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• W3010748240 endingPage "2140" @default.
• W3010748240 startingPage "2140" @default.
• W3010748240 abstract "The development of monoclonal antibodies (mAbs) has provided vast opportunities to treat a wide range of diseases from cancer to viral infections. While plant-based production of mAbs has effectively lowered the upstream cost of mAb production compared to mammalian cell cultures, further optimization of downstream processing, especially in extending the longevity of Protein A resin by an effective bulk separation step, will further reduce the overall prohibitive cost of mAb production. In this study, we explored the feasibility of using aqueous two-phase separation (ATPS) in capturing and separating plant-made mAbs from host proteins. Our results demonstrated that an anti-West Nile virus mAb (E16) was efficiently separated from most plant host proteins by a single ATPS step, comprising the mixing of plant extracts containing Hydrophobin-Protein A fusion protein (HPA) and E16 and the subsequent incubation with an inexpensive detergent. This simple ATPS step yielded a highly enriched E16 mAb preparation with a recovery rate comparable to that of Protein A chromatography. The ATPS-enriched E16 retained its structural integrity and was fully functional in binding its target antigen. Notably, HPA-based ATPS was also effective in enriching E16 from plant host proteins when both HPA and E16 were produced in the same leaves, supporting the potential of further streamlining the downstream purification process. Thus, ATPS based on plant-produced HPA in unpurified extract is a cost-effective yet efficient initial capture step for purifying plant-made mAbs, which may significantly impact the approach of mAb purification." @default.
• W3010748240 created "2020-03-23" @default.
• W3010748240 creator A5035961174 @default.
• W3010748240 creator A5068756299 @default.
• W3010748240 creator A5072549740 @default.
• W3010748240 date "2020-03-20" @default.
• W3010748240 modified "2023-09-28" @default.
• W3010748240 title "Hydrophobin-Protein A Fusion Protein Produced in Plants Efficiently Purified an Anti-West Nile Virus Monoclonal Antibody from Plant Extracts via Aqueous Two-Phase Separation" @default.
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• W3010748240 doi "https://doi.org/10.3390/ijms21062140" @default.
• W3010748240 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/7139538" @default.
• W3010748240 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/32244994" @default.
• W3010748240 hasPublicationYear "2020" @default.
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