Evidence map›Paper›PMID 34419057›Full record

ArticleMicrobial cell factories2021

Combining functional metagenomics and glycoanalytics to identify enzymes that facilitate structural characterization of sulfated N-glycans.

Léa Chuzel, Samantha L Fossa, Madison L Boisvert, Samanta Cajic, René Hennig, Mehul B Ganatra, Udo Reichl, Erdmann Rapp, Christopher H Taron

Open access · goldAbstract read
In one paragraph

Article in Microbial cell factories, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.1field-weighted citation impact, top 22% 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

10 citing papers in PubMed, 21 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Immunoglobulin A carries sulfated andFrontiers in molecular biosciences · 2025
    Article
  5. Raider of the lostFrontiers in molecular biosciences · 2025
    Article
  6. Article
  7. Article
  8. ReliableMolecules (Basel, Switzerland) · 2023
    Article
  9. Article
  10. Special Issue 'Microbial glycobiotechnology'.Microbial cell factories · 2022
    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

9 authors at 2 institutions in 2 countries.

Léa ChuzelBioprocess Engineering, Max Planck Institute for Dynamics of Complex Technical Systems, 39106, Magdeburg, Germany.ORCID http://orcid.org/0000-0001-7185-5872
Samantha L FossaNew England Biolabs, Ipswich, MA, 01938, USA.
Madison L BoisvertNew England Biolabs, Ipswich, MA, 01938, USA.
Samanta CajicBioprocess Engineering, Max Planck Institute for Dynamics of Complex Technical Systems, 39106, Magdeburg, Germany.ORCID http://orcid.org/0000-0001-5820-0732
René HennigglyXera GmbH, 39120, Magdeburg, Germany.ORCID http://orcid.org/0000-0001-9172-7982
Mehul B GanatraNew England Biolabs, Ipswich, MA, 01938, USA.
Udo ReichlBioprocess Engineering, Max Planck Institute for Dynamics of Complex Technical Systems, 39106, Magdeburg, Germany.ORCID http://orcid.org/0000-0001-6538-1332
Erdmann RappBioprocess Engineering, Max Planck Institute for Dynamics of Complex Technical Systems, 39106, Magdeburg, Germany.ORCID http://orcid.org/0000-0001-6618-2626
Christopher H TaronNew England Biolabs, Ipswich, MA, 01938, USA. taron@neb.com.ORCID http://orcid.org/0000-0001-8149-4556
New England Biolabs (United States) · USMax Planck Institute for Dynamics of Complex Technical Systems · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundSulfate modification of N-glycans is important for several biological functions such as clearance of pituitary hormones or immunoregulation. Yet, the prevalence of this N-glycan modification and its functions remain largely unexplored. Characterization of N-glycans bearing sulfate modifications is hampered in part by a lack of enzymes that enable site-specific detection of N-glycan sulfation. In this study, we used functional metagenomic screening to identify enzymes that act upon sulfated N-acetylglucosamine (GlcNAc). Using multiplexed capillary gel electrophoresis with laser-induced fluorescence detection (xCGE-LIF) -based glycoanalysis we proved their ability to act upon GlcNAc-6-SO

resultsOur screen identified a sugar-specific sulfatase that specifically removes sulfate from GlcNAc-6-SO

conclusionThe present study demonstrates the feasibility of using functional metagenomic screening combined with glycoanalytics to discover enzymes that act upon chemical modifications of glycans. The discovered enzymes represent new specificities that can help resolve the presence of GlcNAc-6-SO

Indexed as

AcetylglucosamineEnzymesKineticsMetagenomicsPolysaccharidesSulfatesAcetylglucosamineEnzymesPolysaccharidesSulfatesFunctional metagenomicsGlycan analysisGlycan sulfationGlycoanalyticsHuman microbiomeN-acetylglucosamine-6-sulfateSulfatase

Identifiers

PMID34419057
PMCPMC8379841
OpenAlexW3193663583

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.