Transmembrane domains of type III-secreted proteins affect bacterial-host interactions in enteropathogenic E. coli.

ABSTRACT: Many bacterial pathogens utilize a specialized secretion system, termed type III secretion system (T3SS), to translocate effector proteins into host cells and establish bacterial infection. The T3SS is anchored within the bacterial membranes and contains a long needle/filament that extends toward the host-cell and forms, at its distal end, a pore complex within the host membrane. The T3SS pore complex consists of two bacterial proteins, termed SctB and SctE, which have conflicting targeting indications; a signal sequence that targets to secretion to the extracellular environment via the T3SS, and transmembrane domains (TMDs) that target to membrane localization. In this study, we investigate whether the TMD sequences of SctB and SctE have special features that differentiate them from class

SUBMITTER: Gershberg J 

PROVIDER: S-EPMC7993127 | biostudies-literature | 2021 Dec

REPOSITORIES: biostudies-literature