Structure and design of Langya virus glycoprotein antigens
Open accessPublished version of a preprint
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 Nipah virus (NiV) and Hendra virus (HeV) and that NiV- and HeV-elicited monoclonal and polyclonal antibodies do not cross-react with LayV F and G. We determined cryoelectron microscopy structures of LayV F, in the prefusion and postfusion states, and of LayV G, revealing their conformational landscape and 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.
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- Authors
- Wang, Z., McCallum, M., Yan, L., Gibson, C. A., Sharkey, W., Park, Y.-J., Dang, H. V., Amaya, M., Person, A., Broder, C. C., & Veesler, D.
- Affiliations
- University of Washington (US)
- Uniformed Services University of the Health Sciences (US)
- Howard Hughes Medical Institute (US)
- Corresponding author
- Wang, Zhaoqian
- McCallum, Matthew
- Yan, Lianying
- Veesler, David
- ORCID
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2024-04-09
- Volume
- 121
- Issue
- 16
- Pages
- e2314990121-e2314990121
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC11032465
- OpenAlex
- W4394597800
- Cited by
- 32
- References
- 8
- Citations by year
- 2026: 10 · 2025: 12 · 2024: 9 · 2023: 1
- FWCI
- 9.40
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion, cc-by)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- PubMed Central (submittedVersion, cc-by)
- Funders
- Howard Hughes Medical Institute (N/A)
- HHS | NIH | National Institute of Allergy and Infectious Diseases (75N93022C00036)
- Topics
- Health Sciences › Medicine › Epidemiology › Virology and Viral Diseases
- Health Sciences › Medicine › Infectious Diseases › SARS-CoV-2 and COVID-19 Research
- Health Sciences › Medicine › Epidemiology › Influenza Virus Research Studies
- Keywords
- henipaviruses, fusion glycoprotein, attachment glycoprotein, membrane fusion, viral receptor, Nipah virus, Hendra virus, cross-reactivity, glycoprotein conformation, antigen design, vaccine development, therapeutics
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