Our Coronavirus Response and Ongoing Research
The Research Complex at Harwell has remained open throughout the Coronavirus pandemic, with our efforts focused on supporting research projects in understanding, and ultimately finding effective strategies to defeat the virus. The research scientists based at the Research Complex have been working tirelessly on areas of vaccines and treatments, using their expertise and our unique facilities to bring the Covid-19 pandemic under control.
Thanks to our unique location and access to world-renowned facilities, we believe in cross-disciplinary research and collaboration across the Harwell Campus that throughout these challenging times has delivered outstanding results.
Ultimately, science will defeat this virus and all of us at Research Complex, and our wide network of collaborators are endeavouring to play our part in the global effort to end the Coronavirus pandemic.
Published papers to date include:
 Mass spectrometric assays reveal discrepancies in inhibition profiles for the SARS-CoV-2 papain-like protease, Lennart Brewitz et al., ChemMedChem (2022).
 A potent SARS-CoV-2 neutralising nanobody shows therapeutics efficacy in the Syrian golden hamster model of COVID-19, Jiandong Huo et al., Nature Communications (2021).
 Bispecific repurposed medicines targeting the viral and immunological arms of COVID-19, Martin A. Redhead et al., Scientific Reports (2021).
 Mass spectrometry reveals potential of β-lactams as SARS-CoV-2 Mpro inhibitors, Tika R. Malla et al., Chemical Communications (2021).
 A super-potent tetramerized ACE2 protein displays enhanced neutralization of SARS-CoV-2 virus infection, Ani Miller et al., Scientific Reports (2021).
 Correlative multi-scale cryo-imaging unveils SARS-CoV-2 assembly and egress, Luiza Mendonça et al., Nature Communications (2021).
 The use of nanobodies in a sensitive ELISA test for SARS-CoV-2 Spike 1 protein, Georgina C. Girt et al., Royal Society Open Science (2021).
 A COVID-19 vaccine candidate using SpyCatcher multimerization of the SARS-CoV-2 spike protein receptor-binding domain induces potent neutralising antibody responses, Tiong Kit Tan et al., Nature Communications (2021).
 Neutralizing nanobodies bind SARS-CoV-2 spike RBD and block interaction with ACE2, Jiangdong Huo et al. Nature Structural and Molecular Biology (2020).
 Structural basis for the neutralization of SARS-CoV-2 by an antibody from a convalescent patient, Daming Zhou et al. Nature Structural and Molecular Biology (2020).
 Fragment Binding to the Nsp3 Macrodomain of SARS-CoV-2 Identified Through Crystallographic Screening and Computational Docking, Marion Schuller et al., bioXriv (2020).
 Neutralization of SARS-CoV-2 by Destruction of the Prefusion Spike, Jiandong Huo et al., Cell Host & Microbe (2020).
 Evaluation of the immunogenicity of prime-boost vaccination with the replication-deficient viral vectored COVID-19 vaccine candidate ChAdOx1 nCoV-19, Simon P. Graham et al., npj Vaccines (2021).
Ongoing research with our collaborators includes the Rosalind Franklin Institute and Protein Production UK on isolating nanobodies – a type of antibody, which can bind to the ‘spike’ protein on the surface of the virus. There is current work with the Electron Bio-Imaging Centre (eBIC) and the Diamond Light Source on understanding virus host cell interactions using the Central Laser Facillity’s (CLF) Octopus Bio-Imaging Facility hosted at Research Complex. In addition, the CLF put out a unique worldwide open call to the CLF’s Octopus Bio-imaging Facility for work into Covid-19. Diamond Light Source researchers in collaboration with the University of Oxford and the Rosalind Franklin Institute have been working on the receptor binding domain of spike protein, polymerase as well as viral proteases. The Research Complex continues to support researchers needing lab access for the rapid access proposals at Diamond to work on Covid-19.
We welcome scientists to continue working with us and make use of our unique facilities. Please check our guidelines before coming to the Research Complex to conduct your work.