Rate My Professor Ben Luisi

Ben Luisi serves as Professor of Structural and Molecular Cell Biology in the Department of Biochemistry at the University of Cambridge. He obtained his PhD at the MRC Laboratory of Molecular Biology, University of Cambridge. As head of the Luisi Group, his research centers on the machinery of riboregulation and transport in bacteria. This includes studies of multi-component assemblies that regulate gene expression by controlling the stability and processing of messenger RNA, facilitating rapid responses to environmental and developmental signals through interactions with non-coding regulatory RNAs. Luisi also investigates bacterial multi-drug efflux pumps, particularly tripartite assemblies that span the cell envelope of Gram-negative bacteria, elucidating mechanisms underlying protein and antibiotic transport, bacterial virulence, and drug resistance. His laboratory utilizes X-ray diffraction, cryo-electron microscopy, and complementary biophysical techniques to determine atomic structures and analyze macromolecular complexes.

Luisi has held positions within the Department of Biochemistry, including heading the X-ray crystallography facility established in 1997. He was elected as an EMBO Fellow in 2009 for his contributions to understanding regulatory assemblies and molecular machines. His scholarly impact is substantial, with over 22,900 citations from 346 publications documented on ResearchGate. Notable works include: Du, D. et al. (2014). Structure of the AcrAB-TolC multidrug efflux pump. Nature, 509, 512-515; Koronakis, V. et al. (2000). Crystal structure of the bacterial membrane protein TolC central to multidrug efflux and protein export. Nature, 405, 914-919; Callaghan, A.J. et al. (2005). Structure of Escherichia coli RNase E catalytic domain and implications for RNA turnover. Nature, 437, 1187-1191; Bandyra, K.J. et al. (2018). Substrate recognition and autoinhibition in the central ribonuclease RNase E. Molecular Cell, 72, 275-285; Islam, M.S. et al. (2023). Structure of a bacterial ribonucleoprotein complex central to the control of cell envelope biogenesis. The EMBO Journal, 42, e112574; and recent publications such as Fountain, A.J. et al. (2025). Structural and functional analysis of the Mycobacterium tuberculosis MmpS5L5 efflux pump presages increased bedaquiline resistance. PNAS, 122, e2516660122.