Speaker
Description
Many pathogenic bacteria secreted effector proteins directly into the eukaryotic host cell cytoplasm through their type III secretion system (T3SS), where they exert a number of effects that enable the pathogen to survive and to escape the host defense mechanisms. Lately, we could identify the Yersinia effector YopM as well as Salmonella-derived SspH1 as the first bacteria-derived cell-penetrating effectors (CPEs) that are also able to translocate into host cells in a T3SS-independent manner. In addition to both YopM and SspH1 which belong to the bacterial effectors of the LPX subtype of leucine-rich repeat (LRR) proteins, the Salmonella proteins SspH2 and SlrP as well as different IpaH proteins of Shigella are also part of the LPX family.
Here, we investigated both the cell-penetrating abilities and the functionality of different recombinantly expressed LPX effector proteins as novel ubiquitin E3 ligases (NEL).
