Expression, glycosylation, and function of an anti-rabies virus monoclonal antibody in tobacco and Arabidopsis plants
- 13 Downloads
Plants have emerged as one of the most attractive systems for producing human therapeutic proteins against viral diseases. These include diagnostic reagents, vaccines, and antibodies. This process is known as molecular biofarming. The objective of this study was to develop and evaluate tobacco and Arabidopsis as plant platforms for producing human anti-rabies monoclonal antibody (mAb). Both tobacco and Arabidopsis transgenic plants were generated by Agrobacterium-mediated transformation. Purification of mAb SO57K from each plant was performed with ammonium sulfate-mediated precipitation and protein A affinity columns. SDS–PAGE analysis showed that the purity of mAb SO57K obtained from each transgenic plant was similar, whereas Arabidopsis showed approximately twofold greater protein expression than tobacco. The N-glycosylation was not significantly different between proteins from the two plant species, with both showing oligo-mannose glycan structures. The mAbs SO57 derived from both the model plants had similar neutralizing efficacy against target virus strain CVS-11. Taken together, tobacco and Arabidopsis are both promising platforms for producing a human anti-rabies mAb.
KeywordsMolecular biofarming Platform Tobacco Arabidopsis Transgenic plant Anti-rabies monoclonal antibody Neutralizing efficacy
This research was supported by the Chung-Ang University Research Scholarship Grants in 2015 and the Korean Rural Administration (Grant Code # PJ011110).
- Lee JH, Park DY, Lee KJ, Kim YK, So YK, Ryu JS, Oh SH, Han YS, Ko K et al (2013) Intracellular reprogramming of expression, glycosylation, and function of a plant-derived antiviral therapeutic monoclonal antibody. PLoS ONE 8:e68772. https://doi.org/10.1371/journal.pone.0068772 CrossRefPubMedPubMedCentralGoogle Scholar
- Triguero A, Cabrera G, Cremata JA, Yuen CT, Wheeler J, Ramirez NI (2005) Plant-derived mouse IgG monoclonal antibody fused to KDEL endoplasmic reticulum-retention signal is N-glycosylated homogeneously throughout the plant with mostly high-mannose-type N-glycans. Plant Biotechnol J 3:449–457. https://doi.org/10.1111/j.1467-7652.2005.00137.x CrossRefPubMedGoogle Scholar