IAI FigSearch
Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
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 arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Bourzac, K. M.
Right arrow Articles by Guillemin, K.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Bourzac, K. M.
Right arrow Articles by Guillemin, K.
Infection and Immunity, May 2006, p. 2537-2543, Vol. 74, No. 5
0019-9567/06/$08.00+0     doi:10.1128/IAI.74.5.2537-2543.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

The Helicobacter pylori cag Pathogenicity Island Protein CagN Is a Bacterial Membrane-Associated Protein That Is Processed at Its C Terminus

Kevin M. Bourzac,1 Laura A. Satkamp,2 and Karen Guillemin1*

Institute of Molecular Biology, University of Oregon, Eugene, Oregon,1 Department of Biochemistry and Molecular Biology, The University of Chicago, Chicago, Illinois2

Received 7 December 2005/ Returned for modification 13 January 2006/ Accepted 9 February 2006

Helicobacter pylori infects nearly half the world's population and is associated with a spectrum of gastric maladies. Infections with cytotoxin-associated gene pathogenicity island (cag PAI)-containing strains are associated with an increased risk for gastric cancer. The cag PAI contains genes encoding a type IV secretion system (T4SS) and a delivered effector, CagA, that becomes tyrosine phosphorylated upon delivery into host cells and initiates changes in cell signaling. Although some cag PAI genes have been shown to be required for CagA delivery, a subset of which are homologues of T4SS genes from Agrobacterium tumefaciens, the majority have no known function or homologues. We have performed a detailed investigation of one such cag PAI protein, CagN, which is encoded by the gene HP0538. Our results show that CagN is not delivered into host cells and instead is associated with the bacterial membrane. We demonstrate that CagN is cleaved at its C terminus by a mechanism that is independent of other cag PAI proteins. Finally, we show that a {Delta}cagN mutant is not impaired in its ability to deliver CagA to gastric epithelial cells and initiate cell elongation.


* Corresponding author. Mailing address: Institute of Molecular Biology, University of Oregon, Eugene, OR 97403. Phone: (541) 346-5360. Fax: (541) 346-5891. E-mail: guillemin{at}molbio.uoregon.edu.

Editor: D. L. Burns


Infection and Immunity, May 2006, p. 2537-2543, Vol. 74, No. 5
0019-9567/06/$08.00+0     doi:10.1128/IAI.74.5.2537-2543.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.




This article has been cited by other articles:




Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
J. Bacteriol. J. Virol. Eukaryot. Cell
Microbiol. Mol. Biol. Rev. Clin. Vaccine Immunol. All ASM Journals

Copyright © 2006 by the American Society for Microbiology. All rights reserved.