Evidence map›Paper›PMID 32244994›Full record

ArticleInternational journal of molecular sciences2020

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.

Collin Jugler, Jussi Joensuu, Qiang Chen

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.7field-weighted citation impact, top 11% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

17 citing papers in PubMed, 25 citations in OpenAlex.

  1. Review
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  9. Development of Antibody-Based Therapeutics Against West Nile Virus in Plants.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 2 institutions in 2 countries.

Collin JuglerThe Biodesign Institute and School of Life Sciences, Arizona State University, Mail Zone 5401, 1001 S. McAllister Avenue, Tempe, AZ 85287, USA.
Jussi JoensuuVTT Technical Research Centre of Finland Ltd, Espoo, Finland.
Qiang ChenThe Biodesign Institute and School of Life Sciences, Arizona State University, Mail Zone 5401, 1001 S. McAllister Avenue, Tempe, AZ 85287, USA.ORCID 0000-0003-1498-7013
Arizona State University · USVTT Technical Research Centre of Finland · FI

Funding

Bifunctional antibodies with targeted CNS delivery against West Nile VirusR33AI101329 · NIAID · ARIZONA STATE UNIVERSITY-TEMPE CAMPUS · PI CHEN, QIANG · 2014 to 2016
$1.3M
Division of Intramural Research, National Institute of Allergy and Infectious Diseases R33AI101329NIAID NIH HHS R33 AI101329
6 · The paper itself

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.

Indexed as

Antibodies, MonoclonalEpitopesFungal ProteinsNicotianaPlant ExtractsPlants, Genetically ModifiedRecombinant Fusion ProteinsStaphylococcal Protein AWaterWest Nile virusAntibodies, MonoclonalEpitopesFungal ProteinsPlant ExtractsRecombinant Fusion ProteinsStaphylococcal Protein AWateraqueous two-phase separation (ATPS)hydrophobinmonoclonal antibody (mAb)plant-made antibodyWest Nile virus

Identifiers

PMID32244994
PMCPMC7139538
OpenAlexW3010748240

What OpenQuestion holds

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LicenceCC BY
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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.