Evidence map›Paper›PMID 26966183›Full record

ArticleThe Journal of biological chemistry2016

Endo-F3 Glycosynthase Mutants Enable Chemoenzymatic Synthesis of Core-fucosylated Triantennary Complex Type Glycopeptides and Glycoproteins.

John P Giddens, Joseph V Lomino, Mohammed N Amin, 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 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
7.0field-weighted citation impact, top 3% 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

51 citing papers in PubMed, 89 citations in OpenAlex.

  1. Article
  2. Revealing the Biological Effect of theJournal of the American Chemical Society · 2026
    Article
  3. Article
  4. Article
  5. Glycan Remodeling Technologies for Enhancing Antibody Function.Advances in experimental medicine and biology · 2026
    Review
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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

4 authors at 1 institution in 1 country.

John P GiddensFrom the Institute of Human Virology, University of Maryland School of Medicine, Baltimore, Maryland 21201 and the Department of Chemistry and Biochemistry, University of Maryland, College Park, Maryland 20742.
Joseph V LominoFrom the Institute of Human Virology, University of Maryland School of Medicine, Baltimore, Maryland 21201 and.
Mohammed N AminFrom the Institute of Human Virology, University of Maryland School of Medicine, Baltimore, Maryland 21201 and the Department of Chemistry and Biochemistry, University of Maryland, College Park, Maryland 20742.
Lai-Xi WangFrom the Institute of Human Virology, University of Maryland School of Medicine, Baltimore, Maryland 21201 and the Department of Chemistry and Biochemistry, University of Maryland, College Park, Maryland 20742 wang518@umd.edu.
University of Maryland, Baltimore · US

Funding

Covergent Chemoenzymatic Synthesis of Glycopeptides and GlycoproteinsR01GM080374 · NIGMS · UNIV OF MARYLAND, COLLEGE PARK · PI WANG, LAI-XI · 2007 to 2021
$3.9M
NIGMS NIH HHS R01 GM080374
6 · The paper itself

Abstract

Chemoenzymatic synthesis is emerging as a promising approach to the synthesis of homogeneous glycopeptides and glycoproteins highly demanded for functional glycomics studies, but its generality relies on the availability of a range of enzymes with high catalytic efficiency and well defined substrate specificity. We describe in this paper the discovery of glycosynthase mutants derived from Elizabethkingia meningoseptica endoglycosidase F3 (Endo-F3) of the GH18 family, which are devoid of the inherent hydrolytic activity but are able to take glycan oxazolines for transglycosylation. Notably, the Endo-F3 D165A and D165Q mutants demonstrated high acceptorsubstrate specificity toward α1,6-fucosyl-GlcNAc-Asn or α1,6-fucosyl-GlcNAc-polypeptide in transglycosylation, enabling a highly convergent synthesis of core-fucosylated, complex CD52 glycopeptide antigen. The Endo-F3 mutants were able to use both bi- and triantennary glycan oxazolines as substrates for transglycosylation, in contrast to previously reported endoglycosidases derived from Endo-S, Endo-M, Endo-D, and Endo-A mutants that could not recognize triantennary N-glycans. Using rituximab as a model system, we have further demonstrated that the Endo-F3 mutants are highly efficient for glycosylation remodeling of monoclonal antibodies to produce homogeneous intact antibody glycoforms. Interestingly, the new triantennary glycan glycoform of antibody showed much higher affinity for galectin-3 than that of the commercial antibody. The Endo-F3 mutants represent the first endoglycosidase-based glycosynthases capable of transferring triantennary complex N-glycans, which would be very useful for glycoprotein synthesis and glycosylation remodeling of antibodies.

Indexed as

Bacterial ProteinsFlavobacteriaceaeGlycoproteinsGlycosyltransferasesAntibodies, BacterialAntibodies, Monoclonal, Murine-DerivedGlycosylationAntibodies, BacterialAntibodies, Monoclonal, Murine-DerivedBacterial ProteinsGlycoproteinsGlycosyltransferasesenzyme catalysisglycoproteinglycosidaseglycosylationoligosaccharide

Identifiers

PMID26966183
PMCPMC4861498
OpenAlexW2293739757

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.