Chaperone binding - two better than one?

Fabulous new work is out today by the talented postdoctoral fellow, Dr. Dustin Little. Pathogenic bacteria use a type III secretion system to inject bacterial effector proteins into host cells that manipulate host cell functions to promote bacterial infection. These effectors need chaperone proteins in the bacterial cell that control effector expression and timing of release. By solving the crystal structure of a multi-cargo chaperone, CesT, in complex with a fragment of the effector protein Tir, Dustin discovered a second chaperone binding site on Tir that is involved in effector secretion hierarchy in pathogenic E. coli. Lots of other cool findings in the paper too. A tour de force!