Evidence map›Paper›PMID 28387635›Full record

ArticlemAbs2017

Identification of human IgG1 variant with enhanced FcRn binding and without increased binding to rheumatoid factor autoantibody.

Atsuhiko Maeda, Yuki Iwayanagi, Kenta Haraya, Tatsuhiko Tachibana, Genki Nakamura, Takeru Nambu, Keiko Esaki, Kunihiro Hattori, Tomoyuki Igawa

Open access · goldAbstract read
In one paragraph

Article in mAbs, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.3field-weighted citation impact, top 21% 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

19 citing papers in PubMed, 28 citations in OpenAlex.

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  12. In Translation: FcRn across the Therapeutic Spectrum.International journal of molecular sciences · 2021
    Review
  13. Article
  14. The neonatal Fc receptor: Key to homeostasic control of IgG and IgG-related biopharmaceuticals.American journal of transplantation : official journal of the American Society of Transplantation and the American Society of Transplant Surgeons · 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

9 authors at 1 institution in 1 country.

Atsuhiko Maedaa Chugai Pharmaceutical Co. Ltd., Pharmaceutical Technology Division, Ukima Research Labs. , Ukima, Kita-ku , Tokyo , Japan.
Yuki Iwayanagib Chugai Pharmaceutical Co. Ltd., Research Division, Kamakura Research Labs , Kajiwara, Kamakura , Kanagawa , Japan.
Kenta Harayac Chugai Pharmabody Research Pte. Ltd. , Synapse , Singapore.
Tatsuhiko Tachibanab Chugai Pharmaceutical Co. Ltd., Research Division, Kamakura Research Labs , Kajiwara, Kamakura , Kanagawa , Japan.
Genki Nakamurad Chugai Pharmaceutical Co. Ltd., Research Division, Fuji Gotemba Research Labs , Komakado, Gotemba , Shizuoka , Japan.
Takeru Nambud Chugai Pharmaceutical Co. Ltd., Research Division, Fuji Gotemba Research Labs , Komakado, Gotemba , Shizuoka , Japan.
Keiko Esakid Chugai Pharmaceutical Co. Ltd., Research Division, Fuji Gotemba Research Labs , Komakado, Gotemba , Shizuoka , Japan.
Kunihiro Hattorib Chugai Pharmaceutical Co. Ltd., Research Division, Kamakura Research Labs , Kajiwara, Kamakura , Kanagawa , Japan.
Tomoyuki Igawad Chugai Pharmaceutical Co. Ltd., Research Division, Fuji Gotemba Research Labs , Komakado, Gotemba , Shizuoka , Japan.
Chugai Pharma (United States) · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Various studies have demonstrated that Fc engineering to enhance neonatal Fc receptor (FcRn) binding is effective for elongating half-life or increasing cellular uptake of IgG. A previous study has shown that a N434H mutation to enhance FcRn binding resulted in increased binding to rheumatoid factor (RF) autoantibody, which is not desirable for therapeutic use in autoimmune disease. In this study, we first showed that all the existing Fc variants with enhanced FcRn binding also show increased RF binding, and then identified specific mutations that could be introduced to those Fc variants to reduce the RF binding. Furthermore, we generated novel Fc variants that do not increase RF binding and show half-lives of 45 d in cynomolgus monkey, which is longer than those of previously reported Fc variants. In addition, we generated novel Fc variants with antigen sweeping activity that do not increase RF binding. We expect that these novel Fc variants will be useful as antibody therapeutics against autoimmune diseases.

Indexed as

Amino Acid SubstitutionAnimalsHistocompatibility Antigens Class IHumansImmunoglobulin Fc FragmentsImmunoglobulin GMacaca fascicularisMiceReceptors, FcRheumatoid FactorFc receptor, neonatalHistocompatibility Antigens Class IImmunoglobulin Fc FragmentsImmunoglobulin GReceptors, FcRheumatoid FactorAntibody therapeuticsCH2-CH3 interfaceFc engineeringFcRnpharmacokineticspre-existing ADARFrheumatoid factorsweeping antibody

Identifiers

PMID28387635
PMCPMC5524163
OpenAlexW2604327082

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.