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Journal of Bacteriology, June 2004, p. 3806-3813, Vol. 186, No. 12
0021-9193/04/$08.00+0     DOI: 10.1128/JB.186.12.3806-3813.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

The Type III Secreted Protein BopD in Bordetella bronchiseptica Is Complexed with BopB for Pore Formation on the Host Plasma Membrane

Hisashi Nogawa,1,{dagger} Asaomi Kuwae,1,2,{dagger} Takeshi Matsuzawa,1,2 and Akio Abe1,2*

Laboratory of Bacterial Infection, Kitasato Institute for Life Sciences, Kitasato University, Minato-ku, Tokyo 108-8641,1 The Kitasato Institute, Minato-ku, Tokyo 108-8642, Japan2

Received 23 October 2003/ Accepted 1 March 2004

The cytotoxicity of Bordetella bronchiseptica to infected cells is known to be dependent on a B. bronchiseptica type III secretion system. Although BopB, BopN, BopD, and Bsp22 have been identified as type III secreted proteins, these proteins remain to be characterized. In this study, in order to clarify the function of BopD during Bordetella infection, a BopD mutant was generated. Although secretion of BopD into the culture supernatant was completely abolished by the bopD mutation, the secretion of other type III secreted proteins was not affected by this mutation. It has been reported that severe cytotoxicity, including cell detachment from the substrata, and release of lactate dehydrogenase (LDH) into the supernatant are induced in L2 cells by wild-type B. bronchiseptica infection, and these phenotypes are dependent on the type III secretion system. In contrast, neither cell detachment nor LDH release was induced in L2 cells infected with the BopD mutant. Furthermore, the hemolytic activity of the BopD mutant was greatly impaired compared with that of the wild-type strain. On the basis of the results of coimmunoprecipitation assays with anti-BopB antibodies, we conclude that BopD has the ability to associate with BopB. Finally, we show that the BopD-BopB complex is responsible for the pore formation in the host plasma membrane that functions as the conduit for the transition of effector proteins into host cells.

* Corresponding author. Mailing address: Laboratory of Bacterial Infection, Kitasato Institute for Life Sciences, Kitasato University, 5-9-1 Shirokane, Minato-ku, Tokyo 108-8641, Japan. Phone: 81-3-5791-6123. Fax: 81-3-5791-6125. E-mail: abe{at}lisci.kitasato-u.ac.jp.

{dagger} H. Nogawa and A. Kuwae contributed equally to this work.

Journal of Bacteriology, June 2004, p. 3806-3813, Vol. 186, No. 12
0021-9193/04/$08.00+0     DOI: 10.1128/JB.186.12.3806-3813.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



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