Evidence map›Paper›PMID 29760474›Full record

ArticleNature communications2018

Structural basis for the recognition of complex-type N-glycans by Endoglycosidase S.

Beatriz Trastoy, Erik Klontz, Jared Orwenyo, Alberto Marina, Lai-Xi Wang, Eric J Sundberg, Marcelo E Guerin

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
1.9field-weighted citation impact, top 13% 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

29 citing papers in PubMed, 50 citations in OpenAlex.

  1. Glycan Remodeling Technologies for Enhancing Antibody Function.Advances in experimental medicine and biology · 2026
    Review
  2. Article
  3. Novel Endo-β-Foods (Basel, Switzerland) · 2025
    Article
  4. Article
  5. Immunomodulating Enzymes fromMicroorganisms · 2024
    Review
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Glycobiology of rheumatic diseases.Nature reviews. Rheumatology · 2023
    Review
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Review
  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

7 authors at 4 institutions in 2 countries.

Beatriz TrastoyStructural Biology Unit, CIC bioGUNE, Bizkaia Technology Park, 48160, Derio, Spain.
Erik KlontzInstitute of Human Virology, University of Maryland School of Medicine, Baltimore, MD, 21201, USA.
Jared OrwenyoDepartment of Chemistry and Biochemistry, University of Maryland, College Park, MD, 20742, USA.
Alberto MarinaStructural Biology Unit, CIC bioGUNE, Bizkaia Technology Park, 48160, Derio, Spain.
Lai-Xi WangDepartment of Chemistry and Biochemistry, University of Maryland, College Park, MD, 20742, USA.
Eric J SundbergInstitute of Human Virology, University of Maryland School of Medicine, Baltimore, MD, 21201, USA. ESundberg@som.umaryland.edu.
Marcelo E GuerinStructural Biology Unit, CIC bioGUNE, Bizkaia Technology Park, 48160, Derio, Spain. mrcguerin@cicbiogune.es.
CIC bioGUNE · ESUniversity of Maryland, Baltimore · USUniversity of Maryland, College Park · USUniversity of the Basque Country · ES

Funding

Signaling Pathways in Innate ImmunityT32AI095190 · NIAID · UNIVERSITY OF MARYLAND BALTIMORE · PI Stefanie N. Vogel · 2012 to 2026
$4.7M
Covergent Chemoenzymatic Synthesis of Glycopeptides and GlycoproteinsR01GM080374 · NIGMS · UNIV OF MARYLAND, COLLEGE PARK · PI WANG, LAI-XI · 2007 to 2021
$3.9M
NIAID NIH HHS T32 AI095190NIGMS NIH HHS R01 GM080374
6 · The paper itself

Abstract

Endoglycosidase S (EndoS) is a bacterial endo-β-N-acetylglucosaminidase that specifically catalyzes the hydrolysis of the β-1,4 linkage between the first two N-acetylglucosamine residues of the biantennary complex-type N-linked glycans of IgG Fc regions. It is used for the chemoenzymatic synthesis of homogeneously glycosylated antibodies with improved therapeutic properties, but the molecular basis for its substrate specificity is unknown. Here, we report the crystal structure of the full-length EndoS in complex with its oligosaccharide G2 product. The glycoside hydrolase domain contains two well-defined asymmetric grooves that accommodate the complex-type N-linked glycan antennae near the active site. Several loops shape the glycan binding site, thereby governing the strict substrate specificity of EndoS. Comparing the arrangement of these loops within EndoS and related endoglycosidases, reveals distinct-binding site architectures that correlate with the respective glycan specificities, providing a basis for the bioengineering of endoglycosidases to tailor the chemoenzymatic synthesis of monoclonal antibodies.

Indexed as

Amino Acid MotifsAntibodies, MonoclonalBacterial ProteinsCarbohydrate SequenceCatalytic DomainCloning, MolecularCrystallography, X-RayEscherichia coliGene ExpressionGenetic VectorsGlycoside HydrolasesHydrolysisIsoenzymesKineticsMolecular Docking SimulationOligosaccharidesAntibodies, MonoclonalBacterial ProteinsGlycoside HydrolasesIsoenzymesNDOS protein, Streptococcus pyogenesOligosaccharidesRecombinant Proteins

Identifiers

PMID29760474
PMCPMC5951799
OpenAlexW2807107030

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

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.