Doryen Bubeck received her PhD in Biophysics from Harvard University in 2005 where she used cryo-electron microscopy (cryo-EM) to investigate the cell entry mechanism of poliovirus. As an EMBO postdoctoral fellow and Cancer Research Institute Fellow at the University of Oxford, she continued to explore the structures of membrane proteins, focusing on the complement immune pathway. Over 50 years since the complement membrane attack complex was visualized, a recent highlight from the lab reports the first 3D structure of the complete pore. These results provide a framework for understanding the complex protein associations underlying activation of this innate immune effector and opens new directions of research investigating the lipid environment’s impact on MAC function. Doryen Bubeck is a Reader in Structural Immunology within the Department of Life Sciences and holds a Satellite Group Leader position at the Francis Crick Institute. She is currently the Director of the Centre for Structural Biology at Imperial College. Her current research adopts a structural to investigate the role of membrane proteins in host-pathogen interactions. Supported by an ERC Consolidator Award, she aims to investigate how membrane attack complex (MAC) pore formation is controlled, a process important for fighting infections and preventing complement-mediated tissue damage.
New work from the lab out in Nature Communications!
Bubeck lab culture word cloud, created by lab members past and present:
et al., 2021, Structural basis of soluble membrane attack complex packaging for clearance, Nature Communications, Vol:12, ISSN:2041-1723
et al., 2020, Structural basis for tuning activity and membrane specificity of bacterial cytolysins, Nature Communications, Vol:11, ISSN:2041-1723
et al., 2019, Structural basis of light-induced redox regulation in the Calvin-Benson cycle in cyanobacteria, Proceedings of the National Academy of Sciences of the United States of America, Vol:116, ISSN:0027-8424, Pages:20984-20990
et al., 2019, Single-molecule kinetics of pore assembly by the membrane attack complex, Nature Communications, Vol:10, ISSN:2041-1723, Pages:1-10
et al., 2018, CryoEM reveals how the complement membrane attack complex ruptures lipid bilayers, Nature Communications, Vol:9, ISSN:2041-1723
Boyd CM, Bubeck DA, 2018, Advances in cryoEM and its impact on beta-pore forming proteins, Current Opinion in Structural Biology, Vol:52, ISSN:0959-440X, Pages:41-49
et al., 2016, Disentangling the roles of cholesterol and CD59 in intermedilysin pore formation, Scientific Reports, Vol:6, ISSN:2045-2322
et al., 2016, Structural basis of complement membrane attack complex formation, Nature Communications, Vol:7, ISSN:2041-1723, Pages:1-7
et al., 2013, Structural basis for recognition of the pore-forming toxin intermedilysin by human complement receptor CD59, Cell Reports, Vol:3
et al., 2012, Assembly and Regulation of the Membrane Attack Complex Based on Structures of C5b6 and sC5b9, Cell Reports, Vol:1, ISSN:2211-1247, Pages:200-207