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Infection and Immunity, February 2007, p. 565-573, Vol. 75, No. 2
0019-9567/07/$08.00+0     doi:10.1128/IAI.01479-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Enteropathogenic Escherichia coli, Shigella flexneri, and Listeria monocytogenes Recruit a Junctional Protein, Zonula Occludens-1, to Actin Tails and Pedestals ^,

Miyuki Hanajima-Ozawa,¹ Takeshi Matsuzawa,² Aya Fukui,¹ Shigeki Kamitani,¹ Hiroe Ohnishi,¹ Akio Abe,² Yasuhiko Horiguchi,¹ and Masami Miyake^1*

Department of Molecular Bacteriology, Research Institute for Microbial Diseases, Osaka University, 3-1 Yamadaoka, Suita-city, Osaka 565-0871, Japan,¹ Laboratory of Bacterial Infection, Kitasato Institute for Life Sciences, Kitasato University, 5-9-1 Shirokane, Minato-ku, Tokyo 108-8642, Japan²

Received 15 September 2006/ Returned for modification 4 November 2006/ Accepted 14 November 2006

Enteropathogenic Escherichia coli, Shigella flexneri, and Listeria monocytogenes induce localized actin polymerization at the cytoplasmic face of the plasma membrane or within the host cytoplasm, creating unique actin-rich structures termed pedestals or actin tails. The process is known to be mediated by the actin-related protein 2 and 3 (Arp2/3) complex, which in these cases acts downstream of neural Wiskott-Aldrich syndrome protein (N-WASP) or of a listerial functional homolog of WASP family proteins. Here, we show that zonula occludens-1 (ZO-1), a protein in the tight junctions of polarized epithelial cells, is recruited to actin tails and pedestals. Immunocytochemical analysis revealed that ZO-1 was stained most in the distal part of the actin-rich structures, and the incorporation was mediated by the proline-rich region of the ZO-1 molecule. The direct clustering of membrane-targeted Nck, which is known to activate the N-WASP-Arp2/3 pathway, triggered the formation of the ZO-1-associated actin tails. The results suggest that the activation of the Arp2/3 complex downstream of N-WASP or a WASP-related molecule is a key to the formation of the particular actin-rich structures that bind with ZO-1. We propose that an analysis of the recruitment on a molecular basis will lead to an understanding of how ZO-1 recognizes a distinctive actin-rich structure under pathophysiological conditions.

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* Corresponding author. Mailing address: Department of Molecular Bacteriology, Research Institute for Microbial Diseases, Osaka University, 3-1 Yamadaoka, Suita-city, Osaka 565-0871, Japan. Phone: 81-6-6879-8285. Fax: 81-6-6879-8283. E-mail: mami{at}biken.osaka-u.ac.jp.

Published ahead of print on 21 November 2006.

Editor: A. Camilli

Supplemental material for this article may be found at http://iai.asm.org/.

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Infection and Immunity, February 2007, p. 565-573, Vol. 75, No. 2
0019-9567/07/$08.00+0     doi:10.1128/IAI.01479-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

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