Evidence map›Paper›PMID 32457151›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2020

Membrane-tethered mucin-like polypeptides sterically inhibit binding and slow fusion kinetics of influenza A virus.

Corleone S Delaveris, Elizabeth R Webster, Steven M Banik, Steven G Boxer, Carolyn R Bertozzi

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
5.2field-weighted citation impact, top 3% of its field
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

43 citing papers in PubMed, 89 citations in OpenAlex.

  1. Mucins and Respiratory Virus Infection.Annual review of virology · 2026
    Review
  2. Article
  3. Article
  4. Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Mirror Image Mucins and Thio Mucins with Tunable Biodegradation.Journal of the American Chemical Society · 2023
    Article
  15. Engineered molecular sensors for quantifying cell surface crowding.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  16. Article
  17. Recombinant mucin biotechnology and engineering.Advanced drug delivery reviews · 2023
    Review
  18. Article
  19. Review
  20. 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

5 authors at 2 institutions in 1 country.

Corleone S DelaverisDepartment of Chemistry, Stanford University, Stanford, CA 94305.ORCID 0000-0002-7291-2338
Elizabeth R WebsterDepartment of Chemistry, Stanford University, Stanford, CA 94305.ORCID 0000-0003-2764-1118
Steven M BanikDepartment of Chemistry, Stanford University, Stanford, CA 94305.
Steven G BoxerDepartment of Chemistry, Stanford University, Stanford, CA 94305; sboxer@stanford.edu bertozzi@stanford.edu.ORCID 0000-0001-9167-4286
Carolyn R BertozziDepartment of Chemistry, Stanford University, Stanford, CA 94305; sboxer@stanford.edu bertozzi@stanford.edu.ORCID 0000-0003-4482-2754
Stanford University · USHoward Hughes Medical Institute · US

Funding

Biophysical Studies of Macromolecules and Molecular AssembliesR35GM118044 · NIGMS · STANFORD UNIVERSITY · PI STEVEN G. BOXER · 2016 to 2026
$7.2M
Targeting the Cancer GlycocalyxR01CA227942 · NCI · STANFORD UNIVERSITY · PI Carolyn Bertozzi · 2019 to 2026
$3.6M
NCI NIH HHS R01 CA227942NIGMS NIH HHS R35 GM118044
6 · The paper itself

Abstract

The mechanism(s) by which cell-tethered mucins modulate infection by influenza A viruses (IAVs) remain an open question. Mucins form both a protective barrier that can block virus binding and recruit IAVs to bind cells via the sialic acids of cell-tethered mucins. To elucidate the molecular role of mucins in flu pathogenesis, we constructed a synthetic glycocalyx to investigate membrane-tethered mucins in the context of IAV binding and fusion. We designed and synthesized lipid-tethered glycopolypeptide mimics of mucins and added them to lipid bilayers, allowing chemical control of length, glycosylation, and surface density of a model glycocalyx. We observed that the mucin mimics undergo a conformational change at high surface densities from a compact to an extended architecture. At high surface densities, asialo mucin mimics inhibited IAV binding to underlying glycolipid receptors, and this density correlated to the mucin mimic's conformational transition. Using a single virus fusion assay, we observed that while fusion of virions bound to vesicles coated with sialylated mucin mimics was possible, the kinetics of fusion was slowed in a mucin density-dependent manner. These data provide a molecular model for a protective mechanism by mucins in IAV infection, and therefore this synthetic glycocalyx provides a useful reductionist model for studying the complex interface of host-pathogen interactions.

Indexed as

Virus InternalizationGlycocalyxInfluenza A virusLipid BilayersMucinsN-Acetylneuraminic AcidPeptidesProtein ConformationLipid BilayersMucinsN-Acetylneuraminic AcidPeptidesglycobiologyinfluenza A virusmucin

Identifiers

PMID32457151
PMCPMC7293601
OpenAlexW3030447488

What OpenQuestion holds

Textmetadata
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.