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Infection and Immunity, September 2008, p. 4282-4289, Vol. 76, No. 9
0019-9567/08/$08.00+0     doi:10.1128/IAI.01738-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Identification of Two Translocon Proteins of Vibrio parahaemolyticus Type III Secretion System 2

Department of Bacterial Infections,¹ International Research Center for Infectious Diseases, Research Institute for Microbial Diseases, Osaka University, 3-1 Yamadaoka, Suita, Osaka 565-0871, Japan,² Department of Food Science and Technology, College of Ocean Science and Technology, Kunsan National University, San 68, Miryong-dong, Kusan, Jeollabuk-do, 573-701, Korea,³ Laboratorio Weinmann LTDA, Setor de Microbiologia e Biologia Molecular, Porto Alegre, RS, Brazil⁴

Received 28 December 2007/ Returned for modification 4 February 2008/ Accepted 21 May 2008

The type III secretion system (T3SS) translocon complex is composed of several associated proteins, which form a translocation channel through the host cell plasma membrane. These proteins are key molecules that are involved in the pathogenicity of many T3SS-positive bacteria, because they are necessary to deliver effector proteins into host cells. A T3SS designated T3SS2 of Vibrio parahaemolyticus is thought to be related to the enterotoxicity of this bacterium in humans, but the effector translocation mechanism of T3SS2 is unclear because there is only one gene (the VPA1362 gene) in the T3SS2 region that is homologous to other translocon protein genes. It is also not known whether the VPA1362 protein is functional in the translocon of T3SS2 or whether it is sufficient to form the translocation channel of T3SS2. In this study, we identified both VPA1362 (designated VopB2) and VPA1361 (designated VopD2) as T3SS2-dependent secretion proteins. Functional analysis of these proteins showed that they are essential for T3SS2-dependent cytotoxicity, for the translocation of one of the T3SS2 effector proteins (VopT), and for the contact-dependent activity of pore formation in infected cells in vitro. Their targeting to the host cell membrane depends on T3SS2, and furthermore, they are necessary for T3SS2-dependent enterotoxicity in vivo. These results indicate that VopB2 and VopD2 act as translocon proteins of V. parahaemolyticus T3SS2 and hence have a critical role in the T3SS2-dependent enterotoxicity of this bacterium.

Published ahead of print on 9 June 2008.

Editor: J. B. Bliska