Advertisement
JBC

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


Originally published In Press as doi:10.1074/jbc.M101882200 on June 20, 2001

J. Biol. Chem., Vol. 276, Issue 34, 32071-32079, August 24, 2001
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
276/34/32071    most recent
M101882200v1
Right arrow Submit a Letter to Editor
Right arrow Alert me when this article is cited
Right arrow Alert me when eLetters are posted
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowRequest Permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Toyotome, T.
Right arrow Articles by Sasakawa, C.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Toyotome, T.
Right arrow Articles by Sasakawa, C.
Social Bookmarking
 Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Shigella Protein IpaH9.8 Is Secreted from Bacteria within Mammalian Cells and Transported to the Nucleus*

Takahito ToyotomeDagger , Toshihiko SuzukiDagger , Asaomi KuwaeDagger , Takashi Nonaka§, Hiroyuki Fukuda§, Shinobu Imajoh-Ohmi§, Toshihiko Toyofuku, Masatsugu Hori, and Chihiro SasakawaDagger ||

From the Dagger  Division of Bacterial Infection, Department of Microbiology and Immunology and the § Division of Cell Biology and Biochemistry, Department of Basic Medical Sciences, Institute of Medical Science, University of Tokyo, Minato-ku, Tokyo 108-8639 and the  Department of Internal Medicine and Therapeutics, Osaka University Graduate School of Medicine, Suita, Osaka 565-0871, Japan

Various pathogenic bacteria such as Shigella deliver effector proteins into mammalian cells via the type III secretion system. The delivered Shigella effectors have been shown to variously affect host functions required for efficient bacterial internalization into the cells. In the present study, we investigated the IpaH proteins for their ability to be secreted via the type III secretion system and their fate in mammalian cells. Upon incubation in a medium containing Congo red, the bacteria secrete IpaH into the medium, but secretion of IpaH occurs later than that of IpaBCD. Immunofluorescence microscopy indicated that IpaH9.8 is secreted from intracellular bacteria and transported into the nucleus. On microinjection of the protein, intracellular IpaH9.8 is accumulated at one place around the nucleus and transported into the nucleus. This movement seems to be dependent on the microtubule network, since nuclear accumulation of IpaH9.8 is inhibited in cells treated with microtubule-destabilizing agents. In nuclear import assay, IpaH9.8 was efficiently transported into the nucleus, which was completely blocked by treatment with wheat germ agglutinin. The nuclear transport of IpaH9.8 does not depend on host cytosolic factors but is partially dependent on ATP/GTP, suggesting that, like beta -catenin, IpaH9.8 secreted from intracellular Shigella can be transported into the nucleus.


* This work was supported by the Research for the Future program of the Japan Society for the Promotion of Science and a grant-in-aid for Scientific Research from the Japanese Ministry of Education, Science, Sports, and Culture.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

|| To whom correspondence should be addressed: Dept. of Microbiology and Immunology, Institute of Medical Science, University of Tokyo, Minato-ku, Tokyo 108-8639, Japan. Tel.: 81-3-449-5252; Fax: 81-3-5449-5405; E-mail: sasakawa@ims.u-tokyo.ac.jp.


Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
Clin. Microbiol. Rev.Home page
G. N. Schroeder and H. Hilbi
Molecular Pathogenesis of Shigella spp.: Controlling Host Cell Signaling, Invasion, and Death by Type III Secretion
Clin. Microbiol. Rev., January 1, 2008; 21(1): 134 - 156.
[Abstract] [Full Text] [PDF]


Home page
Infect. Immun.Home page
D. V. Zurawski, C. Mitsuhata, K. L. Mumy, B. A. McCormick, and A. T. Maurelli
OspF and OspC1 Are Shigella flexneri Type III Secretion System Effectors That Are Required for Postinvasion Aspects of Virulence.
Infect. Immun., October 1, 2006; 74(10): 5964 - 5976.
[Abstract] [Full Text] [PDF]


Home page
Infect. Immun.Home page
M. Miura, J. Terajima, H. Izumiya, J. Mitobe, T. Komano, and H. Watanabe
OspE2 of Shigella sonnei Is Required for the Maintenance of Cell Architecture of Bacterium-Infected Cells.
Infect. Immun., May 1, 2006; 74(5): 2587 - 2595.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
A. Kuwae, T. Matsuzawa, N. Ishikawa, H. Abe, T. Nonaka, H. Fukuda, S. Imajoh-Ohmi, and A. Abe
BopC Is a Novel Type III Effector Secreted by Bordetella bronchiseptica and Has a Critical Role in Type III-dependent Necrotic Cell Death
J. Biol. Chem., March 10, 2006; 281(10): 6589 - 6600.
[Abstract] [Full Text] [PDF]


Home page
Nucleic Acids ResHome page
F. Yang, J. Yang, X. Zhang, L. Chen, Y. Jiang, Y. Yan, X. Tang, J. Wang, Z. Xiong, J. Dong, et al.
Genome dynamics and diversity of Shigella species, the etiologic agents of bacillary dysentery
Nucleic Acids Res., November 7, 2005; 33(19): 6445 - 6458.
[Abstract] [Full Text] [PDF]


Home page
Infect. Immun.Home page
C. Sabet, M. Lecuit, D. Cabanes, P. Cossart, and H. Bierne
LPXTG Protein InlJ, a Newly Identified Internalin Involved in Listeria monocytogenes Virulence
Infect. Immun., October 1, 2005; 73(10): 6912 - 6922.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
T. Nagai, A. Abe, and C. Sasakawa
Targeting of Enteropathogenic Escherichia coli EspF to Host Mitochondria Is Essential for Bacterial Pathogenesis: CRITICAL ROLE OF THE 16TH LEUCINE RESIDUE IN EspF
J. Biol. Chem., January 28, 2005; 280(4): 2998 - 3011.
[Abstract] [Full Text] [PDF]


Home page
Infect. Immun.Home page
S. Lucchini, H. Liu, Q. Jin, J. C. D. Hinton, and J. Yu
Transcriptional Adaptation of Shigella flexneri during Infection of Macrophages and Epithelial Cells: Insights into the Strategies of a Cytosolic Bacterial Pathogen
Infect. Immun., January 1, 2005; 73(1): 88 - 102.
[Abstract] [Full Text] [PDF]


Home page
MicrobiologyHome page
F. Dziva, P. M. van Diemen, M. P. Stevens, A. J. Smith, and T. S. Wallis
Identification of Escherichia coli O157 : H7 genes influencing colonization of the bovine gastrointestinal tract using signature-tagged mutagenesis
Microbiology, November 1, 2004; 150(11): 3631 - 3645.
[Abstract] [Full Text] [PDF]


Home page
Infect. Immun.Home page
A. Haraga and S. I. Miller
A Salmonella enterica Serovar Typhimurium Translocated Leucine-Rich Repeat Effector Protein Inhibits NF-{kappa}B-Dependent Gene Expression
Infect. Immun., July 1, 2003; 71(7): 4052 - 4058.
[Abstract] [Full Text] [PDF]


Home page
Infect. Immun.Home page
J. Wei, M. B. Goldberg, V. Burland, M. M. Venkatesan, W. Deng, G. Fournier, G. F. Mayhew, G. Plunkett III, D. J. Rose, A. Darling, et al.
Complete Genome Sequence and Comparative Genomics of Shigella flexneri Serotype 2a Strain 2457T
Infect. Immun., May 1, 2003; 71(5): 2775 - 2786.
[Abstract] [Full Text] [PDF]


Home page
Infect. Immun.Home page
E. Skrzypek, T. Myers-Morales, S. W. Whiteheart, and S. C. Straley
Application of a Saccharomyces cerevisiae Model To Study Requirements for Trafficking of Yersinia pestis YopM in Eucaryotic Cells
Infect. Immun., February 1, 2003; 71(2): 937 - 947.
[Abstract] [Full Text] [PDF]


Home page
Nucleic Acids ResHome page
Q. Jin, Z. Yuan, J. Xu, Y. Wang, Y. Shen, W. Lu, J. Wang, H. Liu, J. Yang, F. Yang, et al.
Genome sequence of Shigella flexneri 2a: insights into pathogenicity through comparison with genomes of Escherichia coli K12 and O157
Nucleic Acids Res., October 15, 2002; 30(20): 4432 - 4441.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2001 by the American Society for Biochemistry and Molecular Biology.
Advertisement
spacer
Advertisement
Advertisement