scholarly journals Partial Proteome Map of Campylobacter Jejuni Strain Nctc11168 by Gel-Free Proteomics Analysis

2014 ◽  
Vol 2 (4) ◽  
pp. 464-477
Author(s):  
Zilun Shi ◽  
Chris Dawson ◽  
Stephen L.W. On ◽  
Malik Altaf Hussain
Keyword(s):  
Campylobacter Jejuni ◽  
Foodborne Pathogen ◽  
Brain Heart Infusion ◽  
Cell Protein ◽  
Absolute Quantitation ◽  
Whole Cell ◽  
Itraq Analysis ◽  
Proteomic Approach ◽  
Whole Cell Protein ◽  
Isobaric Tags

A proteome map of the foodborne pathogen Campylobacter jejuni NCTC11168 was analyzed using a state-of-the-art gel-free proteomic approach for the first time. A whole cell protein extract was prepared from the C. jejuni strain NCTC11168 grown in brain heart infusion (BHI) broth at 42°C under microaerobic conditions. A gel-free technique using isobaric tags for relative and absolute quantitation (iTRAQ) was employed to create a protein expression profile of the strain. Liquid chromatography-mass spectrometry (LC-MS/MS) was used to identify the proteins. Protein functionalities were searched to classify them. A total of 235 proteins were identified in the whole cell protein fraction of C. jejuni NCTC11168 cells using iTRAQ analysis. Functional grouping of the identified proteins showed that forty percent of these proteins were associated with energy metabolism, protein synthesis and genetic information processing. iTRAQ was faster, easier and proved more sensitive than two-dimensional gel-based proteomics approaches previously applied to C. jejuni, making it an attractive tool for further studies of cellular physiological response. DOI: http://dx.doi.org/10.3126/ijasbt.v2i4.11253  Int J Appl Sci Biotechnol, Vol. 2(4): 464-477 

scholarly journals Proteomic Studies for the Investigation of γ-Globin Induction by Decitabine in Human Primary Erythroid Progenitor Cultures

2020 ◽  
Vol 9 (1) ◽  
pp. 134
Author(s):  
Andria Theodorou ◽  
Marios Phylactides ◽  
Eleni Katsantoni ◽  
Kostas Vougas ◽  
Spyros D. Garbis ◽  
...  
Keyword(s):  
Stress Proteins ◽  
Chromatin Modification ◽  
Protein Stabilization ◽  
Absolute Quantitation ◽  
Erythroid Progenitor ◽  
Itraq Analysis ◽  
Proteomic Approach ◽  
Pharmacological Targets ◽  
Liquid Chromatography Tandem Mass ◽  
Isobaric Tags

Reactivation of γ-globin is considered a promising approach for the treatment of β-thalassemia and sickle cell disease. Therapeutic induction of γ-globin expression, however, is fraught with lack of suitable therapeutic targets. The aim of this study was to investigate the effects that treatment with decitabine has on the proteome of human primary erythroid cells from healthy and thalassemic volunteers, as a means of identifying new potential pharmacological targets. Decitabine is a known γ-globin inducer, which is not, however, safe enough for clinical use. A proteomic approach utilizing isobaric tags for relative and absolute quantitation (iTRAQ) analysis, in combination with high-pH reverse phase peptide fractionation followed by liquid chromatography-tandem mass spectrometry (LC-MS/MS), was employed to investigate the effects of decitabine treatment. Bioinformatics analysis making use of the Database for Annotation, Visualization and Integrated Discovery (DAVID) was employed for functional annotation of the 192 differentially expressed proteins identified. The data are available via ProteomeXchange with identifier PXD006889. The proteins fall into various biological pathways, such as the NF-κB signaling pathway, and into many functional categories including regulation of cell proliferation, transcription factor and DNA binding, protein stabilization, chromatin modification and organization, and oxidative stress proteins.

scholarly journals The Campylobacter jejuni CiaD effector co-opts the host cell protein IQGAP1 to promote cell entry

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Nicholas M. Negretti ◽  
Christopher R. Gourley ◽  
Prabhat K. Talukdar ◽  
Geremy Clair ◽  
Courtney M. Klappenbach ◽  
...  
Keyword(s):  
Host Cell ◽  
Campylobacter Jejuni ◽  
Foodborne Pathogen ◽  
Small Gtpase ◽  
Host Cells ◽  
Cell Protein ◽  
Host Cell Protein ◽  
Cell Binding ◽  
Actin Reorganization ◽  
Cell Cytosol

AbstractCampylobacter jejuni is a foodborne pathogen that binds to and invades the epithelial cells lining the human intestinal tract. Maximal invasion of host cells by C. jejuni requires cell binding as well as delivery of the Cia proteins (Campylobacter invasion antigens) to the host cell cytosol via the flagellum. Here, we show that CiaD binds to the host cell protein IQGAP1 (a Ras GTPase-activating-like protein), thus displacing RacGAP1 from the IQGAP1 complex. This, in turn, leads to the unconstrained activity of the small GTPase Rac1, which is known to have roles in actin reorganization and internalization of C. jejuni. Our results represent the identification of a host cell protein targeted by a flagellar secreted effector protein and demonstrate that C. jejuni-stimulated Rac signaling is dependent on IQGAP1.

Preliminary screening for toxin genes amongst stock cultures of Clostridium perfringens strains isolated from dogs and calves

2014 ◽  
Vol 4 (3) ◽  
pp. 127-132
Author(s):  
Egwari L. O. ◽  
Oghogho E. S. ◽  
Okwumabua O. E. ◽  
Oniha M. I.
Keyword(s):  
Clostridium Perfringens ◽  
Protein Profile ◽  
Animal Origin ◽  
Cell Protein ◽  
Toxin Gene ◽  
Whole Cell ◽  
University Of Wisconsin ◽  
Gene Type ◽  
Whole Cell Protein ◽  
Gene 4

The spectrum of Clostridium perfringens infections ranges from food toxinosis to myonecrosis. In the current study, whole cell protein and toxin gene types were profiled in 12 randomly selected C. perfringens veterinary stock cultures from the University of Wisconsin, Madison to determine epidemio-logical similarity, or diversity amongst strains of animal origin. Whole cell protein analysis was done by SDS-PAGE while toxin gene typing was achieved by extracting DNA by boiling, DNA concentration and purity was determined by spectrophotometer and nanodrop while separation was carried out by checking it on gel electrophoresis. Multiplex PCR was used to identify the toxigenic gene-type. C. perfringens B and C. perfringens EE with established profiles were used as control strains. Isolates typed included strains cp 296, 309, 12872 (from dogs) and 304, 305, 306, 341, 342, 10754, 12218-2, 12218-3, 12473 (from calves). All 12 strains possess the cpa gene, 4 strains have cpb2, 3 strains etx, 2 strains positive for cpe and 1 for cpb. None of the strains carries the itx gene. Two strains have only cpa gene however no strains has more than two toxin gene types, with cpa-cpb2 combination be-ing more frequent. C. perfringens 305 (etx and cpa) and 342 (cpe and cpa) shared the same protein profile but belong to different toxinotype. It is evi-dent that the cpa gene is a marker for all C. perfringens strains, and similarity in protein profile is not sine qua non for toxin gene type.

Molecular Typing of Lactobacilli Isolated from Dry Sausage “Lukanka”: Comparison of Whole Cell Protein (WCP) Versus DNA-Based Methods

2010 ◽  
Vol 24 (sup1) ◽  
pp. 598-601
Author(s):  
S.G. Dimov ◽  
S. Stojanovski ◽  
R. Stoyanova ◽  
N. Kirilkov ◽  
S. Antonova-Nikolova ◽  
...  
Keyword(s):  
Molecular Typing ◽  
Cell Protein ◽  
Whole Cell ◽  
Whole Cell Protein ◽  
Dry Sausage

scholarly journals  Analysis of whole cell protein profiles of Salmonella serovars isolated from chicken, turkey and sheep faeces by SDS-PAGE

2010 ◽  
Vol 55 (No. 6) ◽  
pp. 259-263 ◽  
Author(s):  
A. Aksakal
Keyword(s):  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Visual Assessment ◽  
Cell Protein ◽  
Protein Profiles ◽  
Whole Cell ◽  
Sds Page ◽  
Molecular Masses ◽  
Whole Cell Protein ◽  
Salmonella Serovars

This study was carried out to determine the whole cell protein profiles of Salmonella serovars from chicken, turkey and sheep faeces by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). A total of 34 Salmonella strains were included in the study, 14 of them were isolated from chicken, 14 from turkey and six from sheep. SDS-PAGE was carried out using 12% (w/v) separating and 4% (w/v) stacking gels. The results showed more than 30 protein bands ranging in size from 97 kDa (kilodaltons) to below 14.4 kDa as determined by visual assessment of their approximate molecular masses. Protein bands of 78.1, 51.2, 41.5, 37.3, 35.1, 33.9, 30.7, 27.6, 25.4, and 24 kDa were detected in all Salmonella serovars. Salmonella strains used in this study were closely related and could not be differentiated depending on the whole cell protein profiles using SDS-PAGE.

Differentiation of species in the Bacillus brevis group and the Bacillus aneurinolyticus group based on the electrophoretic whole-cell protein pattern

1996 ◽  
Vol 70 (1) ◽  
pp. 31-39 ◽  
Author(s):  
Osamu Shida ◽  
Hiroaki Takagi ◽  
Kiyoshi Kadowaki ◽  
Hiroshi Yano ◽  
Kazuo Komagata
Keyword(s):  
Protein Pattern ◽  
Cell Protein ◽  
Bacillus Brevis ◽  
Whole Cell ◽  
Whole Cell Protein
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