Proteomic Analysis of the Sarcosine-Insoluble Outer Membrane Fraction ofPseudomonasaeruginosaResponding to Ampicilin, Kanamycin, and Tetracycline Resistance

2005 ◽  
Vol 4 (6) ◽  
pp. 2257-2265 ◽  
Author(s):  
Xuanxian Peng ◽  
Changxin Xu ◽  
Haixia Ren ◽  
Xiangmin Lin ◽  
Lina Wu ◽  
...  
Keyword(s):  
Outer Membrane ◽  
Proteomic Analysis ◽  
Membrane Fraction ◽  
Tetracycline Resistance ◽  
Outer Membrane Fraction

Proteomic analysis of the sarcosine-insoluble outer membrane fraction of the bacterial pathogenBartonella henselae

2007 ◽  
pp. 203-224
Author(s):  
Thomas A. Rhomberg ◽  
Olof Karlberg ◽  
Thierry Mini ◽  
Ursula Zimny-Arndt ◽  
Ulrika Wickenberg ◽  
...  
Keyword(s):  
Outer Membrane ◽  
Proteomic Analysis ◽  
Membrane Fraction ◽  
Outer Membrane Fraction

scholarly journals Proteomic Analysis of the Sarcosine-Insoluble Outer Membrane Fraction of Helicobacter pylori Strain 26695

2004 ◽  
Vol 186 (4) ◽  
pp. 949-955 ◽  
Author(s):  
Seung-Chul Baik ◽  
Kyung-Mi Kim ◽  
Su-Min Song ◽  
Do-Su Kim ◽  
Jin-Su Jun ◽  
...  
Keyword(s):  
Helicobacter Pylori ◽  
Outer Membrane ◽  
Proteomic Analysis ◽  
Membrane Fraction ◽  
Outer Membrane Proteins ◽  
Immunoblot Analysis ◽  
Outer Membrane Fraction ◽  
Flight Mass Spectrometry ◽  
Molecular Masses ◽  
H Pylori

ABSTRACT Helicobacter pylori causes gastroduodenal disease, which is mediated in part by its outer membrane proteins (OMPs). To identify OMPs of H. pylori strain 26695, we performed a proteomic analysis. A sarcosine-insoluble outer membrane fraction was resolved by two-dimensional electrophoresis with immobilized pH gradient strips. Most of the protein spots, with molecular masses of 10 to 100 kDa, were visible on the gel in the alkaline pI regions (6.0 to 10.0). The proteome of the OMPs was analyzed by matrix-assisted laser desorption ionization-time-of-flight mass spectrometry. Of the 80 protein spots processed, 62 spots were identified; they represented 35 genes, including 16 kinds of OMP. Moreover, we identified 9 immunoreactive proteins by immunoblot analysis. This study contributes to the characterization of the H. pylori strain 26695 proteome and may help to further elucidate the biological function of H. pylori OMPs and the pathogenesis of H. pylori infection.

scholarly journals Proteomic Analysis of the Sarcosine-Insoluble Outer Membrane Fraction of Helicobacter pylori Strain 26695

2005 ◽  
Vol 187 (4) ◽  
pp. 1541-1541
Author(s):  
Seung-Chul Baik ◽  
Kyung-Mi Kim ◽  
Su-Min Song ◽  
Do-Su Kim ◽  
Jin-Su Jun ◽  
...  
Keyword(s):  
Helicobacter Pylori ◽  
Outer Membrane ◽  
Proteomic Analysis ◽  
Membrane Fraction ◽  
Outer Membrane Fraction

Proteomic analysis of the sarcosine-insoluble outer membrane fraction of the bacterial pathogenBartonella henselae

PROTEOMICS ◽  
2004 ◽  
Vol 4 (10) ◽  
pp. 3021-3033 ◽  
Author(s):  
Thomas A. Rhomberg ◽  
Olof Karlberg ◽  
Thierry Mini ◽  
Ursula Zimny-Arndt ◽  
Ulrika Wickenberg ◽  
...  
Keyword(s):  
Outer Membrane ◽  
Proteomic Analysis ◽  
Membrane Fraction ◽  
Outer Membrane Fraction

Binding between the par region of plasmids R1 and pSC101 and the outer membrane fraction of the host bacteria.

1983 ◽  
Vol 2 (1) ◽  
pp. 27-32 ◽  
Author(s):  
P. Gustafsson ◽  
H. Wolf-Watz ◽  
L. Lind ◽  
K.E. Johansson ◽  
K. Nordström
Keyword(s):  
Outer Membrane ◽  
Membrane Fraction ◽  
Outer Membrane Fraction

Pseudomonas aeruginosa lectin LecB is located in the outer membrane and is involved in biofilm formation

Microbiology ◽  
2005 ◽  
Vol 151 (5) ◽  
pp. 1313-1323 ◽  
Author(s):  
Denis Tielker ◽  
Stephanie Hacker ◽  
Remy Loris ◽  
Martin Strathmann ◽  
Jost Wingender ◽  
...  
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Outer Membrane ◽  
Biofilm Formation ◽  
Membrane Fraction ◽  
Opportunistic Pathogen ◽  
Cell Fractionation ◽  
Intrinsic Resistance ◽  
Outer Membrane Fraction ◽  
Airway Mucosa ◽  
Tract Infections

Pseudomonas aeruginosa is an opportunistic pathogen which causes a variety of diseases, including respiratory tract infections in patients suffering from cystic fibrosis. Therapeutic treatment of P. aeruginosa infections is still very difficult because the bacteria exhibit high intrinsic resistance against a variety of different antibiotics and, in addition, form stable biofilms, e.g. in the human lung. Several virulence factors are produced by P. aeruginosa, among them the two lectins LecA and LecB, which exert different cytotoxic effects on respiratory epithelial cells and presumably facilitate bacterial adhesion to the airway mucosa. Here, the physiology has been studied of the lectin LecB, which binds specifically to l-fucose. A LecB-deficient P. aeruginosa mutant was shown to be impaired in biofilm formation when compared with the wild-type strain, suggesting an important role for LecB in this process. This result prompted an investigation of the subcellular localization of LecB by cell fractionation and subsequent immunoblotting. The results show that LecB is abundantly present in the bacterial outer-membrane fraction. It is further demonstrated that LecB could be released specifically by treatment of the outer-membrane fraction with p-nitrophenyl α-l-fucose, whereas treatment with d-galactose had no effect. In contrast, a LecB protein carrying the mutation D104A, which results in a defective sugar-binding site, was no longer detectable in the membrane fraction, suggesting that LecB binds to specific carbohydrate ligands located at the bacterial cell surface. Staining of biofilm cells using fluorescently labelled LecB confirmed the presence of these ligands.

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