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J. Biol. Chem., Vol. 279, Issue 45, 46896-46906, November 5, 2004

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Conservation of the Biochemical Properties of IncA from Chlamydia trachomatis and Chlamydia caviae

OLIGOMERIZATION OF IncA MEDIATES INTERACTION BETWEEN FACING MEMBRANES^*

Cédric Delevoye, Michael Nilges¶, Alice Dautry-Varsat, and Agathe Subtil||

From the Unité de Biologie des Interactions Cellulaires and the ^¶Unité de Bio-Informatique Structurale, Institut Pasteur, CNRS URA 2582 and 2185, 25 rue du Docteur Roux, 75015 Paris, France

The developmental cycle of Chlamydiaceae occurs in a membrane compartment called an inclusion. IncA is a member of a family of proteins synthesized and secreted onto the inclusion membrane by bacteria. IncA proteins from different species of Chlamydiaceae show little sequence similarity. We report that the biochemical properties of Chlamydia trachomatis and Chlamydia caviae are conserved. Both proteins self-associate to form multimers. When artificially expressed by the host cell, they localize to the endoplasmic reticulum. Strikingly, heterologous expression of IncA in the endoplasmic reticulum completely inhibits concomitant inclusion development. Using truncated forms of IncA from C. caviae, we show that expression of the C-terminal cytoplasmic domain of the protein at the surface of the endoplasmic reticulum is sufficient to disrupt the bacterial developmental cycle. On the other hand, development of a C. trachomatis strain that does not express IncA is not inhibited by artificial IncA expression, showing that the disruptive effect observed with the wild-type strain requires direct interactions between IncA molecules at the inclusion and on the endoplasmic reticulum. Finally, we modeled IncA tetramers in parallel four helix bundles based on the structure of the SNARE complex, a conserved structure involved in membrane fusion in eukaryotic cells. Both C. trachomatis and C. caviae IncA tetramers were highly stable in this model. In conclusion, we show that the property of IncA proteins to assemble into multimeric structures is conserved between chlamydial species, and we propose that these proteins may have co-evolved with the SNARE machinery for a role in membrane fusion.

Received for publication, June 28, 2004 , and in revised form, August 5, 2004.

^* This work was supported by Action Concertée Incitative Biologie Cellulaire, Moléculaire et Structurale. 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.

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

Supported by an Allocation de Recherche du Ministère de l'Enseignement Supérieur et de la Recherche.

^|| To whom correspondence should be addressed. Tel.: 33-1-40-61-30-49; Fax: 33-1-40-61-32-38; E-mail: asubtil{at}pasteur.fr.

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