Evidence map›Paper›PMID 41639433›Full record

ArticleNature chemical biology2026

Uncovering bacterial pseudaminylation with pan-specific antibody tools.

Arthur H Tang, Niccolay Madiedo Soler, Kristian I Karlic, Leo Corcilius, Caitlin E Clarke-Shepperson, Christopher Lehmann, Aleksandra W Debowski, Ashleigh L Dale, Lauren Zavan, Michelle Cielesh and 22 more

Abstract read
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In one paragraph

Article in Nature chemical biology, 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

32 authors.

Arthur H Tang *School of Chemistry, The University of Sydney, Sydney, New South Wales, Australia.
Niccolay Madiedo Soler *The Walter and Eliza Hall Institute of Medical Research, Parkville, Victoria, Australia.ORCID http://orcid.org/0000-0003-3689-9305
Kristian I Karlic *Department of Microbiology and Immunology, University of Melbourne at the Peter Doherty Institute for Infection and Immunity, Melbourne, Victoria, Australia.ORCID http://orcid.org/0000-0003-4408-734X
Leo CorciliusSchool of Chemistry, The University of Sydney, Sydney, New South Wales, Australia.
Caitlin E Clarke-SheppersonSchool of Chemistry, The University of Sydney, Sydney, New South Wales, Australia.
Christopher LehmannSchool of Chemistry, The University of Sydney, Sydney, New South Wales, Australia.
Aleksandra W DebowskiMarshall Centre for Infectious Disease Research and Training, School of Biomedical Sciences, The University of Western Australia, Nedlands, Western Australia, Australia.
Ashleigh L DaleSchool of Life and Environmental Sciences, The University of Sydney, Sydney, New South Wales, Australia.
Lauren ZavanDepartment of Microbiology and Immunology, University of Melbourne at the Peter Doherty Institute for Infection and Immunity, Melbourne, Victoria, Australia.
Michelle CieleshCharles Perkins Centre, The University of Sydney, Sydney, New South Wales, Australia.
Adedunmola P AdewaleDepartment of Chemistry and Biochemistry, Bowdoin College, Brunswick, ME, USA.
Karen D MoultonDepartment of Chemistry and Biochemistry, Bowdoin College, Brunswick, ME, USA.
Lucy LiDepartment of Microbiology and Immunology, University of Melbourne at the Peter Doherty Institute for Infection and Immunity, Melbourne, Victoria, Australia.
Chenzheng GuanThe Walter and Eliza Hall Institute of Medical Research, Parkville, Victoria, Australia.ORCID http://orcid.org/0009-0005-7605-873X
Christopher McCroryDepartment of Microbiology and Immunology, University of Melbourne at the Peter Doherty Institute for Infection and Immunity, Melbourne, Victoria, Australia.ORCID http://orcid.org/0009-0002-2137-1831
Maria Kaparakis-LiaskosDepartment of Microbiology and Immunology, University of Melbourne at the Peter Doherty Institute for Infection and Immunity, Melbourne, Victoria, Australia.
Benjamin P HowdenDepartment of Microbiology and Immunology, University of Melbourne at the Peter Doherty Institute for Infection and Immunity, Melbourne, Victoria, Australia.
Norelle L SherryDepartment of Microbiology and Immunology, University of Melbourne at the Peter Doherty Institute for Infection and Immunity, Melbourne, Victoria, Australia.ORCID http://orcid.org/0000-0002-7789-8360
Ruohan WeiDepartment of Chemistry, State Key Laboratory of Synthetic Chemistry, The University of Hong Kong, Hong Kong, People's Republic of China.
Xuechen LiDepartment of Chemistry, State Key Laboratory of Synthetic Chemistry, The University of Hong Kong, Hong Kong, People's Republic of China.ORCID http://orcid.org/0000-0001-5465-7727
Ruth M HallSchool of Life and Environmental Science, The University of Sydney, Sydney, New South Wales, Australia.ORCID http://orcid.org/0000-0003-2062-3312
Johanna J KenyonInstitute for Biomedicine and Glycomics, Griffith University, Southport, Queensland, Australia.ORCID http://orcid.org/0000-0002-1487-6105
Linda M WakimDepartment of Microbiology and Immunology, University of Melbourne at the Peter Doherty Institute for Infection and Immunity, Melbourne, Victoria, Australia.
Francesca L ShortInfection Program and Department of Microbiology, Biomedicine Discovery Institute, Monash University, Clayton, Victoria, Australia.
Danielle H DubeDepartment of Chemistry and Biochemistry, Bowdoin College, Brunswick, ME, USA.ORCID http://orcid.org/0000-0001-5986-8945
Stuart J CordwellSchool of Life and Environmental Sciences, The University of Sydney, Sydney, New South Wales, Australia.
Mark LaranceCharles Perkins Centre, The University of Sydney, Sydney, New South Wales, Australia.ORCID http://orcid.org/0000-0002-8579-2267
Keith A StubbsSchool of Molecular Sciences, The University of Western Australia, Crawley, Western Australia, Australia.ORCID http://orcid.org/0000-0001-6899-402X
Glen P CarterDepartment of Microbiology and Immunology, University of Melbourne at the Peter Doherty Institute for Infection and Immunity, Melbourne, Victoria, Australia.ORCID http://orcid.org/0000-0002-7306-9362
Nichollas E ScottDepartment of Microbiology and Immunology, University of Melbourne at the Peter Doherty Institute for Infection and Immunity, Melbourne, Victoria, Australia. nichollas.scott@unimelb.edu.au.ORCID http://orcid.org/0000-0003-2556-8316
Ethan D Goddard-BorgerThe Walter and Eliza Hall Institute of Medical Research, Parkville, Victoria, Australia. goddard-borger.e@wehi.edu.au.ORCID http://orcid.org/0000-0002-8181-9733
Richard J PayneSchool of Chemistry, The University of Sydney, Sydney, New South Wales, Australia. richard.payne@sydney.edu.au.ORCID http://orcid.org/0000-0002-3618-9226

Funding

Department of Education and Training | Australian Research Council (ARC) DP210100362Department of Health | National Health and Medical Research Council (NHMRC) GNT1174941Department of Health | National Health and Medical Research Council (NHMRC) GNT2000517Department of Health | National Health and Medical Research Council (NHMRC) GNT2018980Department of Health | National Health and Medical Research Council (NHMRC) GNT2027601Department of Health | National Health and Medical Research Council (NHMRC) GNT2033340Foundation for the National Institutes of Health (Foundation for the National Institutes of Health, Inc.) GM109397
6 · The paper itself

Abstract

Pseudaminic acids (Pse) are a family of carbohydrates found within bacterial lipopolysaccharides, capsular polysaccharides and glycoproteins that are critical for the virulence of human pathogens. However, a dearth of effective tools for detecting and enriching Pse has restricted study to only the most abundant Pse-containing glycoconjugates. Here we devise a synthesis of α- and β-O-pseudaminylated glycopeptides to generate 'pan-specific' monoclonal antibodies (mAbs) that recognize α- and β-configured Pse with diverse N7 acyl groups, as well as its C8 epimer (8ePse), presented within glycans or directly linked to polypeptide backbones. Structural characterization reveals the molecular basis of Pse recognition across a range of diverse chemical contexts. Using these mAbs, we establish a glycoproteomic workflow to map the Pse glycome of Helicobacter pylori, Campylobacter jejuni and Acinetobacter baumannii strains. Finally, we demonstrate that the mAbs recognize diverse capsule types in multidrug-resistant Acinetobacter baumannii and enhance phagocytosis to eliminate infections in mice.

Indexed as

Antibodies, MonoclonalSugar AcidsAcinetobacter baumanniiAnimalsCampylobacter jejuniGlycopeptidesHelicobacter pyloriHumansMicePhagocytosisAntibodies, MonoclonalGlycopeptidesSugar Acids

Identifiers

PMID41639433

What OpenQuestion holds

Textmetadata
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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.