Solid-phase microbead array for multiplex O-serotyping of Escherichia coli

2017 ◽  
Vol 184 (5) ◽  
pp. 1405-1415 ◽  
Author(s):  
Claudia Liebsch ◽  
Stefan Rödiger ◽  
Alexander Böhm ◽  
Jörg Nitschke ◽  
Jörg Weinreich ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Solid Phase ◽  
Microbead Array

scholarly journals Recent Progress on the Electrochemical Biosensing of Escherichia coli O157:H7: Material and Methods Overview

Biosensors ◽  
2020 ◽  
Vol 10 (5) ◽  
pp. 54 ◽  
Author(s):  
Nasrin Razmi ◽  
Mohammad Hasanzadeh ◽  
Magnus Willander ◽  
Omer Nur
Keyword(s):  
Escherichia Coli ◽  
Pathogen Detection ◽  
Recent Progress ◽  
Electrochemical Sensors ◽  
Solid Phase ◽  
Great Promise ◽  
Escherichia Coli O157 ◽  
E Coli ◽  
Electrochemical Biosensing ◽  
Sensitivity And Selectivity

Escherichia coli O157:H7 (E. coli O157:H7) is a pathogenic strain of Escherichia coli which has issued as a public health threat because of fatal contamination of food and water. Therefore, accurate detection of pathogenic E. coli is important in environmental and food quality monitoring. In spite of their advantages and high acceptance, culture-based methods, enzyme-linked immunosorbent assays (ELISAs), polymerase chain reaction (PCR), flow cytometry, ATP bioluminescence, and solid-phase cytometry have various drawbacks, including being time-consuming, requiring trained technicians and/or specific equipment, and producing biological waste. Therefore, there is necessity for affordable, rapid, and simple approaches. Electrochemical biosensors have shown great promise for rapid food- and water-borne pathogen detection. Over the last decade, various attempts have been made to develop techniques for the rapid quantification of E. coli O157:H7. This review covers the importance of E. coli O157:H7 and recent progress (from 2015 to 2020) in the development of the sensitivity and selectivity of electrochemical sensors developed for E. coli O157:H7 using different nanomaterials, labels, and electrochemical transducers.

scholarly journals The Escherichia coli glucuronylsynthase promoted synthesis of steroid glucuronides: improved practicality and broader scope

2014 ◽  
Vol 12 (32) ◽  
pp. 6208-6214 ◽  
Author(s):  
Paul Ma ◽  
Nicholas Kanizaj ◽  
Shu-Ann Chan ◽  
David L. Ollis ◽  
Malcolm D. McLeod
Keyword(s):  
Escherichia Coli ◽  
Solid Phase Extraction ◽  
Solid Phase ◽  
Phase Extraction ◽  
E Coli

Steroid glucuronides can be quickly and conveniently prepared on the milligram scale using theE. coliglucuronylsynthase enzyme followed by purification with solid-phase extraction.

scholarly journals Microtiter solid-phase radioimmunoassay for detection of Escherichia coli heat-labile enterotoxin.

1977 ◽  
Vol 17 (3) ◽  
pp. 541-545 ◽  
Author(s):  
H B Greenberg ◽  
D A Sack ◽  
W Rodriguez ◽  
R B Sack ◽  
R G Wyatt ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Solid Phase ◽  
Heat Labile ◽  
Solid Phase Radioimmunoassay

scholarly journals Tracking Bacterial Spoilage in Cosmetics by a New Bioanalytical Approach: API-SPME-GC-MS to Monitor MVOCs

Cosmetics ◽  
2020 ◽  
Vol 7 (2) ◽  
pp. 38
Author(s):  
Maria Celeiro ◽  
Esther Varela ◽  
Rocio Rodriguez ◽  
Manuel Penedo ◽  
Marta Lores
Keyword(s):  
Escherichia Coli ◽  
Pseudomonas Aeruginosa ◽  
Proteus Mirabilis ◽  
Solid Phase ◽  
Gas Chromatography Mass Spectrometry ◽  
Practical Application ◽  
Biochemical Tests ◽  
Volatile Organic ◽  
Microbial Volatile Organic Compounds ◽  
Original Approach

The main goal of this work was the use of the powerful solid-phase microextraction-gas chromatography-mass spectrometry (SPME-GC-MS) technique to unequivocally identify microbial volatile organic compounds (MVOCs) derived from the enzymatic activity produced during metabolic processes using analytical profile index (API) biochemical tests. Three bacteria were selected for this study: Escherichia coli, Proteus mirabilis, and Pseudomonas aeruginosa. They were inoculated and incubated to both API components and real cosmetics, as well as to a mixture of them. Specific MVOCs were successfully identified as biomarkers for each one of the studied microorganisms: Indole and 2-nitrophenol as Escherichia coli markers, 2-undecanone and phenylethyl alcohol as Proteus mirabilis-specific markers, and 1-undecene and 2′-aminoacetophenone as Pseudomonas aeruginosa ones. In addition, a high number of MVOCs were identified as general markers of bacterial presence. The results revealed that the MVOCs’ formation is highly subtract dependent. Therefore, the ultimate and most challenging objective is to establish a relationship between the identified MVOCs and the original compound present in the substrate. This work establishes the design and development of this original approach, and its practical application to the control of microbial contamination in real cosmetic samples.

Production and solid-phase refolding of human glucagon-like peptide-1 using recombinant Escherichia coli

2011 ◽  
Vol 78 (2) ◽  
pp. 197-203 ◽  
Author(s):  
Sung-Gun Kim ◽  
So-Yeon Shin ◽  
Yong-Cheol Park ◽  
Chul-Soo Shin ◽  
Jin-Ho Seo
Keyword(s):  
Escherichia Coli ◽  
Solid Phase ◽  
Recombinant Escherichia Coli ◽  
Glucagon Like Peptide ◽  
Glucagon Like Peptide 1

Characteristics and clinical application of a radiometric Escherichia coli-based phospholipase A2 assay modified for serum analysis

1993 ◽  
Vol 39 (4) ◽  
pp. 605-613 ◽  
Author(s):  
J Aufenanger ◽  
W Zimmer ◽  
R Kattermann
Keyword(s):  
Escherichia Coli ◽  
Fatty Acids ◽  
Oleic Acid ◽  
Phospholipase A2 ◽  
Human Serum ◽  
Solid Phase ◽  
Pla2 Activity ◽  
E Coli ◽  
Human Sera

Abstract Determination of activities of phospholipase A2 (PLA2) in human sera was based on the hydrolysis of phospholipids from [1-14C]oleic acid-labeled Escherichia coli biomembranes. The E. coli membranes served as substrate specifically for the PLA2 of human serum and were essentially resistant to other lipases in human sera, i.e., lipoprotein lipases, hepatic triacylglycerolipase, or pancreatic lipase in acute pancreatitis. Exchange of phospholipids between the serum and the biomembrane compartment aggravates the determination of PLA2 activity in human serum, which is naturally rich in phospholipids. In our modified E. coli assay, which overcomes these difficulties, the main substrate components phosphatidylethanolamine (70%) and cardiolipin (25%) were > 90% labeled in the sn-2 position. Fatty acids released by PLA2 activity were eluted from an aminopropyl solid-phase column directly into scintillation vials, where the radioactivity was counted. The ratio of [1-14C]oleic acid to released total fatty acids was used to calculate true enzymatic activity. The linear assay range extended from 0 to 3.6 U/L (0-60 nkat/L), with a detection limit of < 0.03 U/L (< 0.5 nkat/L). Within-assay imprecision (CV) was < 6% and between-assay is < 10% over the whole activity range. The normal range for men was 0-0.44 U/L (0-7.33 nkat/L) and for women 0.044-1.11 U/L (0.73-18.4 nkat/L). Patients with septicemia, pancreatitis, acute respiratory distress syndrome, or other severe diseases had PLA2 values up to 540 U/L (9000 nkat/L).

scholarly journals Receptor Structure for F1C Fimbriae of Uropathogenic Escherichia coli

2000 ◽  
Vol 68 (6) ◽  
pp. 3541-3547 ◽  
Author(s):  
A. Salam Khan ◽  
Bernhard Kniep ◽  
Tobias A. Oelschlaeger ◽  
Irma Van Die ◽  
Timo Korhonen ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Solid Phase ◽  
Binding Assays ◽  
E Coli ◽  
High Affinity ◽  
Receptor Structure ◽  
Microtiter Plates ◽  
Bacterial Interaction ◽  
Solid Phase Binding ◽  
Time Specific

ABSTRACT F1C fimbriae are correlated with uropathogenic Escherichia coli strains. Although F1C fimbriae mediate binding to kidney tubular cells, their receptor is not known. In this paper, we demonstrate for the first time specific carbohydrate residues as receptor structure for F1C-fimbria-expressing E. coli. The binding of the F1C fimbriated recombinant E. coli strain HB101(pPIL110-54) and purified F1C fimbriae to reference glycolipids of different carbohydrate compositions was evaluated by using thin-layer chromatography (TLC) overlay and solid-phase binding assays. TLC fimbrial overlay analysis revealed the binding ability of purified F1C fimbriae only to glucosylceramide (GlcCer), β1-linked galactosylceramide 2 (GalCer2) with nonhydroxy fatty acids, lactosylceramide, globotriaosylceramide, paragloboside (nLc4Cer), lactotriaosylceramide, gangliotriaosylceramide (asialo-GM2 [GgO3Cer]) and gangliotetraosylceramide (asialo-GM1[GgO4Cer]). The binding of purified F1C fimbriae as well as F1C fimbriated recombinant E. coli strain HB101(pPIL110-54) was optimal to microtiter plates coated with asialo-GM2 (GgO3Cer). The bacterial interaction with asialo-GM1 (GgO4Cer) and asialo-GM2 (GgO3Cer) was strongly inhibited only by disaccharide GalNAcβ1-4Galβ linked to bovine serum albumin. We observed no binding to globotetraosylceramide or Forssman antigen (Gb5Cer) glycosphingolipids or to sialic-acid-containing gangliosides. It was demonstrated that the presence of a GalCer or GlcCer residue alone is not sufficient for optimal binding, and additional carbohydrate residues are required for high-affinity adherence. Indeed, the binding efficiency of F1C fimbriated recombinant bacteria increased by 19-fold when disaccharide sequence GalNAcβ1-4Galβ is linked to glucosylceramide as in asialo-GM2 (GgO3Cer). Thus, it is suggested that the disaccharide sequence GalNAcβ1-4Galβ of asialo-GM2 (GgO3Cer) which is positioned internally in asialo-GM1 (GgO4Cer) is the high-affinity binding epitope for the F1C fimbriae of uropathogenicE. coli.

Sign in / Sign up

Export Citation Format

Share Document