Abstract 2149 Biochemical and biophysical characterization of Eag protein chaperones in complex with effector transmembrane domains

The ability to secrete proteins is an essential component of bacterial communication and virulence. The type VI secretion system (T6SS) is a dynamic protein nanomachine that forcibly secretes toxic effectors into prey-cells in a contact-dependent manner. Many T6SS effectors possess transmembrane domains (TMDs) in their N-termini which are hypothesized to catalyze the transition of the toxin across the inner-membrane of a prey-cell. For proper loading onto the T6SS prior to secretion, TMD-containing effectors require assistance from Effector Associated Gene (Eag) chaperones.