|Automated construction and screening of protein expression|
|Automated imaging of protein crystallization experiments|
Professor of Molecular Biology
Protein Production UK (PPUK) is being developed as a programme for protein engineering and production as part of the Structural Biology theme of the Rosalind Franklin Institute (RFI). PPUK aims to develop new and innovative methods and to work in partnership with academic groups and industry to enable uptake of the technology.
PPUK has an established pipeline for protein production based on the technology developed by the Oxford Protein Production Facility (OPPF), involving construction of multi-purpose vectors (e.g. for producing complexes, and membrane proteins), high-throughput expression screening in different cell hosts (microbial, insect and mammalian cells) combined with scale-up to multi-litre culture volumes and downstream processing. New technology platforms that are under development include production of single-domain antibodies (nanobodies) for the stabilisation of membrane proteins and macro-molecular complexes for analysis by cryo-EM.
We are using nanobody technology to identify binding agents with diagnostic and therapeutic potential for the treatment of respiratory viral diseases.
A COVID-19 vaccine candidate using SpyCatcher multimerization of the SARS-CoV-2 spike protein receptor-binding domain induces potent neutralising antibody responses
Tan TK. et al, (2021), Nature Communications, 12
Structural Biology of Nanobodies against the Spike Protein of SARS-CoV-2
Tang Q. et al, (2021), Viruses, 13, 2214 - 2214
Cryo-EM structure of PepT2 reveals structural basis for proton-coupled peptide and prodrug transport in mammals
Parker JL. et al, (2021), Science Advances, 7, eabh3355 - eabh3355
Author Correction: Neutralizing nanobodies bind SARS-CoV-2 spike RBD and block interaction with ACE2.
Huo J. et al, (2021), Nature structural & molecular biology
The structure of nontypeable Haemophilus influenzae SapA in a closed conformation reveals a constricted ligand-binding cavity and a novel RNA binding motif.
Lukacik P. et al, (2021), PloS one, 16