Evidence map›Paper›PMID 31837192›Full record

ArticlePlant biotechnology journal2020

BGAL1 depletion boosts the level of β-galactosylation of N- and O-glycans in N. benthamiana.

Ricarda Kriechbaum, Esmaiel Ziaee, Clemens Grünwald-Gruber, Pierre Buscaill, Renier A L van der Hoorn, Alexandra Castilho

Open access · goldAbstract read
In one paragraph

Article in Plant biotechnology journal, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
3.5field-weighted citation impact, top 8% 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

23 citing papers in PubMed, 38 citations in OpenAlex.

  1. Article
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  8. Article
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  11. Unexpected Arabinosylation after Humanization of Plant ProteinFrontiers in bioengineering and biotechnology · 2022
    Article
  12. Review
  13. Article
  14. Review
  15. Article
  16. Article
  17. Cracking the "Sugar Code": A Snapshot ofFrontiers in plant science · 2021
    Review
  18. Article
  19. Glycosylation of Plant-Produced Immunoglobulins.Experientia supplementum (2012) · 2021
    Article
  20. Article
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

6 authors at 3 institutions in 3 countries.

Ricarda KriechbaumDepartment of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences, Vienna, Austria.
Esmaiel ZiaeeDepartment of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences, Vienna, Austria.
Clemens Grünwald-GruberDepartment of Chemistry, University of Natural Resources and Life Sciences, Vienna, Austria.
Pierre BuscaillThe Plant Chemetics Laboratory, Department of Plant Sciences, University of Oxford, Oxford, UK.
Renier A L van der HoornThe Plant Chemetics Laboratory, Department of Plant Sciences, University of Oxford, Oxford, UK.ORCID 0000-0002-3692-7487
Alexandra CastilhoDepartment of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences, Vienna, Austria.ORCID 0000-0003-4114-7861
BOKU University · ATUniversity of Oxford · GBShiraz University · IR

Funding

Austrian Science Fund FWF P 31131Austrian Science Fund FWF P31131-B32Biotechnology and Biological Sciences Research Council BB/R017913/1
6 · The paper itself

Abstract

Glyco-design of proteins is a powerful tool in fundamental studies of structure-function relationship and in obtaining profiles optimized for efficacy of therapeutic glycoproteins. Plants, particularly Nicotiana benthamiana, are attractive hosts to produce recombinant glycoproteins, and recent advances in glyco-engineering facilitate customized N-glycosylation of plant-derived glycoproteins. However, with exception of monoclonal antibodies, homogenous human-like β1,4-galactosylation is very hard to achieve in recombinant glycoproteins. Despite significant efforts to optimize the expression of β1,4-galactosyltransferase, many plant-derived glycoproteins still exhibit incomplete processed N-glycans with heterogeneous terminal galactosylation. The most obvious suspects to be involved in trimming terminal galactose residues are β-galactosidases (BGALs) from the glycosyl hydrolase family GH35. To elucidate the so far uncharacterized mechanisms leading to the trimming of terminal galactose residues from glycans of secreted proteins, we studied a N. benthamiana BGAL known to be active in the apoplast (NbBGAL1). Here, we determined the NbBGAL1 subcellular localization, substrate specificity and in planta biological activity. We show that NbBGAL1 can remove β1,4- and β1,3-galactose residues on both N- and O-glycans. Transient BGAL1 down-regulation by RNA interference (RNAi) and BGAL1 depletion by genome editing drastically reduce β-galactosidase activity in N. benthamiana and increase the amounts of fully galactosylated complex N-glycans on several plant-produced glycoproteins. Altogether, our data demonstrate that NbBGAL1 acts on galactosylated complex N-glycans of plant-produced glycoproteins.

Indexed as

NicotianaPolysaccharidesGlycoproteinsGlycosylationHumansRecombinant ProteinsGlycoproteinsPolysaccharidesRecombinant ProteinsCas9CRISPRglyco-engineeringNbBGAL1Nicotiana benthamianaRNAiβ1,4-galactosylationβ-galactosidases

Identifiers

PMID31837192
PMCPMC7292537
OpenAlexW2994646800

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.