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<dc:subject>
<z:AutomaticTag><rdf:value>Humans</rdf:value></z:AutomaticTag>
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<dc:subject>
<z:AutomaticTag>
<rdf:value>Helicobacter Infections</rdf:value>
</z:AutomaticTag>
</dc:subject>
<dc:subject>
<z:AutomaticTag>
<rdf:value>Helicobacter pylori</rdf:value>
</z:AutomaticTag>
</dc:subject>
<dc:subject>
<z:AutomaticTag><rdf:value>Gastric Acid</rdf:value></z:AutomaticTag>
</dc:subject>
<dc:subject>
<z:AutomaticTag>
<rdf:value>Hydrogen-Ion Concentration</rdf:value>
</z:AutomaticTag>
</dc:subject>
<dc:subject>
<z:AutomaticTag>
<rdf:value>Membrane Potentials</rdf:value>
</z:AutomaticTag>
</dc:subject>
<dc:subject>
<z:AutomaticTag>
<rdf:value>Proton Pump Inhibitors</rdf:value>
</z:AutomaticTag>
</dc:subject>
<dc:subject>
<z:AutomaticTag><rdf:value>Protons</rdf:value></z:AutomaticTag>
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<dc:title>Acid, protons and Helicobacter pylori</dc:title>
<dcterms:abstract>The anti-ulcer drugs that act as covalent inhibitors of the gastric acid pump are targeted to the gastric H+/K+ ATPase by virtue of accumulation in acid and conversion to the active sulfenamide. This results in extremely effective inhibition of acid secretion. Appropriate dosage is able to optimize acid control therapy for reflux and peptic ulcer disease as compared to H2 receptor antagonists. However, clinical data on recurrence show that Helicobacter pylori eradication should accompany treatment of the lesion. These drugs have been found to synergize with many antibiotics for eradication. The survival of aerobes depends on their ability to maintain a driving force for protons across their inner membrane, the sum of a pH and potential difference gradient, the protonmotive force (pmf). The transmembrane flux of protons across the F1F0 ATPase, driven by the pmf, is coupled to the synthesis of ATP. The internal pH of H. pylori was measured using the fluorescent dye probe, BCECF, and the membrane potential defined by the uptake of the carbocyanine dye, DiSC3 [5] at different pHs to mimic the gastric environment. The protonmotive force at pH 7.0 was composed of a delta pH of 1.4 (-84mV) and a delta potential difference of -131mV, to give a pmf of -215 mV. The effect of variations in external pH on survival of the bacteria in the absence of urea correlated with the effect of external pH on the ability of the bacteria to maintain a pmf. The effect of the addition of 5 mM urea on the pmf was measured at different medium pH values. Urea restored the pmf at pH 3.0 or 3.5, but abolished the pmf at pH 7.0 or higher, due the production of the alkalinizing cation, NH3. Hence H. pylori is an acid-tolerant neutrophile due to urease activity, but urease activity also limits its survival to an acidic environment. These data help explain the occupation of the stomach by the organism and its distribution between fundus and antrum. This distribution and its alteration by proton pump inhibitors also explains the synergism of proton pump inhibition and antibiotics such as amoxicillin and clarithromycin in H. pylori eradication.</dcterms:abstract>
<dc:date>1996</dc:date>
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PMCID: PMC2589012</dc:description>
<bib:pages>301-316</bib:pages>
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<prism:volume>69</prism:volume>
<dc:title>The Yale Journal of Biology and Medicine</dc:title>
<prism:number>3</prism:number>
<dcterms:alternative>Yale J Biol Med</dcterms:alternative>
<dc:identifier>ISSN 0044-0086</dc:identifier>
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<foaf:surname>Penn</foaf:surname>
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<foaf:surname>Hinds</foaf:surname>
<foaf:givenName>Jason</foaf:givenName>
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<foaf:surname>O'Toole</foaf:surname>
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<dc:title>The HP0256 gene product is involved in motility and cell envelope architecture of Helicobacter pylori</dc:title>
<dcterms:abstract>Abstract
Background
Helicobacter pylori
is the causative agent for gastritis, and peptic and duodenal ulcers. The bacterium displays 5-6 polar sheathed flagella that are essential for colonisation and persistence in the gastric mucosa. The biochemistry and genetics of flagellar biogenesis in
H. pylori
has not been fully elucidated. Bioinformatics analysis suggested that the gene HP0256, annotated as hypothetical, was a FliJ homologue. In
Salmonella
, FliJ is a chaperone escort protein for FlgN and FliT, two proteins that themselves display chaperone activity for components of the hook, the rod and the filament.
Results
Ablation of the HP0256 gene in
H. pylori
significantly reduced motility. However, flagellin and hook protein synthesis was not affected in the HP0256 mutant. Transmission electron transmission microscopy revealed that the HP0256 mutant cells displayed a normal flagellum configuration, suggesting that HP0256 was not essential for assembly and polar localisation of the flagella in the cell. Interestingly, whole genome microarrays of an HP0256 mutant revealed transcriptional changes in a number of genes associated with the flagellar regulon and the cell envelope, such as outer membrane proteins and adhesins. Consistent with the array data, lack of the HP0256 gene significantly reduced adhesion and the inflammatory response in host cells.
Conclusions
We conclude that HP0256 is not a functional counterpart of FliJ in
H. pylori
. However, it is required for full motility and it is involved, possibly indirectly, in expression of outer membrane proteins and adhesins involved in pathogenesis and adhesion.</dcterms:abstract>
<dc:date>12/2010</dc:date>
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<dc:title>ChePep Controls Helicobacter pylori Infection of the Gastric Glands and Chemotaxis in the <i>Epsilonproteobacteria</i></dc:title>
<dcterms:abstract>ABSTRACT
Microbes use directed motility to colonize harsh and dynamic environments. We discovered that
Helicobacter pylori
strains establish bacterial colonies deep in the gastric glands and identified a novel protein, ChePep, necessary to colonize this niche. ChePep is preferentially localized to the flagellar pole. Although mutants lacking ChePep have normal flagellar ultrastructure and are motile, they have a slight defect in swarming ability. By tracking the movement of single bacteria, we found that ∆ChePep mutants cannot control the rotation of their flagella and swim with abnormally frequent reversals. These mutants even sustain bursts of movement backwards with the flagella pulling the bacteria. Genetic analysis of the chemotaxis signaling pathway shows that ChePep regulates flagellar rotation through the chemotaxis system. By examining
H. pylori
within a microscopic pH gradient, we determined that ChePep is critical for regulating chemotactic behavior. The
chePep
gene is unique to the
Epsilonproteobacteria
but is found throughout this diverse group. We expressed ChePep from other members of the
Epsilonproteobacteria
, including the zoonotic pathogen
Campylobacter jejuni
and the deep sea hydrothermal vent inhabitant
Caminibacter mediatlanticus
, in
H. pylori
and found that ChePep is functionally conserved across this class. ChePep represents a new family of chemotaxis regulators unique to the
Epsilonproteobacteria
and illustrates the different strategies that microbes have evolved to control motility.
IMPORTANCE
Helicobacter pylori
strains infect half of all humans worldwide and contribute to the development of peptic ulcers and gastric cancer.
H. pylori
cannot survive within the acidic lumen of the stomach and uses flagella to actively swim to and colonize the protective mucus and epithelium. The chemotaxis system allows
H. pylori
to navigate by regulating the rotation of its flagella. We identified a new protein, ChePep, which controls chemotaxis in
H. pylori
. ChePep mutants fail to colonize the gastric glands of mice and are completely outcompeted by normal
H. pylori
. Genes encoding ChePep are found only in the class
Epsilonproteobacteria
, which includes the human pathogen
Campylobacter jejuni
and environmental microbes like the deep-sea hydrothermal vent colonizer
Caminibacter mediatlanticus
, and we show that ChePep function is conserved in this class. Our study identifies a new colonization factor in
H. pylori
and also provides insight into the control and evolution of bacterial chemotaxis.
,
Helicobacter pylori
strains infect half of all humans worldwide and contribute to the development of peptic ulcers and gastric cancer.
H. pylori
cannot survive within the acidic lumen of the stomach and uses flagella to actively swim to and colonize the protective mucus and epithelium. The chemotaxis system allows
H. pylori
to navigate by regulating the rotation of its flagella. We identified a new protein, ChePep, which controls chemotaxis in
H. pylori
. ChePep mutants fail to colonize the gastric glands of mice and are completely outcompeted by normal
H. pylori
. Genes encoding ChePep are found only in the class
Epsilonproteobacteria
, which includes the human pathogen
Campylobacter jejuni
and environmental microbes like the deep-sea hydrothermal vent colonizer
Caminibacter mediatlanticus
, and we show that ChePep function is conserved in this class. Our study identifies a new colonization factor in
H. pylori
and also provides insight into the control and evolution of bacterial chemotaxis.</dcterms:abstract>
<dc:date>09/2011</dc:date>
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<dc:title>Disruption of the Epithelial Apical-Junctional Complex by <i>Helicobacter pylori</i> CagA</dc:title>
<dcterms:abstract>Helicobacter pylori
translocates the protein CagA into gastric epithelial cells and has been linked to peptic ulcer disease and gastric carcinoma. We show that injected CagA associates with the epithelial tight-junction scaffolding protein ZO-1 and the transmembrane protein junctional adhesion molecule, causing an ectopic assembly of tight-junction components at sites of bacterial attachment, and altering the composition and function of the apical-junctional complex. Long-term CagA delivery to polarized epithelia caused a disruption of the epithelial barrier function and dysplastic alterations in epithelial cell morphology. CagA appears to target
H. pylori
to host cell intercellular junctions and to disrupt junction-mediated functions.</dcterms:abstract>
<dc:date>2003-05-30</dc:date>
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