Evidence map›Paper›PMID 28597152›Full record

ReviewProtein & cell2018

Glycosylation engineering of therapeutic IgG antibodies: challenges for the safety, functionality and efficacy.

Yusuke Mimura, Toshihiko Katoh, Radka Saldova, Roisin O'Flaherty, Tomonori Izumi, Yuka Mimura-Kimura, Toshiaki Utsunomiya, Yoichi Mizukami, Kenji Yamamoto, Tsuneo Matsumoto and 1 more

Abstract readReview
In one paragraph

Review in Protein & cell, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 100 papers.

0numbers the graph read from it
0cells of the map it votes in
100citing papers in PubMed
–field-weighted citation impact
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

100 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Immunoglobulin G in aging and cancer.Frontiers in immunology · 2026
    Review
  6. Article
  7. Review
  8. Article
  9. Therapeutic effect of galactosyltransferase- and sialyltransferase-encoding mRNA in rheumatoid arthritis.Molecular therapy : the journal of the American Society of Gene Therapy · 2025
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. Article

40 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

11 authors.

Yusuke MimuraDepartment of Clinical Research, NHO Yamaguchi-Ube Medical Center, 685 Higashi-Kiwa, Ube, 755-0241, Japan. mimuray66@outlook.jp.
Toshihiko KatohLaboratory of Molecular Biology and Bioresponse, Division of Integrated Life Science, Graduate School of Biostudies, Kyoto University, Kitashirakawa, Oiwake-Cho, Sakyo-Ku, Kyoto, 606-8502, Japan.
Radka SaldovaNIBRT GlycoScience Group, National Institute for Bioprocessing Research and Training, Mount Merrion, Blackrock, Dublin 4, Ireland.
Roisin O'FlahertyNIBRT GlycoScience Group, National Institute for Bioprocessing Research and Training, Mount Merrion, Blackrock, Dublin 4, Ireland.
Tomonori IzumiCenter for Regenerative Medicine, Yamaguchi University Graduate School of Medicine, 1-1-1 Minami Kogushi, Ube, 755-8505, Japan.
Yuka Mimura-KimuraDepartment of Clinical Research, NHO Yamaguchi-Ube Medical Center, 685 Higashi-Kiwa, Ube, 755-0241, Japan.
Toshiaki UtsunomiyaDepartment of Clinical Research, NHO Yamaguchi-Ube Medical Center, 685 Higashi-Kiwa, Ube, 755-0241, Japan.
Yoichi MizukamiCenter for Gene Research, Yamaguchi University, 1-1-1 Minami-Kogushi, Ube, 755-8505, Japan.
Kenji YamamotoResearch Institute for Bioresources and Biotechnology, Ishikawa Prefectural University, 1-308 Suematsu, Nonoichi, Ishikawa, 921-8836, Japan.
Tsuneo MatsumotoDepartment of Clinical Research, NHO Yamaguchi-Ube Medical Center, 685 Higashi-Kiwa, Ube, 755-0241, Japan.
Pauline M RuddNIBRT GlycoScience Group, National Institute for Bioprocessing Research and Training, Mount Merrion, Blackrock, Dublin 4, Ireland.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Glycosylation of the Fc region of IgG has a profound impact on the safety and clinical efficacy of therapeutic antibodies. While the biantennary complex-type oligosaccharide attached to Asn297 of the Fc is essential for antibody effector functions, fucose and outer-arm sugars attached to the core heptasaccharide that generate structural heterogeneity (glycoforms) exhibit unique biological activities. Hence, efficient and quantitative glycan analysis techniques have been increasingly important for the development and quality control of therapeutic antibodies, and glycan profiles of the Fc are recognized as critical quality attributes. In the past decade our understanding of the influence of glycosylation on the structure/function of IgG-Fc has grown rapidly through X-ray crystallographic and nuclear magnetic resonance studies, which provides possibilities for the design of novel antibody therapeutics. Furthermore, the chemoenzymatic glycoengineering approach using endoglycosidase-based glycosynthases may facilitate the development of homogeneous IgG glycoforms with desirable functionality as next-generation therapeutic antibodies. Thus, the Fc glycans are fertile ground for the improvement of the safety, functionality, and efficacy of therapeutic IgG antibodies in the era of precision medicine.

Indexed as

AnimalsAntibodies, MonoclonalGlycosylationHumansImmunoglobulin GProtein EngineeringReceptors, FcTreatment OutcomeAntibodies, MonoclonalImmunoglobulin GReceptors, Fcchemoenzymatic glycoengineeringcrystal structureendoglycosidasefucoseglycosylationintravenous immunoglobulinsialic acidtransglycosylationultra performance liquid chromatography

Identifiers

PMID28597152
PMCPMC5777974

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.