OxTalks will soon move to the new Halo platform and will become 'Oxford Events.' There will be a need for an OxTalks freeze. This was previously planned for Friday 14th November – a new date will be shared as soon as it is available (full details will be available on the Staff Gateway).
In the meantime, the OxTalks site will remain active and events will continue to be published.
If staff have any questions about the Oxford Events launch, please contact halo@digital.ox.ac.uk
Dr Salgado is a structural biologist and biochemist interested in proteins associated with pathogenicity and disease. After a PhD at STRUBI, Oxford, and postdoctoral experience at Birkbeck and Imperial College London, she established and leads the C. difficile Structural Microbiology group at Newcastle University.
Her lab focuses on detailed structural and functional characterisation of proteins involved in key pathogenicity pathways in a major human pathogen, Clostridioides difficile, now the most prevalent hospital acquired infection in the UK. Combining biochemistry, microbiology and structural approaches, they study C. difficile spores and surface proteins.
C. difficile’s armour – the S-layer
Like many bacteria, C. difficile has an outside para-crystalline layer called S-layer that is presumed to act as a protective armour and has been implicated in virulence, host interaction and immune activation. Recently, they determined the structure of SlpA, the main protein in the S-layer of C. difficile, and a model for S-layer assembly. This work provides a basis for development of C. difficile-specific therapeutics.
Dormancy – sporulation engulfment machinery
Work in the Salgado lab has identified two essential proteins involved in the early stages of sporulation. They have also contributed to elucidating details of the engulfment mechanism (Dembek et al., 2018) and start defining the complex machinery involved in this process, which was termed the engulfasome (Kelly and Salgado, 2019).
Current work focuses on further elucidating the molecular details of the engulfasome machinery.