Evidence map›Paper›PMID 41421343›Full record

ArticleStructure (London, England : 1993)2026

The impact of N-glycan conformational entropy on the binding affinity of Fc γ receptor IIIa/CD16a.

Paul G Kremer, William D Tolbert, Eliza Gazaway, Braulio G Hernandez, Marek K Korzeniowski, Zofia A Dyba, Tobias Grelsson, Oliver C Grant, William N Lanzilotta, Marzena Pazgier and 2 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Structure (London, England : 1993), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Article
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

12 authors.

Paul G KremerDepartment of Biochemistry and Molecular Biology, University of Georgia, Athens, GA, USA.
William D TolbertInfectious Disease Division, Department of Medicine, Uniformed Services University of the Health Sciences, Bethesda, MD, USA; Henry M. Jackson Foundation for the Advancement of Military Medicine, Inc., Bethesda, MD, USA.
Eliza GazawayDepartment of Biochemistry and Molecular Biology, University of Georgia, Athens, GA, USA; Complex Carbohydrate Research Center, University of Georgia, Athens, GA, USA.
Braulio G HernandezDepartment of Biochemistry and Molecular Biology, University of Georgia, Athens, GA, USA.
Marek K KorzeniowskiInfectious Disease Division, Department of Medicine, Uniformed Services University of the Health Sciences, Bethesda, MD, USA; Henry M. Jackson Foundation for the Advancement of Military Medicine, Inc., Bethesda, MD, USA.
Zofia A DybaInfectious Disease Division, Department of Medicine, Uniformed Services University of the Health Sciences, Bethesda, MD, USA; Department of Chemistry and Biochemistry, University of Maryland, College Park, MD, USA.
Tobias GrelssonComplex Carbohydrate Research Center, University of Georgia, Athens, GA, USA.
Oliver C GrantComplex Carbohydrate Research Center, University of Georgia, Athens, GA, USA.
William N LanzilottaDepartment of Biochemistry and Molecular Biology, University of Georgia, Athens, GA, USA.
Marzena PazgierInfectious Disease Division, Department of Medicine, Uniformed Services University of the Health Sciences, Bethesda, MD, USA.
Robert J WoodsDepartment of Biochemistry and Molecular Biology, University of Georgia, Athens, GA, USA; Complex Carbohydrate Research Center, University of Georgia, Athens, GA, USA.
Adam W BarbDepartment of Biochemistry and Molecular Biology, University of Georgia, Athens, GA, USA; Complex Carbohydrate Research Center, University of Georgia, Athens, GA, USA; Department of Chemistry, University of Georgia, Athens, GA, USA. Electronic address: abarb@uga.edu.

Funding

Structure-Function Analytics CoreP01AI162242 · NIAID · DUKE UNIVERSITY · PI TOMARAS, GEORGIA DORIS · 2021 to 2025
$22.2M
Selecting HA glycosylation for improved vaccine responsesR01AI155975 · NIAID · BOSTON UNIVERSITY MEDICAL CAMPUS · PI WAN, XIUFENG HENRY, WOODS, ROBERT J · 2021 to 2025
$4.0M
A new strategy to eliminate HIV-1-infected cells by unlocking the Env trimerR01AI174908 · NIAID · HENRY M. JACKSON FDN FOR THE ADV MIL/MED · PI Marzena Elzbieta Pazgier · 2023 to 2026
$2.8M
Composition and structure of antibody receptors at the surface of primary human cells during immune activationU01AI148114 · NIAID · UNIVERSITY OF GEORGIA · PI BARB, ADAM WESLEY, MACE, EMILY MARGARET · 2020 to 2024
$2.0M
Transitioning GLYCAM-Web to a self-sustaining carbohydrate modeling serviceR24GM136984 · NIGMS · UNIVERSITY OF GEORGIA · PI WOODS, ROBERT J · 2020 to 2022
$1.4M
Increasing the protective capacity of antibodies by enhancing Fc-mediated responsesR01AI187028 · NIAID · UNIVERSITY OF GEORGIA · PI Adam Wesley Barb, Jarrod Mousa · 2025 to 2026
$833k
NIAID NIH HHS P01 AI162242NIAID NIH HHS R01 AI155975NIAID NIH HHS R01 AI174908NIAID NIH HHS R01 AI187028NIAID NIH HHS U01 AI148114NIGMS NIH HHS R24 GM136984
6 · The paper itself

Abstract

The affinity of Fc γ receptor IIIa (FcγRIIIa) binding to immunoglobulin G1 (IgG1) correlates with patient responses for antibody-based therapeutics. Among multiple factors affecting affinity, a mechanism defining how the composition of the FcγRIIIa N162 glycan regulates affinity remains undefined. Here, we evaluate the binding modes of two competitive FcγRIIIa ligands. IgG1 Fc binding is sensitive to N162 glycan composition, unlike the antigen-binding fragment (Fab) of the FcγRIII-specific antibody 3G8. Both ligands bound to overlapping surfaces, utilizing different angles of attack such that the IgG1 Fc but not 3G8 Fab limited the space available to the FcγRIII N162 N-glycan. FcγRIII binding to IgG1 Fc generated a 2.1 kcal/mol penalty from a loss of N162 glycan conformational entropy, greater than the 0.3 kcal/mol penalty for 3G8 and consistent with binding measurements. Thus, the conformational entropy of the FcγRIIIa N162-glycan is the predominant force modulating differential binding affinity compared to 3G8 Fab binding for endogenous FcγRIIIa glycoforms.

Indexed as

Immunoglobulin GPolysaccharidesReceptors, IgGBinding SitesEntropyHumansImmunoglobulin Fab FragmentsImmunoglobulin Fc FragmentsLigandsProtein BindingProtein ConformationFCGR3A protein, humanImmunoglobulin Fab FragmentsImmunoglobulin Fc FragmentsImmunoglobulin GLigandsPolysaccharidesReceptors, IgGADCCantibodyglycobiologyimmunobiologyimmunology

Identifiers

PMID41421343
PMCPMC12983350

What OpenQuestion holds

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LicenceTDM
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.