Characterisation of strains of Aeromonas spp. by phenotype and whole-cell protein fingerprint

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.

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Characterization of Pseudomonas Syringae pv. actinidiae,The Causal Agent of Bacterial Canker of Kiwifruit by Whole Cell Protein Electrophoresis and Fatty Acid Analysis.

Developments in Plant Pathology - Pseudomonas Syringae Pathovars and Related Pathogens ◽

10.1007/978-94-011-5472-7_90 ◽

1997 ◽

pp. 499-499

Author(s):

Jaap D. Janse ◽

Marco Scortichini

Keyword(s):

Fatty Acid ◽

Pseudomonas Syringae ◽

Fatty Acid Analysis ◽

Protein Electrophoresis ◽

Causal Agent ◽

Cell Protein ◽

Bacterial Canker ◽

Whole Cell ◽

Whole Cell Protein

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

International Journal of Applied Sciences and Biotechnology ◽

10.3126/ijasbt.v2i4.11253 ◽

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

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

Biotechnology & Biotechnological Equipment ◽

10.1080/13102818.2010.10817905 ◽

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

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

Veterinární Medicína ◽

10.17221/2986-vetmed ◽

2010 ◽

Vol 55 (No. 6) ◽

pp. 259-263 ◽

Cited By ~ 6

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.

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