Evidence map›Paper›PMID 19882694›Full record

ArticleBiotechnology progress

Identification of genes encoding N-glycan processing beta-N-acetylglucosaminidases in Trichoplusia ni and Bombyx mori: Implications for glycoengineering of baculovirus expression systems.

Christoph Geisler, Donald L Jarvis

Open access · greenAbstract read
In one paragraph

Article in Biotechnology progress. 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
0.7field-weighted citation impact, top 32% 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

13 citing papers in PubMed, 24 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. The Role of ChitooligosaccharidolyticInternational journal of molecular sciences · 2022
    Article
  5. Review
  6. Review
  7. CRISPR-Cas9 vectors for genome editing and host engineering in the baculovirus-insect cell system.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  8. The underestimated N-glycomes of lepidopteran species.Biochimica et biophysica acta. General subjects · 2017
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
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

2 authors at 1 institution in 1 country.

Christoph GeislerDept. of Molecular Biology, University of Wyoming, 1000 E. University Avenue, Laramie, WY 82071, USA.
Donald L Jarvis
University of Wyoming · US

Funding

N-GLYCOSYLATION MECHANISM IN INSECT CELLSR01GM049734 · NIGMS · UNIVERSITY OF WYOMING · PI JARVIS, DONALD L. · 1994 to 2010
$2.7M
A novel transgenic silkworm system for recombinant glycoprotein productionR01GM080672 · NIGMS · UNIVERSITY OF WYOMING · PI JARVIS, DONALD L. · 2007 to 2010
$1.1M
NIGMS NIH HHS R01 GM049734NIGMS NIH HHS R01 GM080672NIGMS NIH HHS R01 GM49734NIGMS NIH HHS R01 GM80672
6 · The paper itself

Abstract

Glycoproteins produced by non-engineered insects or insect cell lines characteristically bear truncated, paucimannose N-glycans in place of the complex N-glycans produced by mammalian cells. A key reason for this difference is the presence of a highly specific N-glycan processing beta-N-acetylglucosaminidase in insect, but not in mammalian systems. Thus, reducing or abolishing this enzyme could enhance the ability of glycoengineered insects or insect cell lines to produce complex N-glycans. Of the three insect species routinely used for recombinant glycoprotein production, the processing beta-N-acetylglucosaminidase gene has been isolated only from Spodoptera frugiperda. Thus, the purpose of this study was to isolate and characterize the genes encoding this important processing enzyme from the other two species, Bombyx mori and Trichoplusia ni. Bioinformatic analyses of putative processing beta-N-acetylglucosaminidase genes isolated from these two species indicated that each encoded a product that was, indeed, more similar to processing beta-N-acetylglucosaminidases than degradative or chitinolytic beta-N-acetylglucosaminidases. In addition, over-expression of each of these genes induced an enzyme activity with the substrate specificity characteristic of processing, but not degradative or chitinolytic enzymes. Together, these results demonstrated that the processing beta-N-acetylglucosaminidase genes had been successfully isolated from Trichoplusia ni and Bombyx mori. The identification of these genes has the potential to facilitate further glycoengineering of baculovirus-insect cell expression systems for the production of glycosylated proteins.

Indexed as

Gene ExpressionAcetylglucosaminidaseAnimalsBaculoviridaeCells, CulturedDrosophila melanogasterDrosophila ProteinsGenetic EngineeringMothsPolysaccharidesSubstrate SpecificityAcetylglucosaminidaseDrosophila Proteinsfdl protein, DrosophilaPolysaccharides

Identifiers

PMID19882694
PMCPMC3624021
OpenAlexW1974512982

What OpenQuestion holds

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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.