ArticleNature communications2024
The cryo-EM structure of homotetrameric attachment glycoprotein from langya henipavirus.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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Who cites it
11 citing papers in PubMed, 13 citations in OpenAlex.
- Review
- Cryo-electron tomography of Nipah virus structural protein complexes in virus-like particles.bioRxiv : the preprint server for biology · 2026Article
- Mechanistic and antigenic boundaries of Henipavirus and Parahenipavirus glycoproteins.Nature communications · 2026Article
- Open and closed forms of assembled henipavirus nucleoprotein suggest structural basis of genome access.Science advances · 2026Article
- A risk-gate mechanistic-ecological framework for assessing emergence potential of henipa-related viruses.Frontiers in microbiology · 2026Article
- Antigenic and structural insights into Langya henipavirus attachment glycoprotein.Virologica Sinica · 2025Article
- Unveiling emerging threats: Langya and Mojiang-A dance with unfamiliar foes.Infectious diseases & immunity · 2025Review
- Detection and characterization of Langya virus inOne health (Amsterdam, Netherlands) · 2025Article
- Henipaviruses: epidemiology, ecology, disease, and the development of vaccines and therapeutics.Clinical microbiology reviews · 2025Review
- A Comparative Assessment of the Pathogenic Potential of Newly Discovered Henipaviruses.Pathogens (Basel, Switzerland) · 2024Review
- Cryo-electron microscopy in the study of virus entry and infection.Frontiers in molecular biosciences · 2024Review
Corrections and comments
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Langya Henipavirus (LayV) infection is an emerging zoonotic disease that has been causing respiratory symptoms in China since 2019. For virus entry, LayV's genome encodes the fusion protein F and the attachment glycoprotein G. However, the structural and functional information regarding LayV-G remains unclear. In this study, we revealed that LayV-G cannot bind to the receptors found in other HNVs, such as ephrin B2/B3, and it shows different antigenicity from HeV-G and NiV-G. Furthermore, we determined the near full-length structure of LayV-G, which displays a distinct mushroom-shaped configuration, distinguishing it from other attachment glycoproteins of HNV. The stalk and transmembrane regions resemble the stem and root of mushroom and four downward-tilted head domains as mushroom cap potentially interact with the F protein and influence membrane fusion process. Our findings enhance the understanding of emerging HNVs that cause human diseases through zoonotic transmission and provide implication for LayV related vaccine development.
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Registered trials
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.