Interaction of Helicobacter pylori with host cells:: function of secreted and translocated molecules

被引：80

作者：

Rieder, G ^{[1
]}

Fischer, W ^{[1
]}

Haas, R ^{[1
]}

机构：

[1] Univ Munich, Max Von Pettenkofer Inst, D-80336 Munich, Germany

来源：

CURRENT OPINION IN MICROBIOLOGY | 2005年 / 8卷 / 01期

关键词：

D O I：

10.1016/j.mib.2004.12.004

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

Secreted proteins are of general interest from the perspective of bacteria-host interaction. The gastric bacterial pathogen Helicobacter pylori uses a set of secreted and translocated proteins - including outer membrane adhesins, secreted extracellular enzymes and translocated effector proteins - to adapt to its extraordinary habitat, the gastric mucosa. Two major virulence factors of H. pylori are the vacuolating cytotoxin (VacA) and the cag type-IV secretion system and its translocated effector protein, cytotoxin-associated antigen A (CagA). VacA targets not only epithelial cells, but also cells of the immune system and induces immunosuppression. CagA has been shown to interact with a growing set of eucaryotic signaling molecules in phosphorylation-dependent and -independent ways.

引用

页码：67 / 73

页数：7

共 50 条

[41] A novel apoptosis-inducing protein from Helicobacter pylori [J].

Shibayama, K ;

Kamachi, K ;

Nagata, N ;

Yagi, T ;

Nada, T ;

Doi, YH ;

Shibata, N ;

Yokoyama, K ;

Yamane, K ;

Kato, H ;

Iinuma, Y ;

Arakawa, Y .

MOLECULAR MICROBIOLOGY, 2003, 47 (02) :443-451

[42] c-Src/Lyn kinases activate Helicobacter pylori CagA through tyrosine phosphorylation of the EPIYA motifs [J].

Stein, M ;

Bagnoli, F ;

Halenbeck, R ;

Rappuoli, R ;

Fantl, WJ ;

Covacci, A .

MOLECULAR MICROBIOLOGY, 2002, 43 (04) :971-980

[43] Medical progress:: Helicobacter pylori infection [J].

Suerbaum, S ;

Michetti, P .

NEW ENGLAND JOURNAL OF MEDICINE, 2002, 347 (15) :1175-1186

[44] Inhibition of primary human T cell proliferation by Helicobacter pylori vacuolating toxin (VacA) is independent of VacA effects on IL-2 secretion [J].

Sundrud, MS ;

Torres, VJ ;

Unutmaz, D ;

Cover, TL .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2004, 101 (20) :7727-7732

[45] Formation of anion-selective channels in the cell plasma membrane by the toxin VacA of Helicobacter pylori is required for its biological activity [J].

Szabò, I ;

Brutsche, S ;

Tombola, F ;

Moschioni, M ;

Satin, B ;

Telford, JL ;

Rappuoli, R ;

Montecucco, C ;

Papini, E ;

Zoratti, M .

EMBO JOURNAL, 1999, 18 (20) :5517-5527

[46] Structural definition on the surface of Helicobacter pylori type IV secretion apparatus [J].

Tanaka, J ;

Suzuki, T ;

Mimuro, H ;

Sasakawa, C .

CELLULAR MICROBIOLOGY, 2003, 5 (06) :395-404

[47] The Helicobacter pylori VacA toxin is a urea permease that promotes urea diffusion across epithelia [J].

Tombola, F ;

Morbiato, L ;

Del Giudice, G ;

Rappuoli, R ;

Zoratti, M ;

Papini, E .

JOURNAL OF CLINICAL INVESTIGATION, 2001, 108 (06) :929-937

[48] Effects of Helicobacter pylori CagA protein on the growth and survival of B lymphocytes, the origin of MALT lymphoma [J].

Umehara, S ;

Higashi, H ;

Ohnishi, N ;

Asaka, M ;

Hatakeyama, M .

ONCOGENE, 2003, 22 (51) :8337-8342

[49] Helicobacter pylori vacuolating cytotoxin enters cells, localizes to the mitochondria, and induces mitochondrial membrane permeability changes correlated to toxin channel activity [J].

Willhite, DC ;

Blanke, SR .

CELLULAR MICROBIOLOGY, 2004, 6 (02) :143-154

[50] Protein-tyrosine phosphatase α, RPTPα, is a Helicobacter pylori VacA receptor [J].

Yahiro, K ;

Wada, A ;

Nakayama, M ;

Kimura, T ;

Ogushi, K ;

Niidome, T ;

Aoyagi, H ;

Yoshino, K ;

Yonezawa, K ;

Moss, J ;

Hirayama, T .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2003, 278 (21) :19183-19189

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