Exploiting the natural variation of Arabidopsis thaliana for the seed-specific production of proteins
2012
The seed-specific expression of recombinant proteins in transgenic plants offers several interesting advantages over other production platforms. The aim of this study was to select accessions of Arabidopsis thaliana with the highest potential as a platform for seed-specific production of recombinant proteins. A. thaliana was chosen because of its flexibility, high seed yield per m², high natural protein content and its non-food status. Seven characteristics were measured for 96 accessions; days to first flower bud, days to complete senescence, rosette size, number of main bolts, dry biomass of plant, seed yield and protein content of seeds. Three characteristics (length of life cycle, seed yield and protein content) were used to select accessions with a maximal yield. A variation of length of life cycle between 87 ± 11 days (Ler-1) and more than 200 days (several accessions) was registered. Seed yields per accession varied between 18 ± 16 mg (Wa-1) and 274 ± 76 mg (Mr-0). Protein content ranged between 30% (Ws-2) and 38% (Cvi-0). Based on the results of this study, accession Nok-3 is selected as the accession best suited for exploitation as a seed-based platform for the production of recombinant proteins. Nok-3 has a high seed yield (194 ± 66 mg) combined with a moderate protein content of 34.8% and short life cycle of 126 ± 17 days, resulting in a calculated protein yield per year three times higher than reference accession Col-0. In conclusion, this study illustrates the unexploited variability present in the Arabidopsis gene pool that can be used directly for further optimization of Arabidopsis seeds as production platform. In combination with A. thaliana’s rapid life cycle, flexibility, and high fertility, this makes it an attractive platform for the production of specific groups of recombinant proteins, such as high-purity products produced on a relatively small scale.
Keywords:
- Correction
- Source
- Cite
- Save
- Machine Reading By IdeaReader
39
References
2
Citations
NaN
KQI