Evidence map›Paper›PMID 42664341›Full record

ArticleScience advances2026

Structure-function analysis of the FCRL5-IgG1 Fc complex reveals an unappreciated pathway for B cell modulation by Fc-attenuated IgG.

Bart M Herpers, Mo Guo, Sanghwan Ko, George Delidakis, Jin Eyun Kim, Chang-Han Lee, Mohamed I Gadallah, Jennifer S Brodbelt, Y Jessie Zhang, George Georgiou

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Science advances, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
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

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

10 authors.

Bart M HerpersDepartment of Biomedical Engineering, University of Texas at Austin, Austin, TX, USA.ORCID 0009-0009-6771-4810
Mo GuoDepartment of Molecular Biosciences, University of Texas at Austin, Austin, TX, USA.ORCID 0009-0000-9103-975X
Sanghwan KoDepartment of Chemical Engineering, University of Texas at Austin, Austin, TX, USA.
George DelidakisDepartment of Chemical Engineering, University of Texas at Austin, Austin, TX, USA.ORCID 0000-0002-4330-9476
Jin Eyun KimDepartment of Biomedical Engineering, University of Texas at Austin, Austin, TX, USA.ORCID 0000-0002-6297-3292
Chang-Han LeeDepartment of Chemical Engineering, University of Texas at Austin, Austin, TX, USA.ORCID 0000-0002-7156-4423
Mohamed I GadallahDepartment of Chemistry, University of Texas at Austin, Austin, TX, USA.
Jennifer S BrodbeltDepartment of Chemistry, University of Texas at Austin, Austin, TX, USA.ORCID 0000-0003-3207-0217
Y Jessie ZhangDepartment of Molecular Biosciences, University of Texas at Austin, Austin, TX, USA.ORCID 0000-0002-9360-5388
George GeorgiouDepartment of Molecular Biosciences, University of Texas at Austin, Austin, TX, USA.ORCID 0000-0002-8823-3073

Funding

Ultraviolet Photodissociation Mass Spectrometry for Characterization of Biological MoleculesR35GM139658 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI BRODBELT, JENNIFER S. · 2021 to 2025
$2.9M
Systematic, molecular level analysis of the Fc receptor ligation on antibody effector functionsU01AI148118 · NIAID · UNIVERSITY OF TEXAS AT AUSTIN · PI GEORGIOU, GEORGE GEORGIOU, VARADARAJAN, NAVIN · 2020 to 2024
$2.3M
Deciphering the phosphorylation pattern of RNA polymerase II for eukaryotic transcriptionR35GM148356 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI Yan Jessie Zhang · 2023 to 2026
$2.3M
NIAID NIH HHS U01 AI148118NIGMS NIH HHS R35 GM139658NIGMS NIH HHS R35 GM148356
6 · The paper itself

Abstract

The Fc region of therapeutic IgG antibodies is often engineered to remove or "silence" Fc effector functions, but it remains unclear whether these mutations eliminate all Fc-mediated effector activity. Human Fc receptor-like 5 (FCRL5/FcRH5) is a low-affinity IgG Fc receptor expressed on B cells and is an actively pursued antibody target in multiple myeloma. Here, we show that common Fc function-silencing mutations do not impair FCRL5-mediated activity and therefore attenuate, rather than eliminate, Fc effector function. The crystal structure of the FCRL5-IgG1 Fc complex, solved at 3.4 Å resolution, revealed that FCRL5 binds IgG1 Fc in a 1:1 complex through a binding mode distinct from that of classical Fcγ receptors, explaining why mutations that attenuate Fc effector function spare FCRL5 binding. Fc-engineered antibodies that selectively engage FCRL5 inhibited B cell receptor-induced Ca

Indexed as

B-LymphocytesImmunoglobulin Fc FragmentsImmunoglobulin GReceptors, FcCrystallography, X-RayHumansModels, MolecularMutationProtein BindingStructure-Activity RelationshipFCRL5 protein, humanImmunoglobulin Fc FragmentsImmunoglobulin GReceptors, Fc

Identifiers

PMID42664341
PMCPMC13524021

What Socratic holds

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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 Socratic graph.