Structure and design of Langya virus glycoprotein antigens
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.
| Errataetall: | |
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| Medienart: |
E-Artikel |
| Erscheinungsjahr: |
2024 |
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| Erschienen: |
2024 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:121 |
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| Enthalten in: |
Proceedings of the National Academy of Sciences of the United States of America - 121(2024), 16 vom: 16. Apr., Seite e2314990121 |
| Sprache: |
Englisch |
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| Beteiligte Personen: |
Wang, Zhaoqian [VerfasserIn] |
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| Links: |
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| Themen: |
Antibodies |
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| Anmerkungen: |
Date Completed 11.04.2024 Date Revised 29.04.2024 published: Print-Electronic UpdateOf: bioRxiv. 2023 Aug 26;:. - PMID 37645760 Citation Status MEDLINE |
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| doi: |
10.1073/pnas.2314990121 |
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| funding: |
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| Förderinstitution / Projekttitel: |
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| PPN (Katalog-ID): |
NLM37082413X |
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| 500 | |a UpdateOf: bioRxiv. 2023 Aug 26;:. - PMID 37645760 | ||
| 500 | |a Citation Status MEDLINE | ||
| 520 | |a 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 | ||
| 650 | 4 | |a Journal Article | |
| 650 | 4 | |a CryoEM | |
| 650 | 4 | |a Henipavirus | |
| 650 | 4 | |a Langya virus | |
| 650 | 4 | |a antibodies | |
| 650 | 4 | |a vaccine design | |
| 650 | 7 | |a Glycoproteins |2 NLM | |
| 700 | 1 | |a McCallum, Matthew |e verfasserin |4 aut | |
| 700 | 1 | |a Yan, Lianying |e verfasserin |4 aut | |
| 700 | 1 | |a Gibson, Cecily A |e verfasserin |4 aut | |
| 700 | 1 | |a Sharkey, William |e verfasserin |4 aut | |
| 700 | 1 | |a Park, Young-Jun |e verfasserin |4 aut | |
| 700 | 1 | |a Dang, Ha V |e verfasserin |4 aut | |
| 700 | 1 | |a Amaya, Moushimi |e verfasserin |4 aut | |
| 700 | 1 | |a Person, Ashley |e verfasserin |4 aut | |
| 700 | 1 | |a Broder, Christopher C |e verfasserin |4 aut | |
| 700 | 1 | |a Veesler, David |e verfasserin |4 aut | |
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