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Many Gram-negative pathogens translocate virulence proteins directly into host cells using a type III secretion system. This complex secretion machinery is composed of approximately 25 different proteins that assemble to span both bacterial membranes, and contact the host cell to form a direct channel between the bacterial and host cell cytoplasms. Assembly of the system and efficient secretion of virulence proteins through this apparatus require specific chaperones. Although the machinery is morphologically conserved among all bacteria, the secreted proteins vary widely and are responsible for the range of diseases caused by bacterial pathogens. Recent structures have given insights into important chaperone and effector proteins, as well as revealing the first atomic structures of portions of the secretion machinery itself.

Original publication

DOI

10.1016/j.sbi.2005.10.007

Type

Journal article

Journal

Curr Opin Struct Biol

Publication Date

12/2005

Volume

15

Pages

700 - 707

Keywords

Bacterial Proteins, Gram-Negative Bacteria, Models, Molecular, Molecular Chaperones, Protein Conformation, Protein Transport