Evidence map›Paper›PMID 36763666›Full record

ArticleScience advances2023

Subnanometer structure of an enveloped virus fusion complex on viral surface reveals new entry mechanisms.

Tara C Marcink, Gillian Zipursky, Wenjing Cheng, Kyle Stearns, Shari Stenglein, Kate Golub, Frances Cohen, Francesca Bovier, Daniel Pfalmer, Alexander L Greninger and 3 more

Open access · goldAbstract read
In one paragraph

Article in Science advances, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed, 1 pooled it
8.4field-weighted citation impact, top 2% 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

27 citing papers in PubMed, 1 synthesis or guideline pooled it, 34 citations in OpenAlex.

  1. Pooled it
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  9. Functional and antigenic constraints on the Nipah virus fusion protein.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  10. Functional and antigenic constraints on the Nipah virus fusion protein.bioRxiv : the preprint server for biology · 2026
    Article
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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

13 authors at 4 institutions in 2 countries.

Tara C MarcinkDepartment of Pediatrics, Columbia University Vagelos College of Physicians and Surgeons, New York, NY, USA.ORCID 0000-0003-4295-1229
Gillian ZipurskyDepartment of Pediatrics, Columbia University Vagelos College of Physicians and Surgeons, New York, NY, USA.ORCID 0000-0003-4408-5168
Wenjing ChengDepartment of Pediatrics, Columbia University Vagelos College of Physicians and Surgeons, New York, NY, USA.ORCID 0000-0002-9241-3835
Kyle StearnsDepartment of Pediatrics, Columbia University Vagelos College of Physicians and Surgeons, New York, NY, USA.ORCID 0000-0002-5166-7927
Shari StengleinDepartment of Pediatrics, Columbia University Vagelos College of Physicians and Surgeons, New York, NY, USA.ORCID 0000-0001-8894-509X
Kate GolubDepartment of Pediatrics, Columbia University Vagelos College of Physicians and Surgeons, New York, NY, USA.ORCID 0000-0003-3350-9762
Frances CohenDepartment of Pediatrics, Columbia University Vagelos College of Physicians and Surgeons, New York, NY, USA.
Francesca BovierDepartment of Pediatrics, Columbia University Vagelos College of Physicians and Surgeons, New York, NY, USA.ORCID 0000-0003-3446-9619
Daniel PfalmerDepartment of Laboratory Medicine and Pathology, University of Washington, Seattle, WA, USA.ORCID 0000-0001-5896-5866
Alexander L GreningerDepartment of Laboratory Medicine and Pathology, University of Washington, Seattle, WA, USA.ORCID 0000-0002-7443-0527
Matteo PorottoDepartment of Pediatrics, Columbia University Vagelos College of Physicians and Surgeons, New York, NY, USA.ORCID 0000-0003-3866-9220
Amedee des GeorgesStructural Biology Initiative, CUNY Advanced Science Research Center, City University of New York, New York, NY, USA.ORCID 0000-0002-9704-3781
Anne MosconaDepartment of Pediatrics, Columbia University Vagelos College of Physicians and Surgeons, New York, NY, USA.ORCID 0000-0002-1796-8320
Columbia University · USUniversity of Washington · USThe Graduate Center, CUNY · USUniversity of Campania "Luigi Vanvitelli" · IT

Funding

Hormones: Molecular Mechanism of Action and FunctionsT32DK007328 · NIDDK · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI KOUSTENI, STAVROULA · 1986 to 2025
$7.8M
Engineering protease-resistant alpha-beta peptides for broad-spectrum antiviralsR01AI114736 · NIAID · WEILL MEDICAL COLL OF CORNELL UNIV · PI MOSCONA, ANNE · 2015 to 2019
$3.7M
Engineering protease-resistant antiviral peptide inhibitors for SARS-CoV-2R01AI160961 · NIAID · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI MOSCONA, ANNE · 2021 to 2025
$3.6M
Fusion inhibitors that block host-to-host transmission of SARS-CoV-2R01AI160953 · NIAID · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI POROTTO, MATTEO · 2021 to 2025
$3.6M
Understanding membrane proteins’ allosteric modulation with cryo-EMR35GM133598 · NIGMS · NEW YORK UNIVERSITY · PI Amedee des Georges · 2019 to 2026
$3.4M
Development of novel endosome-targeted Ebola virus entry inhibitors as antiviral agentsR01AI121349 · NIAID · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI POROTTO, MATTEO · 2016 to 2020
$3.2M
Human parainfluenza virus fusion complexglycoproteins imaged in actionF32AI152275 · NIAID · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI MARCINK, TARA · 2021 to 2023
$177k
NIAID NIH HHS F32 AI152275NIAID NIH HHS R01 AI114736NIAID NIH HHS R01 AI121349NIAID NIH HHS R01 AI160953NIAID NIH HHS R01 AI160961NIDDK NIH HHS T32 DK007328NIGMS NIH HHS R35 GM133598
6 · The paper itself

Abstract

Paramyxoviruses-including important pathogens like parainfluenza, measles, and Nipah viruses-use a receptor binding protein [hemagglutinin-neuraminidase (HN) for parainfluenza] and a fusion protein (F), acting in a complex, to enter cells. We use cryo-electron tomography to visualize the fusion complex of human parainfluenza virus 3 (HN/F) on the surface of authentic clinical viruses at a subnanometer resolution sufficient to answer mechanistic questions. An HN loop inserts in a pocket on F, showing how the fusion complex remains in a ready but quiescent state until activation. The globular HN heads are rotated with respect to each other: one downward to contact F, and the other upward to grapple cellular receptors, demonstrating how HN/F performs distinct steps before F activation. This depiction of viral fusion illuminates potentially druggable targets for paramyxoviruses and sheds light on fusion processes that underpin wide-ranging biological processes but have not been visualized in situ or at the present resolution.

Indexed as

Paramyxoviridae InfectionsViral Fusion ProteinsHN ProteinHumansReceptors, Cell SurfaceVirus InternalizationHN ProteinReceptors, Cell SurfaceViral Fusion Proteins

Identifiers

PMID36763666
PMCPMC9917000
OpenAlexW4320032928

What OpenQuestion holds

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LicenceCC BY-NC
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.