Evidence map›Paper›PMID 27288408›Full record

ArticleThe Journal of biological chemistry2016

Glycosynthase Mutants of Endoglycosidase S2 Show Potent Transglycosylation Activity and Remarkably Relaxed Substrate Specificity for Antibody Glycosylation Remodeling.

Tiezheng Li, Xin Tong, Qiang Yang, John P Giddens, Lai-Xi Wang

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 84 papers.

0numbers the graph read from it
0cells of the map it votes in
84citing papers in PubMed
12.0field-weighted citation impact, top 1% 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

84 citing papers in PubMed, 119 citations in OpenAlex.

  1. Article
  2. Generation of DAR1 Glycosite-Specific Antibody-Drug Conjugates Using DisacLink Technology.Chembiochem : a European journal of chemical biology · 2026
    Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Selective fluorination of Fc glycans enhances antibody-mediated effector functions.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  8. JACS Au · 2026
    Article
  9. Review
  10. Article
  11. Glycan Remodeling Technologies for Enhancing Antibody Function.Advances in experimental medicine and biology · 2026
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. BisectingACS chemical biology · 2025
    Article
  17. Article
  18. A Robust α-l-Fucosidase fromACS chemical biology · 2024
    Article
  19. Article
  20. Article

24 more citing papers are in PubMed but not listed here.

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

5 authors at 1 institution in 1 country.

Tiezheng LiFrom the Department of Chemistry and Biochemistry, University of Maryland, College Park, Maryland 20742.
Xin TongFrom the Department of Chemistry and Biochemistry, University of Maryland, College Park, Maryland 20742.
Qiang YangFrom the Department of Chemistry and Biochemistry, University of Maryland, College Park, Maryland 20742.
John P GiddensFrom the Department of Chemistry and Biochemistry, University of Maryland, College Park, Maryland 20742.
Lai-Xi WangFrom the Department of Chemistry and Biochemistry, University of Maryland, College Park, Maryland 20742 wang518@umd.edu.
University of Maryland, College Park · US

Funding

Covergent Chemoenzymatic Synthesis of Glycopeptides and GlycoproteinsR01GM080374 · NIGMS · UNIV OF MARYLAND, COLLEGE PARK · PI WANG, LAI-XI · 2007 to 2021
$3.9M
Synthesis and Function of Antibody Fc Domain GlycoformsR01GM096973 · NIGMS · UNIV OF MARYLAND, COLLEGE PARK · PI WANG, LAI-XI · 2011 to 2020
$2.4M
NIGMS NIH HHS R01 GM080374NIGMS NIH HHS R01 GM096973
6 · The paper itself

Abstract

Glycosylation can exert a profound impact on the structures and biological functions of antibodies. Glycosylation remodeling using the endoglycosidase-catalyzed deglycosylation and transglycosylation approach is emerging as a promising platform to produce homogeneous glycoforms of antibodies, but the broad application of this method will require the availability of highly efficient glycosynthase mutants. We describe in this paper a systematic site-directed mutagenesis of an endoglycosidase from Streptococcus pyogenes of serotype M49 (Endo-S2) and the evaluation of the resulting mutants for their hydrolysis and transglycosylation activities. We found that mutations at the Asp-184 residue gave mutants that demonstrated significantly different properties, some possessed potent transglycosylation activity with diminished hydrolysis activity but others did not, which would be otherwise difficult to predict without the comparative study. In contrast to the previously reported Endo-S mutants that are limited to action on complex type N-glycans, the Endo-S2 glycosynthases described here, including D184M and D184Q, were found to have remarkably relaxed substrate specificity and were capable of transferring three major types (complex, high-mannose, and hybrid type) of N-glycans for antibody glycosylation remodeling. In addition, the Endo-S2 glycosynthase mutants were found to be much more active in general than the Endo-S mutants for transglycosylation. The usefulness of these Endo-S2 glycosynthase mutants was exemplified by an efficient glycosylation remodeling of two therapeutic monoclonal antibodies, rituximab and trastuzumab (Herceptin).

Indexed as

MutationBacterial ProteinsGlycoside HydrolasesGlycosylationHydrolysisRituximabStreptococcus pyogenesSubstrate SpecificityTrastuzumabBacterial ProteinsGlycoside HydrolasesNDOS protein, Streptococcus pyogenesRituximabTrastuzumabantibody engineeringchemoenzymatic synthesisglycoengineeringglycoproteinglycosidaseglycosylationglycosynthaseHerceptinmonoclonal antibodytransglycosylation

Identifiers

PMID27288408
PMCPMC4974367
OpenAlexW2409183178

What OpenQuestion holds

Textmetadata
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.