Evidence map›Paper›PMID 29474426›Full record

ArticlePloS one2018

Generation of efficient mutants of endoglycosidase from Streptococcus pyogenes and their application in a novel one-pot transglycosylation reaction for antibody modification.

Mitsuhiro Iwamoto, Yukiko Sekiguchi, Kensuke Nakamura, Yoshirou Kawaguchi, Takeshi Honda, Jun Hasegawa

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

11 citing papers in PubMed, 24 citations in OpenAlex.

  1. BisectingACS chemical biology · 2025
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  10. Oligosaccharide Synthesis and Translational Innovation.Journal of the American Chemical Society · 2019
    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

6 authors at 1 institution in 1 country.

Mitsuhiro IwamotoModality Research Laboratories, Biologics Division, Daiichi Sankyo Co., Ltd., Tokyo, Japan.ORCID 0000-0002-0212-2322
Yukiko SekiguchiModality Research Laboratories, Biologics Division, Daiichi Sankyo Co., Ltd., Tokyo, Japan.
Kensuke NakamuraModality Research Laboratories, Biologics Division, Daiichi Sankyo Co., Ltd., Tokyo, Japan.
Yoshirou KawaguchiModality Research Laboratories, Biologics Division, Daiichi Sankyo Co., Ltd., Tokyo, Japan.
Takeshi HondaMedicinal Chemistry Management Group, Research Function Division, Daiichi Sankyo Co., Ltd., Tokyo, Japan.
Jun HasegawaModality Research Laboratories, Biologics Division, Daiichi Sankyo Co., Ltd., Tokyo, Japan.
Daiichi-Sankyo (Japan) · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The fine structures of Fc N-glycan modulate the biological functions and physicochemical properties of antibodies. By remodeling N-glycan to obtain a homogeneous glycoform or chemically modified glycan, antibody characteristics can be controlled or modified. Such remodeling can be achieved by transglycosylation reactions using a mutant of endoglycosidase from Streptococcus pyogenes (Endo-S) and glycan oxazoline. In this study, we generated improved mutants of Endo-S by introducing additional mutations to the D233Q mutant. Notably, Endo-S D233Q/Q303L, D233Q/E350Q, and several other mutations resulted in transglycosylation efficiencies exceeding 90%, with a single-digit donor-to-substrate ratio of five, and D233Q/Y402F/D405A and several other mutations resulted in slightly reduced transglycosylation efficiencies accompanied by no detectable hydrolysis activity for 48 h. We further demonstrated that the combined use of mutants of Endo-S with Endo-M or Endo-CC, endoglycosidases from Mucor hiemalis and Coprinopsis cinerea, enables one-pot transglycosylation from sialoglycopeptide to antibodies. This novel reaction enables glycosylation remodeling of antibodies, without the chemical synthesis of oxazoline in advance or in situ.

Indexed as

MutationAntibodies, BacterialGlycoside HydrolasesGlycosylationHydrolysisStreptococcus pyogenesTrastuzumabAntibodies, BacterialGlycoside HydrolasesTrastuzumab

Identifiers

PMID29474426
PMCPMC5825150
OpenAlexW2788514052

What OpenQuestion holds

Textmetadata
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.