Evidence map›Paper›PMID 37645760›Full record

ArticlebioRxiv : the preprint server for biology2023

Structure and design of Langya virus glycoprotein antigens.

Zhaoqian Wang, Matthew McCallum, Lianying Yan, William Sharkey, Young-Jun Park, Ha V Dang, Moushimi Amaya, Ashley Person, Christopher C Broder, David Veesler

Open access · greenAbstract readPreprint
PubMed Full text at PMC Publisher
In one paragraph

Article in bioRxiv : the preprint server for biology, 2023. 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, 4 citations in OpenAlex.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

10 authors at 3 institutions in 1 country.

Zhaoqian WangDepartment of Biochemistry, University of Washington, Seattle, Washington, USA.
Matthew McCallumDepartment of Biochemistry, University of Washington, Seattle, Washington, USA.
Lianying YanDepartment of Microbiology and Immunology, Uniformed Services University, Bethesda, Maryland, USA.
William SharkeyDepartment of Biochemistry, University of Washington, Seattle, Washington, USA.
Young-Jun ParkDepartment of Biochemistry, University of Washington, Seattle, Washington, USA.
Ha V DangDepartment of Biochemistry, University of Washington, Seattle, Washington, USA.
Moushimi AmayaDepartment of Microbiology and Immunology, Uniformed Services University, Bethesda, Maryland, USA.
Ashley PersonDepartment of Biochemistry, University of Washington, Seattle, Washington, USA.
Christopher C BroderDepartment of Microbiology and Immunology, Uniformed Services University, Bethesda, Maryland, USA.
David VeeslerDepartment of Biochemistry, University of Washington, Seattle, Washington, USA.
University of Washington · USUniformed Services University of the Health Sciences · USHoward Hughes Medical Institute · US

Funding

Project 3 - USUHSU19AI142764 · NIAID · HENRY M. JACKSON FDN FOR THE ADV MIL/MED · PI ELDRIDGE, JOHN HAYWARD · 2019 to 2023
$24.6M
Centers for Research on Structural Biology of Infectious Diseases: Universal Influenza Vaccine Research75N93022C00036 · NIAID · SEATTLE CHILDREN'S HOSPITAL · PI STAKER, BART · 2022 to 2025
$21.7M
Unraveling the bat humoral immune response against zoonotic viruses to guide the design of next-generation therapeuticsDP1AI158186 · NIAID · UNIVERSITY OF WASHINGTON · PI VEESLER, DAVID · 2020 to 2024
$5.4M
NIAID NIH HHS 75N93022C00036NIAID NIH HHS DP1 AI158186NIAID NIH HHS U19 AI142764
6 · The paper itself

Abstract

Langya virus (LayV) is a recently discovered henipavirus (HNV), isolated from febrile patients in China. HNV entry into host cells is mediated by the attachment (G) and fusion (F) glycoproteins which are the main targets of neutralizing antibodies. We show here that the LayV F and G glycoproteins promote membrane fusion with human, mouse and hamster target cells using a different, yet unknown, receptor than NiV and HeV and that NiV- and HeV-elicited monoclonal and polyclonal antibodies do not cross-react with LayV F and G. We determined cryo-electron microscopy structures of LayV F, in the prefusion and postfusion states, and of LayV G, revealing previously unknown conformational landscapes and their distinct antigenicity relative to NiV and HeV. We computationally designed stabilized LayV G constructs and demonstrate the generalizability of an HNV F prefusion-stabilization strategy. Our data will support the development of vaccines and therapeutics against LayV and closely related HNVs.

Identifiers

PMID37645760
PMCPMC10462157
OpenAlexW4386029659

What OpenQuestion holds

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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.