicry in HIV Vaccine Design. J Mol Biol. 431(12):2223-2247.
• Ringe, R. P. et al., 2019. Closing and Opening Holes in the Glycan Shield of HIV-1 Envelope Glycoprotein SOSIP Trimers Can Redirect the Neutralizing Antibody Response to the Newly Unmasked Epitopes. J Virol. 93(4):e01656-18.
• Struwe, W. B. et al., 2018. Site-Specific Glycosylation of Virion-Derived HIV-1 Env Is Mimicked by a Soluble Trimeric Immunogen. Cell Rep. 24(8):1958-1966.e5.
• Watanabe, Y. et al., 2018. Structure of the Lassa virus glycan shield provides a model for immunological resistance. Proc Natl Acad Sci U S A. 115(28):7320-7325.
• Watanabe, Y. et al., 2018. Signature of Antibody Domain Exchange by Native Mass Spectrometry and Collision-Induced Unfolding. Anal Chem. 90(12):7325-7331.
• Harvey, D. J. et al., 2018. Isomer Information from Ion Mobility Separation of High-Mannose Glycan Fragments. J Am Soc Mass Spectrom. 29(5):972-988.
• Behrens, A-J. et al., 2017. Targeting Glycans of HIV Envelope Glycoproteins for Vaccine Design. Chemical Biology of Glycoproteins, Chapter 11.
• Behrens, A-J. et al., 2016. Composition and Antigenic Effects of Individual Glycan Sites of a Trimeric HIV-1 Envelope Glycoprotein. Cell Rep. 14(11):2695-706.
• Vasiljevic, S. et al., 2015. Redirecting adenoviruses to tumour cells using therapeutic antibodies: Generation of a versatile human bispecific adaptor. Mol Immunol. 68(2 Pt A):234-43.
• Pritchard, L. K. et al., 2015. Glycan clustering stabilizes the mannose patch of HIV-1 and preserves vulnerability to broadly neutralizing antibodies. Nat Commun. 6:7479.
• Pritchard, L. K. et al., 2015. Structural Constraints Determine the Glycosylation of HIV-1 Envelope Trimers. Cell Rep. 11(10):1604-13.
• Yu, X. et al., 2015. A monoclonal antibody with anti-D-like activity in murine immune thrombocytopenia requires Fc domain function for immune thrombocytopenia ameliorative effects. Transfusion. 55(6 Pt 2):1501-11.