Self-chaperoning of the Type III Secretion System Needle Tip Proteins IpaD and BipD
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Issue Date
2007-02-09Author
Johnson, Steven
Roversi, Pietro
Espina, Marianela
Olive, Andrew J.
Deane, Janet E.
Birket, Susan
Field, Terry
Picking, William D.
Blocker, Ariel J.
Galyov, Edouard E.
Picking, Wendy Lynn
Lea, Susan M.
Publisher
American Society for Biochemistry and Molecular Biology
Type
Article
Article Version
Scholarly/refereed, publisher version
Rights
This research was originally published in Journal of Biological Chemistry. Steven Johnson, Pietro Roversi, Marianela Espina, Andrew Olive, Janet E. Deane, Susan Birket, Terry Field, William D. Picking, Ariel J. Blocker, Edouard E. Galyov, Wendy L. Picking and Susan M. Lea. Self-Chaperoning of the Type III Secretion System needle tip proteins IpaD and BipD. Journal of Biological Chemistry. 2007; 282, 4035-4044. © the American Society for Biochemistry and Molecular Biology.
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Show full item recordAbstract
Bacteria expressing type III secretion systems (T3SS) have been responsible for the deaths of millions worldwide, acting as key virulence elements in diseases ranging from plague to typhoid fever. The T3SS is composed of a basal body, which traverses both bacterial membranes, and an external needle through which effector proteins are secreted. We report multiple crystal structures of two proteins that sit at the tip of the needle and are essential for virulence; IpaD from Shigella flexneri and BipD from Burkholderia pseudomallei. The structures reveal that the N-terminal domains of the molecules are intra-molecular chaperones that prevent premature oligomerization, as well as sharing structural homology with proteins involved in eukaryotic actin rearrangement. Crystal packing has allowed us to construct a model for the tip complex that is supported by mutations designed using the structure.
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Citation
Johnson, S., Roversi, P., Espina, M., Olive, A., Deane, J. E., Birket, S., … Lea, S. M. (2007). Self-Chaperoning of the Type III Secretion System needle tip proteins IpaD and BipD. The Journal of Biological Chemistry, 282(6), 4035–4044. http://doi.org/10.1074/jbc.M607945200
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