Bruce Turnbull

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Professor at Faculty of Biological Sciences

University of Leeds
Country flagUnited Kingdom

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About

Professor Bruce Turnbull is a faculty member at the University of Leeds in the Faculty of Biological Sciences, located in the United Kingdom. His research focuses on cholera toxin mechanics, targeted delivery systems for oligonucleotides, and biocatalysis advancements. Recent articles include topics such as sortase-modified cholera toxoids and the synthesis of cholera toxin B subunit glycoconjugates.

Recent Grants

Grant: Close

BioEmPiRe; Accessing uncharted but essential landscapes to biological machineries by pulse EPR

Open Date: 2022-07-31

Close Date: 2023-07-30

Grant: Close

BubblEs for TArgeting and TReatment of biOfilm InfectioNs (BETATRON)

Open Date: 2022-06-30

Close Date: 2025-06-29

Grant: Close

Wrapping a virus-like particle

Open Date: 2021-06-01

Close Date:

Grant: Close

Rational design of dynamic molecules for enhanced multivalent binding

Open Date: 2019-05-01

Close Date: 2022-05-01

Grant: Close

synBIOcarb: Synthetic biology of carbohydrate-binding proteins: engineering protein-carbohydrate interactions for diagnostics and cell targeting

Open Date: 2018-10-01

Close Date: 2022-09-01

Positions (1)

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Bruce Turnbull

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University of Leeds

The University of Leeds invites applications for the MSCA PhD Fellow in Cross-Disciplinary Glycoscience Research (DC3 – Targeting tissues using multivalent lectin-glycan interactions), part of the Horizon Europe Marie Sklodowska-Curie Doctoral Network (MSCA-DN) GLYCOCALYX. This network unites 15 leading European partners in a multidisciplinary and intersectorial research and training programme, focusing on the self-organisation and barrier functions of the mammalian glycocalyx. The glycocalyx, a dense and complex coat of sugar chains (glycans) covering mammalian cells, is essential for multicellular life. It plays critical roles in inter-cellular communication, tissue development, homeostasis, repair, immune responses, neuronal connectivity, and symbiosis with bacteria. Dysregulation of the glycocalyx can lead to immune diseases, neurodegeneration, and cancer, and it also acts as a defence against pathogens, some of which have evolved to exploit it for infection. Despite its importance, the mammalian glycocalyx remains under-studied due to a lack of preparative and analytical tools and missing physics rules to interpret experimental observations. The GLYCOCALYX Network will train 15 PhD Fellows in chemistry, physics, and biology methods to resolve the dynamic organisation of glycocalyces. Three of these PhD Fellows will be hosted at the University of Leeds. The projects aim to establish a new understanding of how glycocalyces perform selective barrier functions. Fellows will receive cutting-edge scientific training and industry-relevant transferable skills, preparing them for careers in medical technology and research innovation. As the MSCA PhD Fellow (DC3) in Leeds, you will develop modular, multivalent glycocalyx probes to study density-dependent lectin–glycan interactions in molecularly defined model systems. You will elucidate the physical and chemical rules underlying superselective targeting, enabling the rational design of probes for super-resolution imaging of glycocalyx organisation and targeted delivery with exceptional cellular selectivity. The project involves developing new polymer scaffolds, using enzymatic and bio-orthogonal chemistry to functionalise lectins, and studying binding behaviour in model glycocalyces using QCM-D. Interactions with neuronal and endothelial cells will be visualised by super-resolution microscopy. The research combines chemical biology, glycoscience, theoretical modelling, and advanced imaging in an interdisciplinary environment. Applicants should have relevant research experience in chemistry or biochemistry and a keen interest in molecular tools for protein/glycan interactions. The application should include a letter of motivation, CV, contact details for two references (or their letters of recommendation), and transcripts of all higher education courses. The position offers a fixed salary of £53,780 per annum for 3 years (plus family allowance if applicable), in line with MSCA Doctoral Network requirements, subject to tax and National Insurance deductions. Applications must be submitted online by 23.59 (UK time) on March 30, 2026. For further information, contact Professor Bruce Turnbull ([email protected]) or Dr Ralf Richter ([email protected]). More guidance and the application portal can be found at this link .

7 months ago

Articles (14)

Mastering selective molecule trafficking across human cell membranes poses a formidable challenge in healthcare biotechnology while offering the prospect of breakthroughs in drug delivery, gene therapy, and diagnostic imaging. The cholera toxin B-subunit (CTB) has the potential to be a useful cargo transporter for these applications. CTB is a robust protein that is amenable to reengineering for diverse applications; however, protein redesign has mostly focused on modifications of the N- and C-termini of the protein. Exploiting the full power of rational redesign requires a detailed understanding of the contributions of the surface residues to protein stability and binding activity. Here, we employed Rosetta-based computational saturation scans on 58 surface residues of CTB, including the GM1 binding site, to analyze both ligand-bound and ligand-free structures to decipher mutational effects on protein stability and GM1 affinity. Complimentary experimental results from differential scanning fluorimetry and isothermal titration calorimetry provided melting temperatures and GM1 binding affinities for 40 alanine mutants among these positions. The results showed that CTB can accommodate diverse mutations while maintaining its stability and ligand binding affinity. These mutations could potentially allow modification of the oligosaccharide binding specificity to change its cellular targeting, alter the B-subunit intracellular routing, or impact its shelf-life and in vivo half-life through changes to protein stability. We anticipate that the mutational space maps presented here will serve as a cornerstone for future CTB redesigns, paving the way for the development of innovative biotechnological tools.

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2024

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2021

Collaborators (7)

Michael Webb

Associate Professor

University of Leeds

UNITED KINGDOM
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James F. Ross

University of Leeds

UNITED KINGDOM
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Daniel Ungar

Professor

University of York

UNITED KINGDOM
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Winfried Römer

University of Freiburg

GERMANY
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gerald striedner

University Professor

University of Natural Resources and Life Sciences Vienna

AUSTRIA
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David Fulton

Senior Lecturer

Newcastle University

UNITED KINGDOM
View details

Andrew Macdonald

Professor of Tumour Virology

University of Leeds

UNITED KINGDOM
View details
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