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- Acetogenesis (4)
- Acetyl-CoA pathway (4)
- Moorella thermoacetica (4)
- Oxalate (4)
- Acetogenic bacteria (2)
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- Autotrophy (2)
- Bioenergetics (2)
- CO2 fixation (2)
- Clostridium thermoaceticum (2)
- Electron transport (2)
- Nitrate dissimilation (2)
- O-Demethylation (2)
- Thermicanus aegyptius (2)
- Thermophile (2)
- Wood–Ljungdahl pathway (2)
- Characterization (1)
- Development (1)
- Eukaryotic Biomimetic Liposomes (1)
- Regulation (1)
- Review (1)
- Streptococcus pyogenes (1)
- Virulence factors (1)
- Publication
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Articles 1 - 6 of 6
Full-Text Articles in Microbial Physiology
Development And Characterization Of Eukaryotic Biomimetic Liposomes, Bradley Jay Taylor
Development And Characterization Of Eukaryotic Biomimetic Liposomes, Bradley Jay Taylor
All Graduate Theses and Dissertations, Spring 1920 to Summer 2023
This study developed and characterized phospholipid vesicles, or liposomes, that mimic cell surfaces. Microemulsified liposomes contained biotinylated phosphatidylethanolamine, allowing them to be immobilized to avidin-coated glass. Laminin (LN), glycosphingolipids (GMl and GM3), and Escherichia coli's mechanosensitive channel of large conductance (EcoMscL) were embedded into liposome membranes. It was determined whether these embedded molecules exhibited their physiological roles of adhesion, cell recognition, and mechanosensation, respectively. Confocal laser scanning microscopy (CLSM) was employed to examine the interaction of fluorescently probed proteins, toxins, and bacteria with the immobilized microemulsified liposomes. Capture of individual and simultaneous multiple species of bacteria by GMl, GM3, …
Physiology Of The Thermophilic Acetogen Moorella Thermoacetica, Harold L. Drake, Steven L. Daniel
Physiology Of The Thermophilic Acetogen Moorella Thermoacetica, Harold L. Drake, Steven L. Daniel
Faculty Research & Creative Activity
Moorella thermoacetica (originally isolated as Clostridium thermoaceticum) has served as the primary acetogenic bacterium for the resolution of the acetyl coenzyme A (acetyl-CoA) orWood–Ljungdahl pathway, a metabolic pathway that (i) autotrophically assimilates CO2 and (ii) is centrally important to the turnover of carbon in many habitats. The purpose of this article is to highlight the diverse physiological features of this model acetogen and to examine some of the consequences of its metabolic capabilities.
Physiology Of The Thermophilic Acetogen Moorella Thermoacetica, Harold Drake, Steven Daniel
Physiology Of The Thermophilic Acetogen Moorella Thermoacetica, Harold Drake, Steven Daniel
Faculty Research & Creative Activity
Moorella thermoacetica (originally isolated as Clostridium thermoaceticum) has served as the primary acetogenic bacterium for the resolution of the acetyl coenzyme A (acetyl-CoA) orWood–Ljungdahl pathway, a metabolic pathway that (i) autotrophically assimilates CO2 and (ii) is centrally important to the turnover of carbon in many habitats. The purpose of this article is to highlight the diverse physiological features of this model acetogen and to examine some of the consequences of its metabolic capabilities.
Oxalate Metabolism By The Acetogenic Bacterium Moorella Thermoacetica, Steven L. Daniel, Christine Pilsl, Harold L. Drake
Oxalate Metabolism By The Acetogenic Bacterium Moorella Thermoacetica, Steven L. Daniel, Christine Pilsl, Harold L. Drake
Faculty Research & Creative Activity
Whole-cell and cell-extract experiments were performed to study the mechanism of oxalate metabolism in the acetogenic bacterium Moorella thermoacetica. In short-term, whole-cell assays, oxalate consumption was low unless cell suspensions were supplemented with CO2, KNO3, or Na2S2O3. Cell extracts catalyzed the oxalate-dependent reduction of benzyl viologen. Oxalate consumption occurred concomitant to benzyl viologen reduction; when benzyl viologen was omitted, oxalate was not appreciably consumed. Based on benzyl viologen reduction, specific activities of extracts averaged 0.6 μmol oxalate oxidized min−1 mg protein−1. Extracts also catalyzed the formate-dependent reduction of NADP+; however, oxalate-dependent reduction of NADP+ was negligible. Oxalate- or formate-dependent reduction …
Oxalate Metabolism By The Acetogenic Bacterium Moorella Thermoacetica, Steven Daniel, Christine Pilsl, Harold Drake
Oxalate Metabolism By The Acetogenic Bacterium Moorella Thermoacetica, Steven Daniel, Christine Pilsl, Harold Drake
Faculty Research & Creative Activity
Whole-cell and cell-extract experiments were performed to study the mechanism of oxalate metabolism in the acetogenic bacterium Moorella thermoacetica. In short-term, whole-cell assays, oxalate consumption was low unless cell suspensions were supplemented with CO2, KNO3, or Na2S2O3. Cell extracts catalyzed the oxalate-dependent reduction of benzyl viologen. Oxalate consumption occurred concomitant to benzyl viologen reduction; when benzyl viologen was omitted, oxalate was not appreciably consumed. Based on benzyl viologen reduction, specific activities of extracts averaged 0.6 μmol oxalate oxidized min−1 mg protein−1. Extracts also catalyzed the formate-dependent reduction of NADP+; however, oxalate-dependent reduction of NADP+ was negligible. Oxalate- or formate-dependent reduction …
Virulence Factors Of The Group A Streptococci And Genes That Regulate Their Expression, Wayne Hines
Virulence Factors Of The Group A Streptococci And Genes That Regulate Their Expression, Wayne Hines
Biological Sciences Faculty Publications
Group A streptococci produce a wide variety of extracellular (cell-associated and released) virulence factors. The function of these factors varies and includes roles in adhesion, spreading, tissue destruction, immune system evasion, and cell toxicity. How these factors are regulated with regard to one another is important for this organism's ability to bring about the variety of diseases this microbe is capable of causing. Therefore, along with the multitude of virulence factors, there are a number of regulatory systems that regulate, either directly or indirectly, the production of these factors and therefore influence the pathogenesis of group A streptococcal infections.