Thomas A Bowden
Supernumerary Fellow in Structural Biology; Associate Professor of Structural Biology
My current teaching is predominantly dedicated to graduate student supervision. My laboratory is located in the Division of Structural Biology, Wellcome Trust Centre for Human Genetics, and specializes in the adoption of techniques in protein biochemistry and structural biology to study protein-protein interactions. Students in my group are trained in a range of methodologies ranging from molecular biology and protein purification to X-ray crystallography and protein structure determination. I am also involved in graduate student examination and assessment.
Emerging zoonotic viruses cross the species barrier from animals to humans or vice-versa. Their ability to propagate in human cells is dependent on a variety of factors, most importantly, the capacity to target particular cell types by binding to receptor molecules displayed on the cell surface. My group is interested in applying techniques in structural biology, immunology, and cell biology, to establish how viral proteins, which are displayed on the surface of emerging and neglected RNA viruses, facilitate cross-species viral spillover. This work provides molecular-level models for how viruses interact with host cells and can be transmitted to unrelated organisms. Ultimately, the information derived from these studies is being aimed towards the development of therapeutic reagents that can prevent virus infection.
Zeltina A and Bowden TA (2017) Human antibody pieces together the puzzle of the trimeric Lassa virus surface antigen. Nature Structural and Molecular Biology, 7: 559-560.
Rissanen I, Ahmed AA, Azarm K, Beaty S, Hong P, Nambulli S, Duprex WP, Lee B, Bowden TA (2017) Idiosyncratic Mòjiāng virus attachment glycoprotein directs a host-cell entry pathway distinct from genetically related henipaviruses. Nature Communications, 8:16060.
Zeltina, A, Krumm S, Sahin M, Struwe WB, Harlos K, Nunberg JH, Crispin M, Pinschewer DD, Doores KJ, Bowden TA (2017) Convergent immunological solutions to Argentine hemorrhagic fever virus neutralization. Proceedings of the National Academy of Sciences, 114: 7031-7036.
Rissanen I, Stass R, Zeltina A, Hepojoki J, Harlos K, Gilbert RJC, Huiskonen JT, Bowden TA. Structural transitions of the conserved and metastable architecture of the hantaviral glycoprotein envelope. Journal of Virology, [Epub ahead of print].
Halldorsson S, Behrens AJ, Harlos K, Huiskonen JT, Elliott RM, Crispin M, Brennan B, Bowden TA (2016) Crystal structure of a phleboviral Gc glycoprotein reveals a consolidated model of membrane fusion. Proceedings of the National Academy of Sciences, 113: 7154-9.
Li S, Rissanen I, Zeltina A, Hepojoki J, Raghwani J, Harlos K, Pybus OG, Huiskonen JT, Bowden TA (2016) A molecular-level account of the antigenic hantaviral surface. Cell Reports, 15: 959-67.
Zhao Y, Jingshan R, Harlos K, Zeltina A, Bowden TA, Fry EF, Padilla-Parra S, Jones D, Stuart DI (2016) Toremifene inhibits Ebola virus infection by destabilizing the viral glycoprotein. Nature, 535: 169-72.
Lee B, Pernet O, Ahmed AA, Zeltina A, Beaty SM, Bowden TA (2015) Molecular recognition of human ephrinB2 cell surface receptor by an emergent African henipavirus. Proceedings of the National Academy of Science, 112: E2156-2165.
Crispin M, Yu X, Bowden TA (2013) Crystal structure of sialylated IgG Fc: Implications for the mechanism of IVIg therapy. Proceedings of the National Academy of Science, 110: e3544-46.
Bowden TA, Baruah K, Coles CH, Harvey DJ, Song B, Stuart DI, Aricescu AR, Scanlan CN, Jones EY, Crispin M (2012) Chemical and structural analysis of an antibody folding intermediate trapped during glycan biosynthesis. Journal of the American Chemical Society, 134: 17554-63.
For a complete list please see ndm.ox.ac.uk