David Albesa-Jové

This study identifies Tke5, a novel Pseudomonas putida toxin that depolarizes membranes and kills plant pathogens through a unique pore-forming mechanism.

The paper determines the cryo-EM structure of the Tap3-Tke5 complex, revealing the mechanism of adaptor-effector binding for a pore-forming toxin family.

This study identifies Tse4 as a pore-forming toxin that forms ion-selective channels, linking membrane depolarisation to K+ efflux in competing bacteria.

The paper identifies WHIX as a T6SS secretion domain that enables the delivery of effectors with one or two toxic domains, requiring specific immunity proteins to counteract their toxicity.