Evidence map›Paper›PMID 29969180›Full record

ArticlePlant biotechnology journal2019

CRISPR/Cas9-mediated knockout of six glycosyltransferase genes in Nicotiana benthamiana for the production of recombinant proteins lacking β-1,2-xylose and core α-1,3-fucose.

Julia Jansing, Markus Sack, Sruthy Maria Augustine, Rainer Fischer, Luisa Bortesi

Open access · goldAbstract read
In one paragraph

Article in Plant biotechnology journal, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 102 papers.

0numbers the graph read from it
0cells of the map it votes in
102citing papers in PubMed
14.6field-weighted citation impact, top 1% 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

102 citing papers in PubMed, 195 citations in OpenAlex.

  1. Review
  2. Plant-Based Systems for Producing Therapeutic Proteins: Current Status and Future Prospects.BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy · 2026
    Review
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  10. Review
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  13. Metabolic engineering inaBIOTECH · 2025
    Review
  14. Review
  15. Review
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  17. Review
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  20. Article

42 more citing papers are in PubMed but not listed here.

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

5 authors at 1 institution in 1 country.

Julia JansingDepartment for Molecular Biotechnology, RWTH Aachen University, Aachen, Germany.ORCID 0000-0003-2339-0083
Markus SackDepartment for Molecular Biotechnology, RWTH Aachen University, Aachen, Germany.ORCID 0000-0002-7380-9228
Sruthy Maria AugustineDepartment for Molecular Biotechnology, RWTH Aachen University, Aachen, Germany.
Rainer FischerDepartment for Molecular Biotechnology, RWTH Aachen University, Aachen, Germany.
Luisa BortesiDepartment for Molecular Biotechnology, RWTH Aachen University, Aachen, Germany.
RWTH Aachen University · DE

Funding

ERC 269110German federal and state governments
6 · The paper itself

Abstract

Plants offer fast, flexible and easily scalable alternative platforms for the production of pharmaceutical proteins, but differences between plant and mammalian N-linked glycans, including the presence of β-1,2-xylose and core α-1,3-fucose residues in plants, can affect the activity, potency and immunogenicity of plant-derived proteins. Nicotiana benthamiana is widely used for the transient expression of recombinant proteins so it is desirable to modify the endogenous N-glycosylation machinery to allow the synthesis of complex N-glycans lacking β-1,2-xylose and core α-1,3-fucose. Here, we used multiplex CRISPR/Cas9 genome editing to generate N. benthamiana production lines deficient in plant-specific α-1,3-fucosyltransferase and β-1,2-xylosyltransferase activity, reflecting the mutation of six different genes. We confirmed the functional gene knockouts by Sanger sequencing and mass spectrometry-based N-glycan analysis of endogenous proteins and the recombinant monoclonal antibody 2G12. Furthermore, we compared the CD64-binding affinity of 2G12 glycovariants produced in wild-type N. benthamiana, the newly generated FX-KO line, and Chinese hamster ovary (CHO) cells, confirming that the glyco-engineered antibody performed as well as its CHO-produced counterpart.

Indexed as

AnimalsAntibodies, MonoclonalBroadly Neutralizing AntibodiesCHO CellsCricetulusCRISPR-Cas SystemsFucoseFucosyltransferasesGene EditingGene Knockout TechniquesGlycosylationHIV AntibodiesMolecular FarmingNicotianaPentosyltransferasesPlant Proteins2G12 monoclonal antibodyAntibodies, MonoclonalBroadly Neutralizing AntibodiesFucoseFucosyltransferasesgalactoside 3-fucosyltransferaseHIV AntibodiesPentosyltransferasesPlant ProteinsPolysaccharidesRecombinant ProteinsUDP Xylose-Protein XylosyltransferaseXyloseCRISPR/Cas9gene knockoutglyco-engineeringmolecular farmingα-1,3-fucosyltransferaseβ-1,2-xylosyltransferase

Identifiers

PMID29969180
PMCPMC6335070
OpenAlexW2810726554

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

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.