Evidence map›Paper›PMID 32285041›Full record

ArticleCurrent research in biotechnology2020

A Markov model of glycosylation elucidates isozyme specificity and glycosyltransferase interactions for glycoengineering.

Chenguang Liang, Austin W T Chiang, Anders H Hansen, Johnny Arnsdorf, Sanne Schoffelen, James T Sorrentino, Benjamin P Kellman, Bokan Bao, Bjørn G Voldborg, Nathan E Lewis

Open access · goldAbstract read
In one paragraph

Article in Current research in biotechnology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

16 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
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  5. Article
  6. A Boltzmann model predicts glycan structures from lectin binding.bioRxiv : the preprint server for biology · 2024
    Article
  7. Article
  8. Review
  9. Article
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  13. Simulating the enzymes of ganglioside biosynthesis with Glycologue.Beilstein journal of organic chemistry · 2021
    Article
  14. Article
  15. A consensus-based and readable extension ofBeilstein journal of organic chemistry · 2020
    Article
  16. 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

10 authors at 5 institutions in 2 countries.

Chenguang LiangDepartment of Pediatrics, University of California, San Diego, La Jolla, CA 92093, USA.
Austin W T ChiangDepartment of Pediatrics, University of California, San Diego, La Jolla, CA 92093, USA.
Anders H HansenThe Novo Nordisk Foundation Center for Biosustainability, Technical University of Denmark, Hørsholm, Denmark.
Johnny ArnsdorfThe Novo Nordisk Foundation Center for Biosustainability, Technical University of Denmark, Hørsholm, Denmark.
Sanne SchoffelenThe Novo Nordisk Foundation Center for Biosustainability, Technical University of Denmark, Hørsholm, Denmark.
James T SorrentinoDepartment of Pediatrics, University of California, San Diego, La Jolla, CA 92093, USA.
Benjamin P KellmanDepartment of Pediatrics, University of California, San Diego, La Jolla, CA 92093, USA.
Bokan BaoDepartment of Pediatrics, University of California, San Diego, La Jolla, CA 92093, USA.
Bjørn G VoldborgThe Novo Nordisk Foundation Center for Biosustainability, Technical University of Denmark, Hørsholm, Denmark.
Nathan E LewisDepartment of Pediatrics, University of California, San Diego, La Jolla, CA 92093, USA.
University of California, San Diego · USNovo Nordisk Foundation · DKTechnical University of Denmark · DKFoundation Center · USNovo Nordisk (United States) · US

Funding

Unraveling the mammalian secretory pathway through systems biology and algorithm developmentR35GM119850 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI LEWIS, NATHAN ENOCH · 2016 to 2025
$4.3M
NIGMS NIH HHS R35 GM119850
6 · The paper itself

Abstract

Glycosylated biopharmaceuticals are important in the global pharmaceutical market. Despite the importance of their glycan structures, our limited knowledge of the glycosylation machinery still hinders controllability of this critical quality attribute. To facilitate discovery of glycosyltransferase specificity and predict glycoengineering efforts, here we extend the approach to model N-linked protein glycosylation as a Markov process. Our model leverages putative glycosyltransferase (GT) specificity to define the biosynthetic pathways for all measured glycans, and the Markov chain modelling is used to learn glycosyltransferase isoform activities and predict glycosylation following glycosyltransferase knock-in/knockout. We apply our methodology to four different glycoengineered therapeutics (i.e., Rituximab, erythropoietin, Enbrel, and alpha-1 antitrypsin) produced in CHO cells. Our model accurately predicted N-linked glycosylation following glycoengineering and further quantified the impact of glycosyltransferase mutations on reactions catalyzed by other glycosyltransferases. By applying these learned GT-GT interaction rules identified from single glycosyltransferase mutants, our model further predicts the outcome of multi-gene glycosyltransferase mutations on the diverse biotherapeutics. Thus, this modeling approach enables rational glycoengineering and the elucidation of relationships between glycosyltransferases, thereby facilitating biopharmaceutical research and aiding the broader study of glycosylation to elucidate the genetic basis of complex changes in glycosylation.

Indexed as

glycoengineeringglycomicsGlycosylation modelglycosyltransferase interactionsisozyme specificitysystems glycobiology

Identifiers

PMID32285041
PMCPMC7153765
OpenAlexW3002834140

What OpenQuestion holds

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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.