Evidence map›Paper›PMID 27046227›Full record

ArticleNature communications2016

Sialylation converts arthritogenic IgG into inhibitors of collagen-induced arthritis.

Yuhsuke Ohmi, Wataru Ise, Akira Harazono, Daisuke Takakura, Hidehiro Fukuyama, Yoshihiro Baba, Masashi Narazaki, Hirofumi Shoda, Nobunori Takahashi, Yuki Ohkawa and 9 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 106 papers.

0numbers the graph read from it
0cells of the map it votes in
106citing papers in PubMed
17.4field-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

106 citing papers in PubMed, 171 citations in OpenAlex.

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  7. Not all antibodies are created equal: total IgG glycosylation and severity of antibody-mediated rejection in kidney transplantation.Transplant international : official journal of the European Society for Organ Transplantation · 2026
    Article
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  14. Molecular determinants of sialylated IgG anti-inflammatory activity.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  15. Article
  16. Review
  17. Article
  18. Article
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  20. Role of Antibody Glycosylation in Health, Disease, and Therapy.Handbook of experimental pharmacology · 2025
    Review

46 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

19 authors at 9 institutions in 1 country.

Yuhsuke OhmiDepartment of Biochemistry II, Nagoya University Graduate School of Medicine, 65 Tsurumai, Showa-ku, Nagoya 466-0065, Japan.
Wataru IseLaboratory of Lymphocyte Differentiation, WPI Immunology Frontier Research Center and Graduate School of Frontier Biosciences, Osaka University, 3-1 Yamadaoka, Suita, Osaka 565-0871, Japan.
Akira HarazonoDivision of Biological Chemistry and Biologicals, National Institute of Health Sciences, 1-18-1 Kamiyoga, Setagaya-ku, Tokyo 158-8501, Japan.
Daisuke TakakuraLaboratory of Proteome Science, Graduate School of Medical Life Science, Yokohama City University, 1-7-29, Suehiro, Tsurumi-ku, Yokohama, Kanagawa 230-0045, Japan.
Hidehiro FukuyamaLaboratory for Lymphocyte Differentiation, RIKEN Center for Integrative Medical Sciences, 1-7-22, Suehirocho, Tsurumi-ku, Yokohama, Kanagawa 230-0045, Japan.
Yoshihiro BabaLaboratory of Lymphocyte Differentiation, WPI Immunology Frontier Research Center and Graduate School of Frontier Biosciences, Osaka University, 3-1 Yamadaoka, Suita, Osaka 565-0871, Japan.
Masashi NarazakiDepartment of Respiratory Medicine, Allergy and Rheumatic Diseases, Osaka University Graduate School of Medicine, 2-2 Yamadaoka, Suita, Osaka 565-0871, Japan.
Hirofumi ShodaDepartment of Allergy and Rheumatology, Graduate School of Medicine, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, Japan.
Nobunori TakahashiDepartment of Orthopedics, Nagoya University Graduate School of Medicine, 65 Tsurumai, Showa-ku, Nagoya 466-0065, Japan.
Yuki OhkawaDepartment of Biochemistry II, Nagoya University Graduate School of Medicine, 65 Tsurumai, Showa-ku, Nagoya 466-0065, Japan.
Shuting JiDepartment of Biochemistry II, Nagoya University Graduate School of Medicine, 65 Tsurumai, Showa-ku, Nagoya 466-0065, Japan.
Fumihiro SugiyamaLaboratory Animal Resource Center, University of Tsukuba, 1-1-1 Ten-no-dai, Tsukuba 305-8575, Japan.
Keishi FujioDepartment of Allergy and Rheumatology, Graduate School of Medicine, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, Japan.
Atsushi KumanogohDepartment of Respiratory Medicine, Allergy and Rheumatic Diseases, Osaka University Graduate School of Medicine, 2-2 Yamadaoka, Suita, Osaka 565-0871, Japan.
Kazuhiko YamamotoDepartment of Allergy and Rheumatology, Graduate School of Medicine, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, Japan.
Nana KawasakiDivision of Biological Chemistry and Biologicals, National Institute of Health Sciences, 1-18-1 Kamiyoga, Setagaya-ku, Tokyo 158-8501, Japan.
Tomohiro KurosakiLaboratory of Lymphocyte Differentiation, WPI Immunology Frontier Research Center and Graduate School of Frontier Biosciences, Osaka University, 3-1 Yamadaoka, Suita, Osaka 565-0871, Japan.
Yoshimasa TakahashiDepartment of Immunology, National Institute of Infectious Diseases, 1-23-1 Toyama, Shinjuku-ku, Tokyo 162-8640, Japan.
Koichi FurukawaDepartment of Biochemistry II, Nagoya University Graduate School of Medicine, 65 Tsurumai, Showa-ku, Nagoya 466-0065, Japan.
Osaka University · JPNagoya University · JPThe University of Tokyo · JPNational Institute of Infectious Diseases · JPRIKEN Center for Integrative Medical Sciences · JPYokohama City University · JPChubu University · JPNational Institute of Health Sciences · JPUniversity of Tsukuba · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Rheumatoid arthritis (RA)-associated IgG antibodies such as anti-citrullinated protein antibodies (ACPAs) have diverse glycosylation variants; however, key sugar chains modulating the arthritogenic activity of IgG remain to be clarified. Here, we show that reduced sialylation is a common feature of RA-associated IgG in humans and in mouse models of arthritis. Genetically blocking sialylation in activated B cells results in exacerbation of joint inflammation in a collagen-induced arthritis (CIA) model. On the other hand, artificial sialylation of anti-type II collagen antibodies, including ACPAs, not only attenuates arthritogenic activity, but also suppresses the development of CIA in the antibody-infused mice, whereas sialylation of other IgG does not prevent CIA. Thus, our data demonstrate that sialylation levels control the arthritogenicity of RA-associated IgG, presenting a potential target for antigen-specific immunotherapy.

Indexed as

Protein Processing, Post-TranslationalAmino Acid SequenceAnimalsArthritis, ExperimentalArthritis, RheumatoidAutoantibodiesCarbohydrate SequenceCollagen Type IIHumansImmunoglobulin GMiceMice, Inbred C57BLMice, Inbred DBAMice, TransgenicMolecular Sequence DataSialic AcidsAutoantibodiesCollagen Type IIImmunoglobulin GSialic Acids

Identifiers

PMID27046227
PMCPMC4822049
OpenAlexW2324641558

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Registered trials

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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.