Evidence map›Paper›PMID 28604720›Full record

ArticleNature immunology2017

IgG Fc domains that bind C1q but not effector Fcγ receptors delineate the importance of complement-mediated effector functions.

Chang-Han Lee, Gabrielle Romain, Wupeng Yan, Makiko Watanabe, Wissam Charab, Biliana Todorova, Jiwon Lee, Kendra Triplett, Moses Donkor, Oana I Lungu and 15 more

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

Article in Nature immunology, 2017. 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 89 papers.

0numbers the graph read from it
0cells of the map it votes in
89citing papers in PubMed
15.0field-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

89 citing papers in PubMed, 143 citations in OpenAlex.

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  13. Analysis of BeyfortusCurrent issues in molecular biology · 2024
    Review
  14. Article
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29 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

25 authors at 5 institutions in 3 countries.

Chang-Han LeeDepartment of Chemical Engineering, University of Texas at Austin, Austin, Texas, USA.ORCID http://orcid.org/0000-0002-7156-4423
Gabrielle RomainDepartment of Chemical and Biomolecular Engineering, University of Houston, Houston, Texas, USA.
Wupeng YanDepartment of Molecular Biosciences, University of Texas at Austin, Austin, Texas, USA.ORCID http://orcid.org/0000-0001-5387-6362
Makiko WatanabeDepartment of Chemical Engineering, University of Texas at Austin, Austin, Texas, USA.
Wissam CharabDepartment of Chemical Engineering, University of Texas at Austin, Austin, Texas, USA.
Biliana TodorovaInstitut Pasteur, Department of Immunology, Unit of Antibodies in Therapy and Pathology, Paris, France.
Jiwon LeeDepartment of Chemical Engineering, University of Texas at Austin, Austin, Texas, USA.
Kendra TriplettDepartment of Molecular Biosciences, University of Texas at Austin, Austin, Texas, USA.
Moses DonkorDepartment of Chemical Engineering, University of Texas at Austin, Austin, Texas, USA.
Oana I LunguDepartment of Chemical Engineering, University of Texas at Austin, Austin, Texas, USA.
Anja LuxInstitute of Genetics, Department of Biology, University of Erlangen-Nürnberg, Erlangen, Germany.
Nicholas MarshallDepartment of Chemical Engineering, University of Texas at Austin, Austin, Texas, USA.
Margaret A LindorferDepartment of Biochemistry and Molecular Genetics, University of Virginia School of Medicine, Charlottesville, Virginia, USA.
Odile Richard-Le GoffInstitut Pasteur, Department of Immunology, Unit of Antibodies in Therapy and Pathology, Paris, France.
Bianca BalbinoInstitut Pasteur, Department of Immunology, Unit of Antibodies in Therapy and Pathology, Paris, France.
Tae Hyun KangDepartment of Chemical Engineering, University of Texas at Austin, Austin, Texas, USA.
Hidetaka TannoDepartment of Chemical Engineering, University of Texas at Austin, Austin, Texas, USA.
George DelidakisDepartment of Chemical Engineering, University of Texas at Austin, Austin, Texas, USA.
Corrine AlfordDepartment of Biomedical Engineering, University of Texas at Austin, Austin, Texas, USA.
Ronald P TaylorDepartment of Biochemistry and Molecular Genetics, University of Virginia School of Medicine, Charlottesville, Virginia, USA.ORCID http://orcid.org/0000-0003-1578-8382
Falk NimmerjahnInstitute of Genetics, Department of Biology, University of Erlangen-Nürnberg, Erlangen, Germany.
Navin VaradarajanDepartment of Chemical and Biomolecular Engineering, University of Houston, Houston, Texas, USA.
Pierre BruhnsInstitut Pasteur, Department of Immunology, Unit of Antibodies in Therapy and Pathology, Paris, France.ORCID http://orcid.org/0000-0002-4709-8936
Yan Jessie ZhangDepartment of Molecular Biosciences, University of Texas at Austin, Austin, Texas, USA.
George GeorgiouDepartment of Chemical Engineering, University of Texas at Austin, Austin, Texas, USA.
The University of Texas at Austin · USInserm · FRFriedrich-Alexander-Universität Erlangen-Nürnberg · DEUniversity of Houston · USUniversity of Virginia · US

Funding

Gene-specific transcriptional silencing directed by dephosphorylation of RNAP IIR01GM104896 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI ZHANG, YAN JESSIE · 2013 to 2022
$2.4M
Quantitative single-cell biomarkers of T-cells to optimize tumor immunotherapyR01CA174385 · NCI · UNIVERSITY OF HOUSTON · PI COOPER, LAURENCE J.N., VARADARAJAN, NAVIN · 2012 to 2015
$2.1M
NCI NIH HHS R01 CA174385NIGMS NIH HHS R01 GM104896
6 · The paper itself

Abstract

Engineered crystallizable fragment (Fc) regions of antibody domains, which assume a unique and unprecedented asymmetric structure within the homodimeric Fc polypeptide, enable completely selective binding to the complement component C1q and activation of complement via the classical pathway without any concomitant engagement of the Fcγ receptor (FcγR). We used the engineered Fc domains to demonstrate in vitro and in mouse models that for therapeutic antibodies, complement-dependent cell-mediated cytotoxicity (CDCC) and complement-dependent cell-mediated phagocytosis (CDCP) by immunological effector molecules mediated the clearance of target cells with kinetics and efficacy comparable to those of the FcγR-dependent effector functions that are much better studied, while they circumvented certain adverse reactions associated with FcγR engagement. Collectively, our data highlight the importance of CDCC and CDCP in monoclonal-antibody function and provide an experimental approach for delineating the effect of complement-dependent effector-cell engagement in various therapeutic settings.

Indexed as

ImmunotherapyAnimalsAntibodies, MonoclonalBurkitt LymphomaCell Line, TumorChromatography, GelChromatography, LiquidComplement C1qCrystallizationCrystallography, X-RayCytotoxicity, ImmunologicEnzyme-Linked Immunosorbent AssayHumansImmunoglobulin Fc FragmentsImmunoglobulin GIn Vitro TechniquesAntibodies, MonoclonalComplement C1qImmunoglobulin Fc FragmentsImmunoglobulin GReceptors, IgG

Identifiers

PMID28604720
PMCPMC6015732
OpenAlexW2622901432

What OpenQuestion holds

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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.