Evidence map›Paper›PMID 40113779›Full record

ArticleNature communications2025

Structure and unusual binding mechanism of the hyaluronan receptor LYVE-1 mediating leucocyte entry to lymphatics.

Fouzia Bano, Suneale Banerji, Tao Ni, Dixy E Green, Kalila R Cook, Iain W Manfield, Paul L DeAngelis, Emanuele Paci, Martin Lepšík, Robert J C Gilbert and 2 more

Abstract read
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 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing 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

17 citing papers in PubMed.

  1. Review
  2. Review
  3. Ocular Lymphatics in Health and Disease.Diagnostics (Basel, Switzerland) · 2026
    Review
  4. Article
  5. Review
  6. Article
  7. Article
  8. Review
  9. Review
  10. Article
  11. Review
  12. Lung Lymphatics in Edema, Inflammation, and Thrombosis.Arteriosclerosis, thrombosis, and vascular biology · 2025
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Hyaluronan: An Architect and Integrator for Cancer and Neural Diseases.International journal of molecular sciences · 2025
    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

12 authors.

Fouzia Bano *School of Biomedical Sciences, Faculty of Biological Sciences, University of Leeds, Leeds, LS2 9JT, UK.ORCID http://orcid.org/0000-0003-0634-7091
Suneale Banerji *Medical Research Council Translational Immune Discovery Unit, MRC Weatherall Institute of Molecular Medicine, University of Oxford, Oxford, OX3 9DS, UK.
Tao Ni *Division of Structural Biology, Wellcome Trust Centre for Human Genetics, University of Oxford, Roosevelt Drive, Oxford, OX3 7BN, UK.ORCID http://orcid.org/0000-0001-7268-0306
Dixy E GreenDepartment of Biochemistry and Physiology, University of Oklahoma Health Sciences Center, Oklahoma City, OK, 73126, USA.ORCID http://orcid.org/0000-0002-6237-0889
Kalila R CookSchool of Biomedical Sciences, Faculty of Biological Sciences, University of Leeds, Leeds, LS2 9JT, UK.
Iain W ManfieldAstbury Centre for Structural Molecular Biology, University of Leeds, Leeds, LS2 9JT, UK.ORCID http://orcid.org/0000-0003-3765-0325
Paul L DeAngelisDepartment of Biochemistry and Physiology, University of Oklahoma Health Sciences Center, Oklahoma City, OK, 73126, USA.ORCID http://orcid.org/0000-0002-8843-1344
Emanuele PaciAstbury Centre for Structural Molecular Biology, University of Leeds, Leeds, LS2 9JT, UK.
Martin LepšíkCERMAV, Université Grenoble Alpes, CNRS, 38000, Grenoble, France. martin.lepsik@uochb.cas.cz.ORCID http://orcid.org/0000-0003-2607-8132
Robert J C GilbertDivision of Structural Biology, Wellcome Trust Centre for Human Genetics, University of Oxford, Roosevelt Drive, Oxford, OX3 7BN, UK. robert.gilbert@magd.ox.ac.uk.ORCID http://orcid.org/0000-0001-9336-5604
Ralf P RichterSchool of Biomedical Sciences, Faculty of Biological Sciences, University of Leeds, Leeds, LS2 9JT, UK. r.richter@leeds.ac.uk.ORCID http://orcid.org/0000-0003-3071-2837
David G JacksonMedical Research Council Translational Immune Discovery Unit, MRC Weatherall Institute of Molecular Medicine, University of Oxford, Oxford, OX3 9DS, UK. david.jackson@imm.ox.ac.uk.ORCID http://orcid.org/0000-0002-4133-9364

Funding

EC | EC Seventh Framework Programm | FP7 Ideas: European Research Council (FP7-IDEAS-ERC - Specific Programme: "Ideas" Implementing the Seventh Framework Programme of the European Community for Research, Technological Development and Demonstration Activities (2007 to 2013)) ERC-2012-StG-306435EC | Horizon 2020 Framework Programme (EU Framework Programme for Research and Innovation H2020) 795605RCUK | Biotechnology and Biological Sciences Research Council (BBSRC) BB/R000174/1RCUK | Biotechnology and Biological Sciences Research Council (BBSRC) BB/X00158X/1RCUK | Biotechnology and Biological Sciences Research Council (BBSRC) BB/X007278/1RCUK | Medical Research Council (MRC) MC_UU_00008/2RCUK | Medical Research Council (MRC) MR/N000331/1RCUK | Medical Research Council (MRC) MR/X013227/1Wellcome Trust
6 · The paper itself

Abstract

Immune surveillance involves the continual migration of antigen-scavenging immune cells from the tissues to downstream lymph nodes via lymphatic vessels. To enable such passage, cells first dock with the lymphatic entry receptor LYVE-1 on the outer surface of endothelium, using their endogenous hyaluronan glycocalyx, anchored by a second hyaluronan receptor, CD44. Why the process should require two different hyaluronan receptors and by which specific mechanism the LYVE-1•hyaluronan interaction enables lymphatic entry is however unknown. Here we describe the crystal structures and binding mechanics of murine and human LYVE-1•hyaluronan complexes. These reveal a highly unusual, sliding mode of ligand interaction, quite unlike the conventional sticking mode of CD44, in which the receptor grabs free hyaluronan chain-ends and winds them in through conformational re-arrangements in a deep binding cleft, lubricated by a layer of structured waters. Our findings explain the mode of action of a dedicated lymphatic entry receptor and define a distinct, low tack adhesive interaction that enables migrating immune cells to slide through endothelial junctions with minimal resistance, while clinging onto their hyaluronan glycocalyx for essential downstream functions.

Indexed as

GlycoproteinsHyaluronan ReceptorsLeukocytesLymphatic VesselsVesicular Transport ProteinsAnimalsCrystallography, X-RayGlycocalyxHumansHyaluronic AcidMembrane Transport ProteinsMiceModels, MolecularProtein BindingGlycoproteinsHyaluronan ReceptorsHyaluronic AcidLYVE1 protein, humanLYVE1 protein, mouseMembrane Transport ProteinsVesicular Transport Proteins

Identifiers

PMID40113779
PMCPMC11926218

What OpenQuestion holds

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LicenceCC BY
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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.