Dr David Bringloe
Lecturer
Department of Bioscience , School Of Health, Sport And Bioscience
After obtaining a BSc and PhD in molecular biology, I dedicated several years to roles as a researcher and lecturer at institutions in both London and the USA. My primary research expertise lies in the genetic manipulation of genomes for the production of human therapeutic enzymes. Currently, at UEL, I instruct students at both undergraduate and postgraduate levels, with a primary focus on Biochemistry and Biotechnology.
Qualifications
- BSc, PhD, FHEA
Areas Of Interest
- Expression of foreign genes in yeast and plants.
- Plant Molecular Biology
- Plant Biotechnology
- Biotechnology
- Molecular Genetics
OVERVIEW
My current research interests include designing approaches for foreign gene expression in plant systems. Our plant-based strategies are aimed at expressing various human therapeutic enzymes at high levels in whole plants and plant cell suspensions. The genetic manipulation of plant genomes for the production of human proteins stands at the forefront of biotechnology innovation. This transformative process involves the precise insertion of human genes into plant DNA, equipping plant cells with the capability to produce specific therapeutic proteins. By harnessing the plant's natural protein synthesis machinery, it’s possible to cultivate plants that serve as living bioreactors, churning out vital human proteins (enzymes, hormones, antibodies and vaccines) with remarkable efficiency and scalability.
This approach not only offers a sustainable and cost-effective means of protein production but also provides an avenue for the development of life-saving therapies, vaccines, and diagnostics. Genetic manipulation of plant genomes represents a promising frontier in the quest to harness the potential of nature's biofactories for the benefit of human health and medicine.
CURRENT RESEARCH
Human adenosine deaminase (ADA) catalyses the conversion of metabolites, adenosine and deoxyadenosine, to inosine and deoxyinosine. In the genetic disorder, ADA deficiency, these metabolites reach toxic levels in the plasma. They are then taken up by lymphoid progenitors causing impairment of T-cell development and hence immunodeficiency. One treatment for this disease is ADA enzyme-replacement therapy, which supplies exogenous bovine ADA through twice-weekly intramuscular injections of a polyethylene glycol-conjugate (PEG-ADA). The cost of treatment, however, is prohibitively high, therefore a cheaper alternative source of a recombinant form of human ADA would therefore be expedient. In terms of practicality, economy and safety plants have many advantages over other systems for the production of recombinant proteins, where nuclear transformation is broadly used for production of recombinant proteins which are generally extracted from leaves.
Most recent research
PUBLICATIONS
- Singhabahu S., George J., Bringloe D. (2015) High-yield production of apoplast-directed human adenosine deaminase in transgenic tobacco BY-2 cell suspensions. Biotechnology and Applied Biochemistry 62, 87-93.
- Crop Biotech Update (2013) 'Expression of ADA in biotech tobacco plants' 23 January. International Service for the Acquisition of Agri-biotech Applications [Online]. Available at: https://www.isaaa.org/kc/cropbiotechupdate/newsletter/default.asp?Date=1/23/2013(Accessed: 26 March 2013).
- Singhabahu S., George J., and Bringloe D. (2013) Expression of a functional human adenosine deaminase in transgenic tobacco plants. Transgenic Research 22, 643-649.
TEACHING
MODULES
- BS5101 Molecular Biology and Genetics
- BS5102 Principles of Biotechnology
- BS6102 DNA Analysis and Bioinformatics
- BS6117 Applications of Biotechnology
COURSES
- BSc Biochemistry and Biotechnology
- BSc Biomedical Science
- MSc Biomedical Science
INDUSTRY PARTNERS
Publications
The last four years of publications can be viewed below.
Full publications list
Visit the research repository to view a full list of publications
- High-yield production of apoplast-directed human adenosine deaminase in transgenic tobacco BY-2 cell suspensions Biotechnology and Applied Biochemistry. 62 (1), pp. 87-93. https://doi.org/10.1002/bab.1240