A Gatekeeper Chaperone Complex Directs Translocator Secretion during Type Three Secretion

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Type Three Secretion Systems (T3SS) are essential virulence factors found in many pathogenic Gram-negative bacteria. These machines aid infection by delivering bacterial proteins into host cells where these proteins modulate host processes and help establish a niche for the bacteria. Protein delivery occurs in a highly regulated manner in which proteins involved in early steps in infection, or necessary to build the secretion conduit, are typically secreted before other substrates, a phenomenon termed secretion hierarchy. This study presents the structure of a molecular complex that physically links one class of early substrates, components of the secretion pore termed translocators, to a gatekeeper protein, a protein that has been implicated in the secretion hierarchy. Disruption of this interaction in Shigella disrupts the secretion of translocators, while supporting increased secretion of effectors, resulting in phenotypes indistinguishable from a gatekeeper deletion, and leading to the conclusion that a gatekeeper-chaperone-translocator complex is a critical component of the T3SS.

Vyšlo v časopise: A Gatekeeper Chaperone Complex Directs Translocator Secretion during Type Three Secretion. PLoS Pathog 10(11): e32767. doi:10.1371/journal.ppat.1004498
Kategorie: Research Article
prolekare.web.journal.doi_sk: https://doi.org/10.1371/journal.ppat.1004498

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