Literature DB >> 3950447

Campylobacter pyloridis and gastritis: association with intercellular spaces and adaptation to an environment of mucus as important factors in colonization of the gastric epithelium.

S L Hazell, A Lee, L Brady, W Hennessy.   

Abstract

Stomach biopsy specimens from greater than 40 individuals with Campylobacter pyloridis-associated gastritis were examined by light and electron microscopy. The bacteria were consistently seen in two locations: within the gastric mucus and associated with intercellular junctions of gastric epithelial cells. C. pyloridis is suggested to be one of a broad group of spiral bacteria that are adapted to the peculiar niche provided by intestinal mucus. The spiral morphology and the form of motility of these organisms give them a selective advantage in a viscous environment. This point has been demonstrated in vitro by measurement of the velocity of clinical isolates in solutions of methyl cellulose of varying viscosity. The localization of C. pyloridis close to intercellular junctions is proposed to be due to the presence of preferred metabolites or growth factors, e.g., urea and hemin. All isolates show an extremely high urease activity and require hemin for growth.

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Year:  1986        PMID: 3950447     DOI: 10.1093/infdis/153.4.658

Source DB:  PubMed          Journal:  J Infect Dis        ISSN: 0022-1899            Impact factor:   5.226


  125 in total

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Review 2.  Motility and chemotaxis in Campylobacter and Helicobacter .

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3.  Local gastric and serum concentrations of rebamipide following oral ingestion in healthy volunteers.

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4.  Peptidoglycan crosslinking relaxation promotes Helicobacter pylori's helical shape and stomach colonization.

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5.  The urease enzyme of Helicobacter pylori does not function as an adhesin.

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6.  Electron microscopic study of association between Helicobacter pylori and gastric and duodenal mucosa.

Authors:  L A Noach; T M Rolf; G N Tytgat
Journal:  J Clin Pathol       Date:  1994-08       Impact factor: 3.411

7.  Characterization of an acidic-pH-inducible stress protein (hsp70), a putative sulfatide binding adhesin, from Helicobacter pylori.

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8.  Mutation of the cytotoxin-associated cagA gene does not affect the vacuolating cytotoxin activity of Helicobacter pylori.

Authors:  M K Tummuru; T L Cover; M J Blaser
Journal:  Infect Immun       Date:  1994-06       Impact factor: 3.441

9.  Cloning and characterization of hemolytic genes from Helicobacter pylori.

Authors:  E S Drazek; A Dubois; R K Holmes; D Kersulyte; N S Akopyants; D E Berg; R L Warren
Journal:  Infect Immun       Date:  1995-11       Impact factor: 3.441

10.  Inability of an isogenic urease-negative mutant stain of Helicobacter mustelae to colonize the ferret stomach.

Authors:  K A Andrutis; J G Fox; D B Schauer; R P Marini; J C Murphy; L Yan; J V Solnick
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