Evidence map›Paper›PMID 41278654›Full record

ArticlebioRxiv : the preprint server for biology2025

Human coronavirus HKU1 neutralization by glycan receptor mimicry.

Ziqi Feng, Nurgun Kose, Fernando R Moreira, Anne L M Kimpel, Jeffrey Copps, Naveenchandra Suryadevara, Daniel J Jackson, James E Gern, Ian A Wilson, Sheng Li and 5 more

Abstract readPreprint
In one paragraph

Article in bioRxiv : the preprint server for biology, 2025. 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

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

15 authors.

Ziqi FengDepartment of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.ORCID 0000-0001-5046-9788
Nurgun KoseVanderbilt Center for Antibody Therapeutics, Vanderbilt University Medical Center, Nashville, TN 37232, USA.ORCID 0000-0001-7425-292X
Fernando R MoreiraDepartment of Epidemiology, Gillings School of Global Public Health, University of North Carolina, Chapel Hill, NC 27599, USA.
Anne L M KimpelDepartment of Chemical Biology & Drug Discovery, Utrecht Institute for Pharmaceutical Sciences, Utrecht University, 3584 CG Utrecht, The Netherlands.
Jeffrey CoppsDepartment of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.ORCID 0000-0003-4793-7258
Naveenchandra SuryadevaraVanderbilt Center for Antibody Therapeutics, Vanderbilt University Medical Center, Nashville, TN 37232, USA.ORCID 0000-0003-2571-1290
Daniel J JacksonDepartment of Pediatrics, School of Medicine and Public Health, University of Wisconsin, Madison, WI 53792, USA.ORCID 0000-0001-6938-2690
James E GernDepartment of Pediatrics, School of Medicine and Public Health, University of Wisconsin, Madison, WI 53792, USA.ORCID 0000-0002-6667-4708
Ian A WilsonDepartment of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.ORCID 0000-0002-6469-2419
Sheng LiDepartment of Medicine, University of California San Diego, La Jolla, CA 92093, USA.
Robert P de VriesDepartment of Chemical Biology & Drug Discovery, Utrecht Institute for Pharmaceutical Sciences, Utrecht University, 3584 CG Utrecht, The Netherlands.ORCID 0000-0002-1586-4464
Ralph S BaricDepartment of Epidemiology, Gillings School of Global Public Health, University of North Carolina, Chapel Hill, NC 27599, USA.ORCID 0000-0001-6827-8701
Sandhya BangaruDepartment of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.ORCID 0000-0001-7994-4693
James E CroweVanderbilt Center for Antibody Therapeutics, Vanderbilt University Medical Center, Nashville, TN 37232, USA.ORCID 0000-0002-0049-1079
Andrew B WardDepartment of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.ORCID 0000-0001-7153-3769

Funding

Identification of neutralizing epitopes on SARS-CoV-2 spike for design of vaccines and small-molecule antiviralsUM1AI144462 · NIAID · SCRIPPS RESEARCH INSTITUTE, THE · PI BURTON, DENNIS R. · 2019 to 2025
$201.6M
Wisconsin Infant Study Cohort (WISC) ECHO Pediatric Follow-UpUH3OD023282 · OD · UNIVERSITY OF WISCONSIN-MADISON · PI James E. Gern · 2018 to 2026
$64.8M
Virus-Bacterial Interactions and Exacerba of AsthmaP01HL070831 · NHLBI · UNIVERSITY OF WISCONSIN-MADISON · PI BOCHKOV, YURY A · 2002 to 2017
$31.3M
Human antibody-based countermeasures against the Wuhan Coronavirus SARS-CoV-2R01AI157155 · NIAID · WASHINGTON UNIVERSITY · PI BARIC, RALPH S, CROWE, JAMES E · 2020 to 2024
$6.0M
Structure, Function and Antigenicity of Coronavirus Spike ProteinsR01AI127521 · NIAID · UNIVERSITY OF TEXAS AT AUSTIN · PI MCLELLAN, JASON SCOTT, WARD, ANDREW BARRETT · 2017 to 2021
$3.1M
Gates Foundation INV-004923NHLBI NIH HHS P01 HL070831NIAID NIH HHS R01 AI127521NIAID NIH HHS R01 AI157155NIAID NIH HHS UM1 AI144462NIH HHS UH3 OD023282
6 · The paper itself

Abstract

Entry of seasonal human coronavirus HKU1 (HCoV-HKU1) into host cells is facilitated by sequential binding to sialoglycans and transmembrane serine protease 2 (TMPRSS2) receptors. However, the neutralizing capacity of antibodies disrupting these receptor interactions have not been examined. Here, we describe the isolation and characterization of a human monoclonal antibody (mAb) HKU1-2 that recognizes the HCoV-HKU1 spike protein and exhibits dose-dependent neutralization of the virus. Epitope mapping and structural analysis revealed that HKU1-2 mAb targets the sialoglycan binding site in the N-terminal domain of the spike protein. A cryo-electron microscopy (cryo-EM) structure of the spike-Fab complex further demonstrated the ability of HKU1-2 to mimic sialic acid binding thereby effectively blocking sialoglycan receptor engagement. HKU1-2 binding is primarily mediated by CDRH3 recognition of NTD residues K80 and W89 that are known to be critical for sialic acid engagement. Overall, our results demonstrate antibody recognition and neutralization of HCoV-HKU1 by receptor mimicry.

Indexed as

HKU1neutralizing antibodyseasonal coronavirussialic acid receptorspike protein

Identifiers

PMID41278654
PMCPMC12637458

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.