Evidence map›Paper›PMID 31913280›Full record

ArticleNature communications2020

The mechanistic and functional profile of the therapeutic anti-IgE antibody ligelizumab differs from omalizumab.

Pascal Gasser, Svetlana S Tarchevskaya, Pascal Guntern, Daniel Brigger, Rahel Ruppli, Noemi Zbären, Silke Kleinboelting, Christoph Heusser, Theodore S Jardetzky, Alexander Eggel

Open access · goldAbstract readComparative Study
PubMed Full text at PMC Publisher
In one paragraph

Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 95 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
95citing papers in PubMed, 1 pooled it
14.1field-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

95 citing papers in PubMed, 1 synthesis or guideline pooled it, 188 citations in OpenAlex.

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  5. Antibodies targeting a shared epitope exploit IgE allostery to drive distinct functional outcomes.Proceedings of the National Academy of Sciences of the United States of America · 2026
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35 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

10 authors at 4 institutions in 2 countries.

Pascal GasserDepartment of BioMedical Research, University of Bern, Bern, Switzerland.ORCID http://orcid.org/0000-0003-3708-1660
Svetlana S TarchevskayaDepartment of Structural Biology, Stanford University School of Medicine, Stanford, CA, 94305, USA.
Pascal GunternDepartment of BioMedical Research, University of Bern, Bern, Switzerland.ORCID http://orcid.org/0000-0001-8840-8577
Daniel BriggerDepartment of BioMedical Research, University of Bern, Bern, Switzerland.
Rahel RuppliDepartment of BioMedical Research, University of Bern, Bern, Switzerland.
Noemi ZbärenDepartment of BioMedical Research, University of Bern, Bern, Switzerland.
Silke KleinboeltingDepartment of Structural Biology, Stanford University School of Medicine, Stanford, CA, 94305, USA.
Christoph HeusserPharmaceutical Research, Novartis AG, 4002, Basel, Switzerland.
Theodore S JardetzkyDepartment of Structural Biology, Stanford University School of Medicine, Stanford, CA, 94305, USA. tjardetzky@stanford.edu.ORCID http://orcid.org/0000-0002-3664-0072
Alexander EggelDepartment of BioMedical Research, University of Bern, Bern, Switzerland. alexander.eggel@dbmr.unibe.ch.ORCID http://orcid.org/0000-0001-8746-3339
University of Bern · CHStanford University · USNovartis (Switzerland) · CHStanford Medicine · US

Funding

Accelerated dissociation of IgE receptor complexesR01AI115469 · NIAID · STANFORD UNIVERSITY · PI Theodore S Jardetzky · 2017 to 2026
$3.8M
Suppression of basophil activation by IgE glycovariantsR01HL141493 · NHLBI · STANFORD UNIVERSITY · PI JARDETZKY, THEODORE S · 2018 to 2021
$1.6M
NHLBI NIH HHS R01 HL141493NIAID NIH HHS R01 AI115469
6 · The paper itself

Abstract

Targeting of immunoglobulin E (IgE) represents an interesting approach for the treatment of allergic disorders. A high-affinity monoclonal anti-IgE antibody, ligelizumab, has recently been developed to overcome some of the limitations associated with the clinical use of the therapeutic anti-IgE antibody, omalizumab. Here, we determine the molecular binding profile and functional modes-of-action of ligelizumab. We solve the crystal structure of ligelizumab bound to IgE, and report epitope differences between ligelizumab and omalizumab that contribute to their qualitatively distinct IgE-receptor inhibition profiles. While ligelizumab shows superior inhibition of IgE binding to FcεRI, basophil activation, IgE production by B cells and passive systemic anaphylaxis in an in vivo mouse model, ligelizumab is less potent in inhibiting IgE:CD23 interactions than omalizumab. Our data thus provide a structural and mechanistic foundation for understanding the efficient suppression of FcεRI-dependent allergic reactions by ligelizumab in vitro as well as in vivo.

Indexed as

AnimalsAnti-Allergic AgentsAntibodies, Anti-IdiotypicAntibodies, Monoclonal, HumanizedBasophilsB-LymphocytesHumansHypersensitivityImmunoglobulin EMiceMice, Inbred C57BLMice, TransgenicOmalizumabReceptors, IgEAnti-Allergic AgentsAntibodies, Anti-IdiotypicAntibodies, Monoclonal, Humanizedanti-IgE antibodiesImmunoglobulin EligelizumabOmalizumabReceptors, IgE

Identifiers

PMID31913280
PMCPMC6949303
OpenAlexW2999840425

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.