The Ability of a Recombinant Escherichia coli Strain to Synthesize 2-C-Methyl-D-Erythritol-2,4-Cyclopyrophosphate Correlates with Its Tolerance to In Vitro Induced Oxidative Stress and to the Bactericidal Action of Murine Peritoneal Macrophages

1996 ◽  
Vol 32 (4) ◽  
pp. 225-228 ◽  
Author(s):  
Olga D. Ogrel ◽  
Konstantin V. Fegeding ◽  
Elena F. Kharatian ◽  
Andrew B. Sudarikov ◽  
Dmitry N. Ostrovsky
Keyword(s):  
Oxidative Stress ◽  
Escherichia Coli ◽  
Peritoneal Macrophages ◽  
Coli Strain ◽  
Recombinant Escherichia Coli ◽  
Bactericidal Action ◽  
Murine Peritoneal Macrophages

scholarly journals Evaluation of biological safety in vitro and immunogenicity in vivo of recombinant Escherichia coli Shiga toxoids as candidate vaccines in cattle

2015 ◽  
Vol 46 (1) ◽  
Author(s):  
Katharina Kerner ◽  
Philip S Bridger ◽  
Gabriele Köpf ◽  
Julia Fröhlich ◽  
Stefanie Barth ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Recombinant Escherichia Coli ◽  
Biological Safety

BIOSYNTHESIS OF BUTYRIC ACID FROM GLUCOSE THROUGH THE INVERTED FATTY ACID BETA-OXIDATION PATHWAY BY RECOMBINANT ESCHERICHIA COLI STRAIN IN BIOCATALYTIC MODE DUE TO ENFORCED ATP HYDROLYSIS

2021 ◽  
Vol 1 (19) ◽  
pp. 268-269
Author(s):  
A.Yu. Skorokhodova ◽  
V.G. Debabov
Keyword(s):  
Escherichia Coli ◽  
Fatty Acid ◽  
Butyric Acid ◽  
Atp Hydrolysis ◽  
Coli Strain ◽  
Recombinant Escherichia Coli ◽  
Beta Oxidation ◽  
Oxidation Pathway ◽  
Full Cell ◽  
Fatty Acid Beta Oxidation

The feasibility of the application of enforced ATP hydrolysis to ensure anaerobic functioning of Escherichia coli strain producing butyric acid through the inverted fatty acid beta-oxidation pathway as a full-cell biocatalyst has been demonstrated.

Immunocytochemical Analysis of Murine Peritoneal Macrophages Treated with “Poly-Plat”, an in Vitro and in Vivo Study

1998 ◽  
Vol 4 (S2) ◽  
pp. 1122-1123
Author(s):  
H. J. Muenchen ◽  
S.K. Aggarwal
Keyword(s):  
Immune System ◽  
Mechanism Of Action ◽  
Second Generation ◽  
Peritoneal Macrophages ◽  
In Vivo Study ◽  
Immunocytochemical Analysis ◽  
Murine Peritoneal Macrophages

Poly-[(trans-1,2-diaminocyclohexane) platinumj-carboxyamylose (“poly-plat“) is a second generation analog of cisplatin which enhances the immune system with greater efficacy in vitro and in vivo “Poly-plat” contains 1/5 the platinum of CDDP and demonstrates less toxicity. In order to understand the mechanism of action of this compound an in vitro and in vivo study was performed. Swiss Webster mice and isolated murine peritoneal macrophages were treated with “poly-plat” (10 mg/kg). The Swiss Webster mice were given bolus injections and sacrificed at 2 and 12 days. Peritoneal macrophages were then isolated and allowed to incubate in culture for 24 h. Peritoneal macrophages were also isolated from normal mice and treated with the drugs for 2 h. After treatments the macrophages were placed in fresh media and allowed to incubate 24 h. Supematants were isolated at various times during culture for immunocytochemical analysis.Both in vitro and in vivo studies showed enhanced immunostimulation after their respective treatments.

scholarly journals SodA Contributes to the Virulence of Avian PathogenicEscherichia coliO2 Strain E058 in Experimentally Infected Chickens

2019 ◽  
Vol 201 (6) ◽  
Author(s):  
Qingqing Gao ◽  
Le Xia ◽  
Xiaobo Wang ◽  
Zhengqin Ye ◽  
Jinbiao Liu ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Escherichia Coli ◽  
Hydrogen Peroxide ◽  
Virulence Factor ◽  
Infection Process ◽  
Strain Identification ◽  
Bacterial Disease ◽  
Wild Type ◽  
Content Type

ABSTRACTStrains of avian pathogenicEscherichia coli(APEC), the common pathogen of avian colibacillosis, encounter reactive oxygen species (ROS) during the infection process. Superoxide dismutases (SODs), acting as antioxidant factors, can protect against ROS-mediated host defenses. Our previous reports showed that thesodAgene (encoding a Mn-cofactor-containing SOD [MnSOD]) is highly expressed during the septicemic infection process of APEC.sodAhas been proven to be a virulence factor of certain pathogens, but its role in the pathogenicity of APEC has not been fully identified. In this study, we deleted thesodAgene from the virulent APEC O2 strain E058 and examined thein vitroandin vivophenotypes of the mutant. ThesodAmutant was more sensitive to hydrogen peroxide in terms of both its growth and viability than was the wild type. The ability to form a biofilm was weakened in thesodAmutant. ThesodAmutant was significantly more easily phagocytosed by chicken macrophages than was the wild-type strain. Chicken infection assays revealed significantly attenuated virulence of thesodAmutant compared with the wild type at 24 h postinfection. The virulence phenotype was restored by complementation of thesodAgene. Quantitative real-time reverse transcription-PCR revealed that the inactivation ofsodAreduced the expression of oxidative stress response geneskatE,perR, andosmCbut did not affect the expression ofsodBandsodC. Taken together, our studies indicate that SodA is important for oxidative resistance and virulence of APEC E058.IMPORTANCEAvian colibacillosis, caused by strains of avian pathogenicEscherichia coli, is a major bacterial disease of severe economic significance to the poultry industry worldwide. The virulence mechanisms of APEC are not completely understood. This study investigated the influence of an antioxidant protein, SodA, on the phenotype and pathogenicity of APEC O2 strain E058. This is the first report demonstrating that SodA plays an important role in protecting a specific APEC strain against hydrogen peroxide-induced oxidative stress and contributes to the virulence of this pathotype strain. Identification of this virulence factor will enhance our knowledge of APEC pathogenic mechanisms, which is crucial for designing successful strategies against associated infections and transmission.

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