AJP - GI Watch the video to learn how APS reaches out to developing nations.
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Am J Physiol Gastrointest Liver Physiol 275: G681-G688, 1998;
0193-1857/98 $5.00
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
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
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Sommi, P.
Right arrow Articles by Ventura, U.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Sommi, P.
Right arrow Articles by Ventura, U.
Vol. 275, Issue 4, G681-G688, October 1998

Persistence of Helicobacter pylori VacA toxin and vacuolating potential in cultured gastric epithelial cells

Patrizia Sommi1, Vittorio Ricci1, Roberto Fiocca2, Vittorio Necchi2, Marco Romano3, John L. Telford4, Enrico Solcia2, and Ulderico Ventura1

1 Institute of Human Physiology and 2 Department of Human Pathology, University of Pavia and Istituto Ricovero e Cura a Carrattere Scientifico Policlinico San Matteo, 27100 Pavia; 3 Department of Medicine-Gastroenterology II, University of Naples, 80131 Naples; and 4 Immunological Research Institute of Siena-Chiron Vaccine, 53100 Siena, Italy

The vacuolating toxin A (VacA) is one of the most important virulence factors in Helicobacter pylori-induced damage to human gastric epithelium. Using human gastric epithelial cells in culture and broth culture filtrate from a VacA-producing H. pylori strain, we studied 1) the delivery of VacA to cells, 2) the localization and fate of internalized toxin, and 3) the persistence of toxin inside the cell. The investigative techniques used were neutral red dye uptake, ultrastructural immunocytochemistry, quantitative immunofluorescence, and immunoblotting. We found that VacA 1) is delivered to cells in both free and membrane-bound form (i.e., as vesicles formed by the bacterial outer membrane), 2) localizes inside the endosomal-lysosomal compartment, in both free and membrane-bound form, 3) persists within the cell for at least 72 h, without loss of vacuolating power, which, however, becomes evident only when NH4Cl is added, and 4) generally does not degrade into fragments smaller than ~90 kDa. Our findings suggest that, while accumulating inside the endosomal-lysosomal compartment, a large amount of VacA avoids the main lysosomal degradative processes and retains its apparent molecular integrity.

outer membrane vesicles; VacA internalization; VacA metabolism; VacA immunocytochemistry


This article has been cited by other articles:


Home page
 Cancer Res.Home page
T. L. Cover, U. S. Krishna, D. A. Israel, and R. M. Peek Jr.
Induction of Gastric Epithelial Cell Apoptosis by Helicobacter pylori Vacuolating Cytotoxin
Cancer Res., March 1, 2003; 63(5): 951 - 957.
[Abstract] [Full Text] [PDF]

Home page
 Am. J. Physiol. Gastrointest. Liver Physiol.Home page
V. Ricci, B. A. Manzo, C. Tuccillo, P. Boquet, U. Ventura, M. Romano, and R. Zarrilli
NSAIDs counteract H. pylori VacA toxin-induced cell vacuolation in MKN 28 gastric mucosal cells
Am J Physiol Gastrointest Liver Physiol, September 1, 2002; 283(3): G511 - G520.
[Abstract] [Full Text] [PDF]

Home page
 Infect. Immun.Home page
H. K. Patel, D. C. Willhite, R. M. Patel, D. Ye, C. L. Williams, E. M. Torres, K. B. Marty, R. A. MacDonald, and S. R. Blanke
Plasma Membrane Cholesterol Modulates Cellular Vacuolation Induced by the Helicobacter pylori Vacuolating Cytotoxin
Infect. Immun., August 1, 2002; 70(8): 4112 - 4123.
[Abstract] [Full Text] [PDF]

Home page
 Infect. Immun.Home page
D. C. Willhite, D. Ye, and S. R. Blanke
Fluorescence Resonance Energy Transfer Microscopy of the Helicobacter pylori Vacuolating Cytotoxin within Mammalian Cells
Infect. Immun., July 1, 2002; 70(7): 3824 - 3832.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Biol. CellHome page
V. Ricci, A. Galmiche, A. Doye, V. Necchi, E. Solcia, and P. Boquet
High Cell Sensitivity to Helicobacter pylori VacA Toxin Depends on a GPI-anchored Protein and is not Blocked by Inhibition of the Clathrin-mediated Pathway of Endocytosis
Mol. Biol. Cell, November 1, 2000; 11(11): 3897 - 3909.
[Abstract] [Full Text]

Home page
 Infect. Immun.Home page
W. Schraw, M. S. McClain, and T. L. Cover
Kinetics and Mechanisms of Extracellular Protein Release by Helicobacter pylori
Infect. Immun., October 1, 1999; 67(10): 5247 - 5252.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
D. M. Czajkowsky, H. Iwamoto, T. L. Cover, and Z. Shao
The vacuolating toxin from Helicobacter pylori forms hexameric pores in lipid bilayers at low pH
PNAS, March 2, 1999; 96(5): 2001 - 2006.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Visit Other APS Journals Online