Evidence map›Paper›PMID 35452676›Full record

ArticleThe Journal of biological chemistry2022

Antibody recognition of complement factor H reveals a flexible loop involved in atypical hemolytic uremic syndrome pathogenesis.

Takanori Yokoo, Aki Tanabe, Yoko Yoshida, Jose M M Caaveiro, Makoto Nakakido, Yoichiro Ikeda, Yoshihiro Fujimura, Masaneori Matsumoto, Kevin Entzminger, Toshiaki Maruyama and 3 more

Erratum issuedOpen access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in The Journal of biological chemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.3field-weighted citation impact, top 46% 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

1 citing paper in PubMed, 4 citations in OpenAlex.

  1. Improving the solubility of single domain antibodies using VH-like hallmark residues.Protein science : a publication of the Protein Society · 2025
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

13 authors at 3 institutions in 1 country.

Takanori YokooDepartment of Chemistry and Biotechnology, School of Engineering, The University of Tokyo, Bunkyo-ku, Tokyo, Japan.
Aki TanabeDepartment of Bioengineering, School of Engineering, The University of Tokyo, Bunkyo-ku, Tokyo, Japan.
Yoko YoshidaDivision of Nephrology and Endocrinology, The University of Tokyo, Bunkyo-ku, Tokyo, Japan.
Jose M M CaaveiroDepartment of Global Healthcare, Graduate School of Pharmaceutical Sciences, Kyushu University, Higashi-ku, Fukuoka, Japan.
Makoto NakakidoDepartment of Chemistry and Biotechnology, School of Engineering, The University of Tokyo, Bunkyo-ku, Tokyo, Japan; Department of Bioengineering, School of Engineering, The University of Tokyo, Bunkyo-ku, Tokyo, Japan. Electronic address: nakakido@g.ecc.u-tokyo.ac.jp.
Yoichiro IkedaDivision of Nephrology and Endocrinology, The University of Tokyo, Bunkyo-ku, Tokyo, Japan.
Yoshihiro FujimuraDepartment of Blood Transfusion Medicine, Nara Medical University, Kashihara, Nara, Japan.
Masaneori MatsumotoDepartment of Blood Transfusion Medicine, Nara Medical University, Kashihara, Nara, Japan.
Kevin EntzmingerAbwiz Bio Inc, San Diego, California, USA.
Toshiaki MaruyamaAbwiz Bio Inc, San Diego, California, USA.
C J OkumuraAbwiz Bio Inc, San Diego, California, USA.
Masaomi NangakuDivision of Nephrology and Endocrinology, The University of Tokyo, Bunkyo-ku, Tokyo, Japan.
Kouhei TsumotoDepartment of Chemistry and Biotechnology, School of Engineering, The University of Tokyo, Bunkyo-ku, Tokyo, Japan; Department of Bioengineering, School of Engineering, The University of Tokyo, Bunkyo-ku, Tokyo, Japan; The institute of Medical Science, The University of Tokyo, Minato-ku, Tokyo, Japan. Electronic address: tsumoto@bioeng.t.u-tokyo.ac.jp.
The University of Tokyo · JPNara Medical University · JPKyushu University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Atypical hemolytic uremic syndrome (aHUS) is a disease associated with dysregulation of the immune complement system, especially of the alternative pathway (AP). Complement factor H (CFH), consisting of 20 domains called complement control protein (CCP1-20), downregulates the AP as a cofactor for mediating C3 inactivation by complement factor I. However, anomalies related to CFH are known to cause excessive complement activation and cytotoxicity. In aHUS, mutations and the presence of anti-CFH autoantibodies (AAbs) have been reported as plausible causes of CFH dysfunction, and it is known that CFH-related aHUS carries a high probability of end-stage renal disease. Elucidating the detailed functions of CFH at the molecular level will help to understand aHUS pathogenesis. Herein, we used biophysical data to reveal that a heavy-chain antibody fragment, termed VHH4, recognized CFH with high affinity. Hemolytic assays also indicated that VHH4 disrupted the protective function of CFH on sheep erythrocytes. Furthermore, X-ray crystallography revealed that VHH4 recognized the Leu1181-Leu1189

Indexed as

Atypical Hemolytic Uremic SyndromeAntibodies, MonoclonalAutoantibodiesComplement ActivationComplement Factor HEpitopesHumansMutationAntibodies, MonoclonalAutoantibodiesComplement Factor HEpitopesaHUSautoantibodyautoimmune diseaseCFHcomplement systemisothermal titration calorimetryMD simulationsurface plasmon resonanceVHHX-ray crystallography

Identifiers

PMID35452676
PMCPMC9127587
OpenAlexW4224281098

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.