Oxford Events, the new replacement for OxTalks, will launch on 16th March. From now until the launch of Oxford Events, new events cannot be published or edited on OxTalks while all existing records are migrated to the new platform. The existing OxTalks site will remain available to view during this period.
From 16th, Oxford Events will launch on a new website: events.ox.ac.uk, and event submissions will resume. You will need a Halo login to submit events. Full details are available on the Staff Gateway.
Commensal and pathogenic bacteria rely on surface-associated adhesins for colonization, pathogenesis, and persistence within host tissues. Until recently, adhesins were known only to interact with host targets through non-covalent interactions. We have identified a large class of surface proteins composed of domains containing intramolecular cross-links between amino acid side-chains. These TIE (thioester, isopeptide, ester) proteins are exceedingly prevalent and diverse in Gram-positive bacteria, and can be likened to “chemical harpoons”, covalently anchoring bacteria to their targets on host cell surfaces. TIE proteins may therefore have evolved to mediate fast, mechanically persistent binding of bacteria to host tissues. Insights yielded by the combined efforts of structural and cell biology support covalent bacteria-host binding as a new molecular principle in host-microbe interaction, and represents an unexploited target to treat bacterial infection.
