Antibodies to Escherichia coli 06 Porins Cross-React with Urinary Pathogens

Kawahara, Motoshi; Human, Liset G.; Winningham, Jefferey S.; Domingue, Gerald J.

doi:10.1016/s0171-2985(11)80408-0

Cited by 2 publications

(2 citation statements)

References 28 publications

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“…Furthermore, to broaden the search for antigens, we included the LEE-negative O113:H11 serotype, which has also been associated with HUS (37,38). Prior studies have reported that exposure to enterobacterial OMPs stimulates a humoral immune response in infected patients (39)(40)(41), therefore making them candidates suitable for use in vaccines against Gram-negative pathogens (42)(43)(44)(45).…”

Section: Discussionmentioning

confidence: 99%

Immunoproteomic Analysis To Identify Shiga Toxin-Producing Escherichia coli Outer Membrane Proteins Expressed during Human Infection

et al. 2014

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b Shiga-toxin producing Escherichia coli (STEC) is the etiologic agent of acute diarrhea, dysentery, and hemolytic-uremic syndrome (HUS). There is no approved vaccine for STEC infection in humans, and antibiotic use is contraindicated, as it promotes Shiga toxin production. In order to identify STEC-associated antigens and immunogenic proteins, outer membrane proteins (OMPs) were extracted from STEC O26:H11, O103, O113:H21, and O157:H7 strains, and commensal E. coli strain HS was used as a control. SDS-PAGE, two-dimensional-PAGE analysis, Western blot assays using sera from pediatric HUS patients and controls, and matrix-assisted laser desorption ionization-tandem time of flight analyses were used to identify 12 immunogenic OMPs, some of which were not reactive with control sera. Importantly, seven of these proteins have not been previously reported to be immunogenic in STEC strains. Among these seven proteins, OmpT and Cah displayed IgG and IgA reactivity with sera from HUS patients. Genes encoding these two proteins were present in a majority of STEC strains. Knowledge of the antigens produced during infection of the host and the immune response to those antigens will be important for future vaccine development.

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Section: Discussionmentioning

confidence: 99%

Immunoproteomic Analysis To Identify Shiga Toxin-Producing Escherichia coli Outer Membrane Proteins Expressed during Human Infection

et al. 2014

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“…Furthermore, some of these OMPs are target receptors for bacteriophages and colicins. Finally, due to their location as interfaces between the cell and the environment, OMPs are important candidate antigens for developing strategies aimed at providing protection against bacterial pathogens [7–10].…”

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confidence: 99%

Proteomic analysis of the Escherichia coli outer membrane

Molloy

Herbert²,

Slade

et al. 2000

European Journal of Biochemistry

441

396

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Outer membrane proteins (OMPs) of Gram-negative bacteria are key molecules that interface the cell with the environment. Traditional biochemical and genetic approaches have yielded a wealth of knowledge relating to the function of OMPs. Nonetheless, with the completion of the Escherichia coli genome sequencing project there is the opportunity to further expand our understanding of the organization, expression and function of the OMPs in this Gram-negative bacterium. In this report we describe a proteomic approach which provides a platform for parallel analysis of OMPs. We propose a rapid method for isolation of bacterial OMPs using carbonate incubation, purification and protein array by two-dimensional electrophoresis, followed by protein identification using mass spectrometry. Applying this method to examine E. coli K-12 cells grown in minimal media we identified 21 out of 26 (80%) of the predicted integral OMPs that are annotated in SWISS-PROT release 37 and predicted to separate within the range of pH 4±7 and molecular mass 10±80 kDa. Five outer membrane lipoproteins were also identified and only minor contamination by nonmembrane proteins was observed. Importantly, this research readily demonstrates that integral OMPs, commonly missing from 2D gel maps, are amenable to separation by two-dimensional electrophoresis. Two of the identified OMPs (YbiL, YeaF) were previously known only from their ORFs, and their identification confirms the cognate genes are transcribed and translated. Furthermore, we show that like the E. coli iron receptors FhuE and FhuA, the expression of YbiL is markedly increased by iron limitation, suggesting a putative role for this protein in iron transport. In an additional demonstration we show the value of parallel protein analysis to document changes in E. coli OMP expression as influenced by culture temperature.

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Antibodies to Escherichia coli 06 Porins Cross-React with Urinary Pathogens

Cited by 2 publications

References 28 publications

Immunoproteomic Analysis To Identify Shiga Toxin-Producing Escherichia coli Outer Membrane Proteins Expressed during Human Infection

Immunoproteomic Analysis To Identify Shiga Toxin-Producing Escherichia coli Outer Membrane Proteins Expressed during Human Infection

Proteomic analysis of the Escherichia coli outer membrane

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