Authors: P Pillay T Kibido M du Plessis C van der Vyver G Beyene B J Vorster K J Kunert U Schlüter
Publish Date: 2012/09/11
Volume: 168, Issue: 6, Pages: 1608-1620
Abstract
Plants are an effective and inexpensive host for the production of commercially interesting heterologous recombinant proteins The Escherichia coliderived glutathione reductase was transiently expressed as a recombinant model protein in the cytosol of tobacco plants using the technique of leaf agroinfiltration Proteolytic cysteine protease activity progressively increased over time when glutathione reductase accumulated in leaves Application of cysteine protease promoter–GUS fusions in transgenic tobacco identified a cysteine protease NtCP2 expressed in mature leaves and being stress responsive to be expressed as a consequence of agroinfiltration Transgenic tobacco plants constitutively expressing the rice cysteine protease inhibitor oryzacystatinI had significantly lower cysteine protease activity when compared to nontransgenic tobacco plants Lower cysteine protease activity in transgenic plants was directly related to higher glutathione reductase activity and also higher glutathione reductase amounts in transgenic plants Overall our work has demonstrated as a novel aspect that transgenic tobacco plants constitutively expressing an exogenous cysteine protease inhibitor have the potential for producing more recombinant protein which is very likely due to the reduced activity of endogenous cysteine protease
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