J Bacteriol Virol.  2011 Dec;41(4):267-278. 10.4167/jbv.2011.41.4.267.

Comparison of Proteome Components of Helicobacter pylori Before and After Mouse Passage

• Lee KJ
• Kim BR
• Cho YA
• Song YG
• Song JY
• Lee KH
• Kang HL
• Baik SC
• Cho MJ
• Rhee KH
• Seo JH
• Youn HS
• Lee WK

• KMID: 2168654
• DOI: http://doi.org/10.4167/jbv.2011.41.4.267

Abstract

The mouse model is alleged to be a useful tool for understanding of pathophysiological roles of Helicobacter pylori in the development of gastric disorders. However, it has been observed that H. pylori strains significantly differed in their fitness in mice and even mouse strains differed in their susceptibilities to a H. pylori strain. Bacterial components of H. pylori which could affect on its fitness in mice have to be elucidated for the establishment of the mouse model for H. pylori infections. In the comparison of colonization ability between two H. pylori Korean isolates, 51 (isolated from a patient with duodenal ulcer) and 52 (isolated from a patient with gastric cancer), 52 could colonize better than 51 on the gastric mucosa of mouse. Proteome components of H. pylori 52, as a good colonizer and H. pylori 51, as a poor one were quantitatively compared each other. Five bacterial proteins including catalase, urease subunit alpha/beta, enolase and ferritin, were up-regulated in 52. In addition, the respective proteome components of the two strains were also compared with their mouse-passaged homologous strains. Seven and five proteins, which included catalase, flagellin A/B in common, were up-regulated in mouse-adapted 51 and 52, respectively. Among the fourteen identified proteins, urease subunit alpha/beta, flagellin A/B, catalase, ferritin, superoxide dismutase and neutrophil-activation protein have been previously known to be necessary to gastric colonization of H. pylori in animal models. The other up-regulated proteins including enolase, elongation factor Tu and fructose-bisphosphate aldolase have been reported to be associated with acid tolerance of H. pylori. These data provide confirmatory evidence for the importance of those proteins in the development of H. pylori-associated gastric disorders.

Keyword

Helicobacter pylori; Proteome; Colonization; Mouse passage

MeSH Terms

Animals
Bacterial Proteins
Catalase
Colon
Ferritins
Flagellin
Fructose-Bisphosphate Aldolase
Gastric Mucosa
Helicobacter
Helicobacter pylori
Humans
Mice
Models, Animal
Peptide Elongation Factor Tu
Phosphopyruvate Hydratase
Proteins
Proteome
Sprains and Strains
Superoxide Dismutase
Urease
Bacterial Proteins
Catalase
Ferritins
Flagellin
Fructose-Bisphosphate Aldolase
Peptide Elongation Factor Tu
Phosphopyruvate Hydratase
Proteins
Proteome
Superoxide Dismutase
Urease

Figure

• 

  Figure 1. Mouse colonization abilities of H. pylori 51 and 52. Mice were inoculated with H. pylori twice for two consecutive days with a dose of 2 × 109 cells. Mice were sacrificed 2 weeks later, antrum and corpus were separated and H. pylori was examined from each tissue by plate counts. Each spot represents the CFU count from one mouse. According to Mann-Whitney U test analysis, there is a significant difference between 51 and 52 in FVB corpus colonization ability (p = 0.04). The horizontal bars within each group represent the median value.

• 

  Figure 2. Two-dimensional gel electrophoresis profiles of H. pylori 51 and 52. A total 100 μg of whole-cell protein of each strain was applied on 170-mm IPG strips with a range of pH 3–10, followed by 12% SDS-PAGE, and visualized by silver staining. The bold numbers with thick arrows represent proteins that are strong in spot intensity compared to the other strain.

• 

  Figure 3. Comparison of two-dimensional gel electrophoresis profiles of H. pylori 52 before and after FVB mouse passage. 100 μg of whole-cell protein of each strain was applied on 170-mm IPG strips with a range of pH 3∼10, followed by 12% SDS-PAGE, and visualized by silver staining. The bold numbers with thick arrows represent proteins that are up-regulated after mouse passage.

• 

  Figure 4. Comparison of two-dimensional gel electrophoresis profiles of H. pylori 51 before and after FVB mouse passage. 100 μg of whole-cell protein of each strain was applied on 170-mm IPG strips with a range of pH 3∼10, followed by 12% SDS-PAGE, and visualized by silver staining. The bold numbers with thick arrows represent proteins that are up-regulated after mouse passage.

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