Evidence map›Paper›PMID 41617027›Full record

ArticleThe Journal of biological chemistry2026

Engineered IgA-Fc fusion protein with bioactive nanobody neutralizes SARS-CoV-2 variants with mucosal delivery potential.

Rachel M Golonka, Lauren E Intravaia, Ala M Shaqra, Qi Li, Yongzhi Chen, Fiachra Humphries, Nese Kurt-Yilmaz, Kate A Fitzgerald, Celia A Schiffer, Yang Wang and 1 more

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Review
  2. Review
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

11 authors.

Rachel M GolonkaDivision of Innate Immunity, Department of Medicine, University of Massachusetts Chan Medical School, Worcester, Massachusetts, USA.
Lauren E IntravaiaDepartment of Biochemistry and Molecular Biotechnology, University of Massachusetts Chan Medical School, Worcester, Massachusetts, USA.
Ala M ShaqraDepartment of Biochemistry and Molecular Biotechnology, University of Massachusetts Chan Medical School, Worcester, Massachusetts, USA.
Qi LiDivision of Innate Immunity, Department of Medicine, University of Massachusetts Chan Medical School, Worcester, Massachusetts, USA.
Yongzhi ChenDivision of Innate Immunity, Department of Medicine, University of Massachusetts Chan Medical School, Worcester, Massachusetts, USA.
Fiachra HumphriesDivision of Innate Immunity, Department of Medicine, University of Massachusetts Chan Medical School, Worcester, Massachusetts, USA.
Nese Kurt-YilmazDepartment of Biochemistry and Molecular Biotechnology, University of Massachusetts Chan Medical School, Worcester, Massachusetts, USA.
Kate A FitzgeraldDivision of Innate Immunity, Department of Medicine, University of Massachusetts Chan Medical School, Worcester, Massachusetts, USA.
Celia A SchifferDepartment of Biochemistry and Molecular Biotechnology, University of Massachusetts Chan Medical School, Worcester, Massachusetts, USA.
Yang WangDivision of Innate Immunity, Department of Medicine, University of Massachusetts Chan Medical School, Worcester, Massachusetts, USA.
Lisa A CavaciniDivision of Innate Immunity, Department of Medicine, University of Massachusetts Chan Medical School, Worcester, Massachusetts, USA. Electronic address: lisa.cavacini@umassmed.edu.

Funding

Structure-guided and epitope-based design of potent and broadly neutralizing nanobodies for COVID-19 mucosal immunotherapyR01AI159182 · NIAID · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI Lisa A Cavacini, Katherine A. Fitzgerald · 2021 to 2026
$3.4M
NIAID NIH HHS R01 AI159182
6 · The paper itself

Abstract

The COVID-19 pandemic accelerated the development of monoclonal antibodies (mAb) targeting SARS-CoV-2, with IgG1-based mAbs dominating the therapeutic landscape. However, IgA-the predominant immunoglobulin at mucosal surfaces-represents a promising alternative for respiratory infections due to its natural role in immune exclusion and pathogen neutralization. Here, we engineered IgA-Fc fusion proteins conjugated with nanobodies (V

Indexed as

Antibodies, NeutralizingImmunoglobulin AImmunoglobulin Fc FragmentsRecombinant Fusion ProteinsSARS-CoV-2Single-Domain AntibodiesAnimalsAntibodies, ViralCamelids, New WorldCOVID-19HumansMiceProtein EngineeringSpike Glycoprotein, CoronavirusAntibodies, NeutralizingAntibodies, ViralImmunoglobulin AImmunoglobulin Fc FragmentsRecombinant Fusion ProteinsSingle-Domain AntibodiesSpike Glycoprotein, Coronavirusantibody engineeringdrug development and deliveryFc-fusion proteinimmunogenicityimmunoglobulin A (IgA)monoclonal antibodiesnanobody)recombinant protein expressionSARS-CoV-2single-domain antibody (sdAbstructural modeling

Identifiers

PMID41617027
PMCPMC13080570

What OpenQuestion holds

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LicenceCC BY
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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 OpenQuestion graph.