Evidence map›Paper›PMID 40610439›Full record

ArticleNature communications2025

Discovery of a single-subunit oligosaccharyltransferase that enables glycosylation of full-length IgG antibodies in bacteria.

Belen Sotomayor, Thomas C Donahue, Sai Pooja Mahajan, May N Taw, Sophia W Hulbert, Erik J Bidstrup, D Natasha Owitipana, Alexandra Pang, Xu Yang, Souvik Ghosal and 6 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. Article
  2. Review
  3. Antibody glycosylation in neuroimmune diseases.Journal of translational medicine · 2025
    Review
  4. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

16 authors.

Belen SotomayorRobert Frederick Smith School of Chemical and Biomolecular Engineering, Cornell University, Ithaca, NY, 14853, USA.ORCID http://orcid.org/0000-0002-3786-7252
Thomas C DonahueRobert Frederick Smith School of Chemical and Biomolecular Engineering, Cornell University, Ithaca, NY, 14853, USA.
Sai Pooja MahajanDepartment of Chemical and Biomolecular Engineering, Johns Hopkins University, Baltimore, MD, 21218, USA.
May N TawDepartment of Microbiology, Cornell University, Ithaca, NY, 14853, USA.ORCID http://orcid.org/0000-0002-8196-5765
Sophia W HulbertBiochemistry, Molecular and Cell Biology, Cornell University, Ithaca, NY, 14853, USA.
Erik J BidstrupRobert Frederick Smith School of Chemical and Biomolecular Engineering, Cornell University, Ithaca, NY, 14853, USA.ORCID http://orcid.org/0000-0001-9014-2042
D Natasha OwitipanaDepartment of Chemistry and Biochemistry, University of Maryland, College Park, MD, 20742, USA.
Alexandra PangRobert Frederick Smith School of Chemical and Biomolecular Engineering, Cornell University, Ithaca, NY, 14853, USA.
Xu YangComplex Carbohydrate Research Center, University of Georgia, 315 Riverbend Road, Athens, GA, 30602-4712, USA.ORCID http://orcid.org/0000-0001-9802-9845
Souvik GhosalDepartment of Chemistry and Chemical Biology, Cornell University, Ithaca, NY, 14853, USA.ORCID http://orcid.org/0000-0003-2412-0544
Christopher A AlabiRobert Frederick Smith School of Chemical and Biomolecular Engineering, Cornell University, Ithaca, NY, 14853, USA.ORCID http://orcid.org/0000-0003-2654-018X
Parastoo AzadiComplex Carbohydrate Research Center, University of Georgia, 315 Riverbend Road, Athens, GA, 30602-4712, USA.
Jeffrey J GrayDepartment of Chemical and Biomolecular Engineering, Johns Hopkins University, Baltimore, MD, 21218, USA.ORCID http://orcid.org/0000-0001-6380-2324
Michael C JewettDepartment of Bioengineering, Stanford University, Stanford, CA, 94305, USA.ORCID http://orcid.org/0000-0003-2948-6211
Lai-Xi WangDepartment of Chemistry and Biochemistry, University of Maryland, College Park, MD, 20742, USA.ORCID http://orcid.org/0000-0003-4293-5819
Matthew P DeLisaRobert Frederick Smith School of Chemical and Biomolecular Engineering, Cornell University, Ithaca, NY, 14853, USA. md255@cornell.edu.ORCID http://orcid.org/0000-0003-3226-1566

Funding

National Glycoscience Resource- CCRC Service and Training - NGlycoR@CCRCR24GM137782 · NIGMS · UNIVERSITY OF GEORGIA · PI Parastoo Azadi · 2020 to 2026
$5.2M
Covergent Chemoenzymatic Synthesis of Glycopeptides and GlycoproteinsR01GM080374 · NIGMS · UNIV OF MARYLAND, COLLEGE PARK · PI WANG, LAI-XI · 2007 to 2021
$3.9M
Training future leaders at the chemistry-biology interfaceT32GM138826 · NIGMS · CORNELL UNIVERSITY · PI Jeremy Baskin · 2021 to 2026
$2.6M
Technologies to predict and probe glycosyl transferR01GM127578 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI GRAY, JEFFREY J · 2018 to 2020
$1.6M
Immuno-Engineering: Integrated Engineering and Immunology TrainingT32EB023860 · NIBIB · CORNELL UNIVERSITY · PI AUGUST, AVERY, PUTNAM, DAVID A · 2018 to 2022
$933k
National Science Foundation (NSF) CBET-1605242, CBET-1936823, MCB-1413563, DMR-1933525NIBIB NIH HHS T32 EB023860NIGMS NIH HHS R01 GM080374NIGMS NIH HHS R01 GM127578NIGMS NIH HHS R24 GM137782NIGMS NIH HHS T32 GM138826United States Department of Defense | Defense Advanced Research Projects Agency (DARPA) W911NF-23-2-0039United States Department of Defense | Defense Threat Reduction Agency (DTRA) HDTRA1-15-10052, HDTRA1-20-10004U.S. Department of Health & Human Services | NIH | National Institute of General Medical Sciences (NIGMS) R01GM127578, R01GM080374, R24GM137782
6 · The paper itself

Abstract

Human immunoglobulin G (IgG) antibodies are a major class of biotherapeutics and undergo N-linked glycosylation in their Fc domain, which is critical for immune functions and therapeutic activity. Hence, technologies for producing authentically glycosylated IgGs are in high demand. Previous attempts to engineer Escherichia coli for this purpose have met limited success due in part to the lack of oligosaccharyltransferase (OST) enzymes that can install N-glycans at the conserved N297 site in the Fc region. Here, we identify a single-subunit OST from Desulfovibrio marinus with relaxed substrate specificity that catalyzes glycosylation of native Fc acceptor sites. By chemoenzymatic remodeling the attached bacterial glycans to homogeneous, asialo complex-type G2 N-glycans, the E. coli-derived Fc binds human FcγRIIIa/CD16a, a key receptor for antibody-dependent cellular cytotoxicity (ADCC). Overall, the discovery of D. marinus OST provides previously unavailable biocatalytic capabilities and sets the stage for using E. coli to produce fully human antibodies.

Indexed as

Bacterial ProteinsEscherichia coliHexosyltransferasesImmunoglobulin GMembrane ProteinsGlycosylationHumansImmunoglobulin Fc FragmentsPolysaccharidesReceptors, IgGSubstrate SpecificityBacterial Proteinsdolichyl-diphosphooligosaccharide - protein glycotransferaseHexosyltransferasesImmunoglobulin Fc FragmentsImmunoglobulin GMembrane ProteinsPolysaccharidesReceptors, IgG

Identifiers

PMID40610439
PMCPMC12229607

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.