H. pylori Escape Host Immunoreaction Through Inhibiting ILK Expression by VacA

Yuan, Jianping; Li, Ping; Tao, Jing; Shi, Xiaodong; Hu, Bao-Yu; Chen, Huabiao; Guo, Xia

doi:10.1038/cmi.2009.26

Cited by 21 publications

(14 citation statements)

References 44 publications

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“…Bacterial arginase and γ-glutamyl transferase show similar functions in altering the normal function of T-cells [74,75], while arginase and VacA additionally downregulate the expression of inducible nitric oxide synthase [76,77].…”

Section: Manipulation Of the Immune Systemmentioning

confidence: 99%

The Human Gastric PathogenHelicobacter pyloriand Its Association with Gastric Cancer and Ulcer Disease

Bauer

Meyer

2011

Ulcers

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With the momentous discovery in the 1980's that a bacterium,Helicobacter pylori, can cause peptic ulcer disease and gastric cancer, antibiotic therapies and prophylactic measures have been successful, only in part, in reducing the global burden of these diseases. To date, ~700,000 deaths worldwide are still attributable annually to gastric cancer alone. Here, we reviewH. pylori's contribution to the epidemiology and histopathology of both gastric cancer and peptic ulcer disease. Furthermore, we examine the host-pathogen relationship andH. pyloribiology in context of these diseases, focusing on strain differences, virulence factors (CagA and VacA), immune activation and the challenges posed by resistance to existing therapies. We consider also the important role of host-genetic variants, for example, in inflammatory response genes, in determining infection outcome and the role ofH. pyloriin other pathologies—some accepted, for example, MALT lymphoma, and others more controversial, for example, idiopathic thrombocytic purpura. More recently, intriguing suggestions thatH. pylorihas protective effects in GERD and autoimmune diseases, such as asthma, have gained momentum. Therefore, we consider the basis for these suggestions and discuss the potential impact for future therapeutic rationales.

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Section: Manipulation Of the Immune Systemmentioning

confidence: 99%

The Human Gastric PathogenHelicobacter pyloriand Its Association with Gastric Cancer and Ulcer Disease

Bauer

Meyer

2011

Ulcers

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“…Megasomes show a limited lumenal acidification and acquire only a limited amount of late endosomal/lysosomal markers [221]. Moreover, Yuan et al [223] suggested that VacA may favor H. pylori survival in macrophages by decreasing ROS production in such cells through inhibition of the expression of endothelial nitric oxygen synthase mediated by a suppressive effect of the toxin on the expression of integrin-linked kinase. However, a VacA role in H. pylori-induced homotypic phagosome fusion or prolonged intracellular survival of bacteria in human monocytes has been challenged by Rittig et al [224].…”

Section: Effects On Phagocytosis and Antigen Presentationmentioning

confidence: 97%

Helicobacter pylori vacuolating toxin

Ricci

Sommi

Boquet

2015

The Comprehensive Sourcebook of Bacterial Protein Toxins

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“…It usually causes chronic infection and persists for the life of the host and is not eradicated despite a vigorous immune response was raised by host immune system [3], suggesting that the bacterial reserve some mechanisms for escaping from host immune response, such mechanisms have been under extensive study and reported elsewhere [4], [5], [6].…”

Section: Introductionmentioning

confidence: 99%

Expression, Purification and Characterization of Arginase from Helicobacter pylori in Its Apo Form

Zhang

et al. 2011

PLoS ONE

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Arginase, a manganese-dependent enzyme that widely distributed in almost all creatures, is a urea cycle enzyme that catalyzes the hydrolysis of L-arginine to generate L-ornithine and urea. Compared with the well-studied arginases from animals and yeast, only a few eubacterial arginases have been characterized, such as those from H. pylori and B. anthracis. However, these enzymes used for arginase activity assay were all expressed with LB medium, as low concentration of Mn2+ was detectable in the medium, protein obtained were partially Mn2+ bonded, which may affect the results of arginase activity assay. In the present study, H. pylori arginase (RocF) was expressed in a Mn2+ and Co2+ free minimal medium, the resulting protein was purified through affinity and gel filtration chromatography and the apo-form of RocF was confirmed by flame photometry analysis. Gel filtration indicates that the enzyme exists as monomer in solution, which was unique as compared with homologous enzymes. Arginase activity assay revealed that apo-RocF had an acidic pH optimum of 6.4 and exhibited metal preference of Co2+>Ni2+>Mn2+. We also confirmed that heat-activation and reducing regents have significant impact on arginase activity of RocF, and inhibits S-(2-boronoethyl)-L-Cysteine (BEC) and Nω-hydroxy-nor-Arginine (nor-NOHA) inhibit the activity of RocF in a dose-dependent manner.

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H. pylori Escape Host Immunoreaction Through Inhibiting ILK Expression by VacA

Cited by 21 publications

References 44 publications

The Human Gastric PathogenHelicobacter pyloriand Its Association with Gastric Cancer and Ulcer Disease

The Human Gastric PathogenHelicobacter pyloriand Its Association with Gastric Cancer and Ulcer Disease

Helicobacter pylori vacuolating toxin

Expression, Purification and Characterization of Arginase from Helicobacter pylori in Its Apo Form

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