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J. Biol. Chem., Vol. 280, Issue 52, 42929-42937, December 30, 2005

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The Needle Component of the Type III Secreton of Shigella Regulates the Activity of the Secretion Apparatus^*

Roma Kenjale1, Justin Wilson2, Sebastian F. Zenk3, Saroj Saurya, Wendy L. Picking, William D. Picking, and Ariel Blocker4

From the Sir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, United Kingdom and the Department of Molecular Biosciences, University of Kansas, Lawrence, Kansas 66045-7534

Gram-negative bacteria commonly interact with eukaryotic host cells by using type III secretion systems (TTSSs or secretons). TTSSs serve to transfer bacterial proteins into host cells. Two translocators, IpaB and IpaC, are first inserted with the aid of IpaD by Shigella into the host cell membrane. Then at least two supplementary effectors of cell invasion, IpaA and IpgD, are transferred into the host cytoplasm. How TTSSs are induced to secrete is unknown, but their activation appears to require direct contact of the external distal tip of the apparatus with the host cell. The extracellular domain of the TTSS is a hollow needle protruding 60 nm beyond the bacterial surface. The monomeric unit of the Shigella flexneri needle, MxiH, forms a superhelical assembly. To probe the role of the needle in the activation of the TTSS for secretion, we examined the structure-function relationship of MxiH by mutagenesis. Most point mutations led to normal needle assembly, but some led to polymerization or possible length control defects. In other mutants, secretion was constitutively turned "on." In a further set, it was "constitutively on" but experimentally "uninducible." Finally, upon induction of secretion, some mutants released only the translocators and not the effectors. Most types of mutants were defective in interactions with host cells. Together, these data indicate that the needle directly controls the activity of the TTSS and suggest that it may be used to "sense" host cells.

Received for publication, August 1, 2005 , and in revised form, October 13, 2005.

^* The laboratory of W. D. P. was supported by Public Health Service Grants AI034428 and RR017708 and the University of Kansas Research Development Fund. The laboratory of A. B. was supported by the Guy G. F. Newton Senior Research Fellowship. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

A. B. dedicates this paper to Kaoru Komoriya and to her own daughter, Miriam Longchamp, born August 21, 2002.

The on-line version of this article (available at http://www.jbc.org) contains supplemental Table S1.

¹ Supported by a Barbara Johnson Bishop Scholarship.

² Supported by a Wellcome Trust Vacation Scholarship.

³ Supported by the Studienstiftung des Deutschen Volkes.

⁴ To whom correspondence should be addressed: Sir William Dunn School of Pathology, University of Oxford, South Parks Rd., OX1 3RE, United Kingdom. Tel.: 44-1865-285-748 (laboratory) or 44-1865-275-541 (office); Fax: 44-1865-275-515; E-mail: ariel.blocker{at}path.ox.ac.uk.

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