Hydrophobic characterisation of Helicobacter (Campylobacter) pylori

H. Pruul; C. Stewart Goodwin; P. J. McDonald; G. Lewis; D. Pankhurst

doi:10.1099/00222615-32-2-93

Hydrophobic characterisation of Helicobacter (Campylobacter) pylori

H. Pruul, C. Stewart Goodwin, P. J. McDonald, G. Lewis, D. Pankhurst

Research output: Contribution to journal › Article › peer-review

12 Citations (Scopus)

Abstract

Cell-surface hydrophobicity of Helicobacter (formerly Campylobacter) pylori was tested by aqueous two-phase partitioning and hydrophobic interaction chromatography. The hydrophobicity of H. pylori greatly exceeded that of Campylobacter fetus subsp. fetus, C. jejuni and Bacillus subtilis. A partition coefficient (PC) of hydrophobicity in the two-phase system was determined for H. pylori. PC was dependent on pH and the PC value was increased by greater than 20-fold at pH 2.5. Lithium cations increased PC, indicating a net negative surface charge. The presence of urea prevented the relative loss of hydrophobicity at raised pH. Exposure of H. pylori to proteolytic enzymes reduced the ability of the bacteria to adhere to human polymorphonuclear neutrophils (PMN). These findings suggest that H. pylori possesses protein-associated hydrophobic factors that are responsible for the non-opsonic adherence to PMN cell membranes.

Original language	English
Pages (from-to)	93-100
Number of pages	8
Journal	Journal of Medical Microbiology
Volume	32
Issue number	2
DOIs	https://doi.org/10.1099/00222615-32-2-93
Publication status	Published - 1 Jun 1990
Externally published	Yes

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abstract = "Cell-surface hydrophobicity of Helicobacter (formerly Campylobacter) pylori was tested by aqueous two-phase partitioning and hydrophobic interaction chromatography. The hydrophobicity of H. pylori greatly exceeded that of Campylobacter fetus subsp. fetus, C. jejuni and Bacillus subtilis. A partition coefficient (PC) of hydrophobicity in the two-phase system was determined for H. pylori. PC was dependent on pH and the PC value was increased by greater than 20-fold at pH 2.5. Lithium cations increased PC, indicating a net negative surface charge. The presence of urea prevented the relative loss of hydrophobicity at raised pH. Exposure of H. pylori to proteolytic enzymes reduced the ability of the bacteria to adhere to human polymorphonuclear neutrophils (PMN). These findings suggest that H. pylori possesses protein-associated hydrophobic factors that are responsible for the non-opsonic adherence to PMN cell membranes.",

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AU - Pruul, H.

AU - Goodwin, C. Stewart

AU - McDonald, P. J.

AU - Lewis, G.

AU - Pankhurst, D.

PY - 1990/6/1

Y1 - 1990/6/1

N2 - Cell-surface hydrophobicity of Helicobacter (formerly Campylobacter) pylori was tested by aqueous two-phase partitioning and hydrophobic interaction chromatography. The hydrophobicity of H. pylori greatly exceeded that of Campylobacter fetus subsp. fetus, C. jejuni and Bacillus subtilis. A partition coefficient (PC) of hydrophobicity in the two-phase system was determined for H. pylori. PC was dependent on pH and the PC value was increased by greater than 20-fold at pH 2.5. Lithium cations increased PC, indicating a net negative surface charge. The presence of urea prevented the relative loss of hydrophobicity at raised pH. Exposure of H. pylori to proteolytic enzymes reduced the ability of the bacteria to adhere to human polymorphonuclear neutrophils (PMN). These findings suggest that H. pylori possesses protein-associated hydrophobic factors that are responsible for the non-opsonic adherence to PMN cell membranes.

AB - Cell-surface hydrophobicity of Helicobacter (formerly Campylobacter) pylori was tested by aqueous two-phase partitioning and hydrophobic interaction chromatography. The hydrophobicity of H. pylori greatly exceeded that of Campylobacter fetus subsp. fetus, C. jejuni and Bacillus subtilis. A partition coefficient (PC) of hydrophobicity in the two-phase system was determined for H. pylori. PC was dependent on pH and the PC value was increased by greater than 20-fold at pH 2.5. Lithium cations increased PC, indicating a net negative surface charge. The presence of urea prevented the relative loss of hydrophobicity at raised pH. Exposure of H. pylori to proteolytic enzymes reduced the ability of the bacteria to adhere to human polymorphonuclear neutrophils (PMN). These findings suggest that H. pylori possesses protein-associated hydrophobic factors that are responsible for the non-opsonic adherence to PMN cell membranes.

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Hydrophobic characterisation of Helicobacter (Campylobacter) pylori

Abstract

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