Evidence map›Paper›PMID 37804142›Full record

ArticleBiotechnology journal2024

A genome-edited N. benthamiana line for industrial-scale production of recombinant glycoproteins with targeted N-glycosylation.

Benjamin Kogelmann, Stanislav Melnik, Michaela Bogner, Somanath Kallolimath, Eva Stöger, Lin Sun, Richard Strasser, Marc-André D'Aoust, Pierre-Olivier Lavoie, Pooja Saxena and 2 more

Abstract read
In one paragraph

Article in Biotechnology journal, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
–field-weighted citation impact
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

13 citing papers in PubMed.

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  12. Codon optimization regulates IgG3 and IgM expression and glycosylation inFrontiers in bioengineering and biotechnology · 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

12 authors.

Benjamin KogelmannDepartment of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences, Vienna, Austria.ORCID https://orcid.org/0000-0003-4796-6315
Stanislav MelnikDepartment of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences, Vienna, Austria.
Michaela BognerDepartment of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences, Vienna, Austria.
Somanath KallolimathDepartment of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences, Vienna, Austria.
Eva StögerDepartment of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences, Vienna, Austria.ORCID https://orcid.org/0000-0002-7651-7992
Lin SunDepartment of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences, Vienna, Austria.
Richard StrasserDepartment of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences, Vienna, Austria.ORCID https://orcid.org/0000-0001-8764-6530
Marc-André D'AoustMedicago Inc., Quebec, Quebec, Canada.
Pierre-Olivier LavoieMedicago Inc., Quebec, Quebec, Canada.
Pooja SaxenaMedicago Inc., Quebec, Quebec, Canada.
Johannes S GachDivision of Infectious Diseases, University of California, Irvine, Irvine, California, USA.
Herta SteinkellnerDepartment of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences, Vienna, Austria.

Funding

Austrian Centre of Industrial Biotechnology 94032Austrian Science Fund I 3721-B30Austrian Science Fund I 4328-B
6 · The paper itself

Abstract

Control over glycosylation is an important quality parameter in recombinant protein production. Here, we demonstrate the generation of a marker-free genome edited Nicotiana benthamiana N-glycosylation mutant (NbXF-KO) carrying inactivated β1,2-xylosyltransferase and α1,3-fucosyltransferase genes. The knockout of seven genes and their stable inheritance was confirmed by DNA sequencing. Mass spectrometric analyses showed the synthesis of N-glycans devoid of plant-specific β1,2-xylose and core α 1,3-fucose on endogenous proteins and a series of recombinantly expressed glycoproteins with different complexities. Further transient glycan engineering towards more diverse human-type N-glycans resulted in the production of recombinant proteins decorated with β1,4-galactosylated and α2,6-sialylated structures, respectively. Notably, a monoclonal antibody expressed in the NbXF-KO displayed glycosylation-dependent activities. Collectively, the engineered plants grow normally and are well suited for upscaling, thereby meeting industrial and regulatory requirements for the production of high-quality therapeutic proteins.

Indexed as

GlycoproteinsUDP Xylose-Protein XylosyltransferaseGlycosylationHumansPlants, Genetically ModifiedPolysaccharidesRecombinant ProteinsGlycoproteinsPolysaccharidesRecombinant ProteinsUDP Xylose-Protein XylosyltransferaseCRISPR/Cas9fucoseN-glycan engineeringNicotiana benthamianarecombinant glycoproteins

Identifiers

PMID37804142
PMCPMC11475529

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.