CoChat
Sign Up
PreprintCited by 32Virology and Viral DiseasesSARS-CoV-2 and COVID-19 ResearchInfluenza Virus Research Studies

The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.

Structure and design of Langya virus glycoprotein antigens

Open access
Wang, Zhaoqian, McCallum, Matthew, Yan, Lianying, Sharkey, William, Park, Young-Jun, Dang, Ha V., Amaya, Moushimi, Person, Ashley, Broder, Christopher C., Veesler, David·2023·Proceedings of the National Academy of Sciences
DOI 10.1101/2023.08.20.554025PMC PMC11032465

Preprint — published as 10.1073/pnas.2314990121 · Paper page

Open this paper in CoChat — free accountOpen PDF

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.

Overview

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1101/2023.08.20.554025

Cites

3 of 3 references verified0 citation errors · 0 not checkable

Statistics

Verification

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Citations

Cites

Flagged first, then by citations

Research works printed but not linked: 96

  1. Eaton, B. T. , Broder, C. C. , Middleton, D. & Wang, L. F. Hendra and Nipah viruses: different and dangerous. Nat. Rev. Microbiol. 4, 23–35 (2006). · DOI
  2. 10.1038/ncomms5105 · DOI
  3. 10.3201/eid1301.060791 · DOI
  4. Hernández, L. H. A. et al. First Genomic Evidence of a Henipa-like Virus in Brazil. Viruses 14, (2022). · DOI
  5. 10.1371/journal.ppat.1002836 · DOI
  6. 2022, Discovery and Genomic Characterization of a Novel Henipavirus, Angavokely Virus, from Fruit Bats in Madagascar, J. Virol, 96, e0092122, 10.1128/jvi.00921-22 · DOI · Paper page
  7. 2022, Novel Hendra Virus Variant Detected by Sentinel Surveillance of Horses in Australia, Emerg. Infect. Dis, 28, 693, 10.3201/eid2803.211245 · DOI
  8. Wang, J. et al. A new Hendra virus genotype found in Australian flying foxes. Virol. J. 18, 197 (2021). · DOI
  9. 2020, Vaccines to Emerging Viruses: Nipah and Hendra, Annu Rev Virol, 7, 447, 10.1146/annurev-virology-021920-113833 · DOI
  10. Wang, Z. et al. Architecture and antigenicity of the Nipah virus attachment glycoprotein. Science eab m5561 (2022). · DOI
  11. 10.1128/JVI.79.20.12714-12720.2005 · DOI
  12. 10.1073/pnas.1523303113 · DOI
  13. 10.1371/journal.ppat.1005322 · DOI
  14. 10.1128/JVI.00469-10 · DOI
  15. 10.1038/s41594-021-00584-8 · DOI
  16. 10.1038/s41594-019-0308-9 · DOI
  17. 10.1093/infdis/jiz515 · DOI
  18. Doyle, M. P. et al. Cooperativity mediated by rationally selected combinations of human monoclonal antibodies targeting the henipavirus receptor binding protein. Cell Rep. 36, 109628 (2021). · DOI
  19. 10.1016/j.cell.2020.11.023 · DOI
  20. 10.1128/JVI.00005-14 · DOI
  21. 2014, Therapeutic treatment of Nipah virus infection in nonhuman primates with a neutralizing human monoclonal antibody, Sci. Transl. Med, 6, 242r
  22. 10.1016/j.vaccine.2011.06.015 · DOI
  23. 10.1038/nature03838 · DOI
  24. 10.1073/pnas.1911773116 · DOI
  25. 10.1073/pnas.0504887102 · DOI
  26. Pryce, R. et al. A key region of molecular specificity orchestrates unique ephrin-B1 utilization by Cedar virus. Life Sci Alliance 3, (2020). · DOI
  27. 10.1073/pnas.1501690112 · DOI
  28. Wu, Z. et al. Novel Henipa-like virus, Mojiang Paramyxovirus, in rats, China, 2012. Emerg. Infect. Dis. 20, 1064–1066 (2014). · DOI
  29. Lee, S.-H. et al. Discovery and Genetic Characterization of Novel Paramyxoviruses Related to the Genus Henipavirus in Crocidura Species in the Republic of Korea. Viruses 13, (2021). · DOI
  30. 2022, A Zoonotic Henipavirus in Febrile Patients in China, N. Engl. J. Med, 387, 470, 10.1056/NEJMc2202705 · DOI
  31. Rissanen, I. et al. Idiosyncratic Mòjiāng virus attachment glycoprotein directs a host-cell entry pathway distinct from genetically related henipaviruses. Nat. Commun. 8, 16060 (2017). · DOI
  32. 2023, Structure and antigenicity of divergent Henipavirus fusion glycoproteins, Nat. Commun, 14, 3577, 10.1038/s41467-023-39278-8 · DOI
  33. 2023, Structures of Langya Virus Fusion Protein Ectodomain in Pre-and Postfusion Conformation, J. Virol, 97, e0043323, 10.1128/jvi.00433-23 · DOI
  34. 10.1074/jbc.M504598200 · DOI
  35. Cheliout Da Silva, S. , et al. Functional Analysis of the Fusion and Attachment Glycoproteins of Mojiang Henipavirus. Viruses 13, (2021). · DOI
  36. 10.1128/JVI.01304-12 · DOI
  37. 10.1128/JVI.79.12.7922-7925.2005 · DOI
  38. 10.1073/pnas.1912503116 · DOI
  39. 10.1038/nature16988 · DOI
  40. 10.1073/pnas.1708727114 · DOI
  41. 10.1128/JVI.00555-11 · DOI
  42. 10.1073/pnas.1106536108 · DOI · Paper page
  43. 10.1073/pnas.1213802109 · DOI
  44. 10.1073/pnas.0503989102 · DOI
  45. 10.1128/JVI.01318-12 · DOI
  46. 10.1126/science.1234914 · DOI · Paper page
  47. 10.1038/nature04322 · DOI
  48. 10.1073/pnas.1707304114 · DOI · Paper page
  49. 10.1016/j.cell.2018.12.028 · DOI · Paper page
  50. Loomis, R. J. et al. Structure-Based Design of Nipah Virus Vaccines: A Generalizable Approach to Paramyxovirus Immunogen Development. Front. Immunol. 11, 842 (2020). · DOI
  51. 2022, Potent monoclonal antibody-mediated neutralization of a divergent Hendra virus variant, Proc. Natl. Acad. Sci. U. S. A, 119, e2122769119, 10.1073/pnas.2122769119 · DOI
  52. 10.1128/JVI.02699-09 · DOI
  53. 10.1126/scitranslmed.3002901 · DOI
  54. 10.1086/528801 · DOI
  55. 10.1126/science.add2187 · DOI · Paper page
  56. 10.1128/JVI.00076-12 · DOI
  57. 2023, 3DFlex: determining structure and motion of flexible proteins from cryo-EM, Nat. Methods, 20, 860, 10.1038/s41592-023-01853-8 · DOI
  58. 10.1016/S1473-3099(19)30634-6 · DOI
  59. 2012, A Hendra virus G glycoprotein subunit vaccine protects African green monkeys from Nipah virus challenge, Sci. Transl. Med, 4, 146r
  60. 10.1128/JVI.79.11.6690-6702.2005 · DOI
  61. 10.1128/JVI.01619-06 · DOI
  62. 10.1016/j.vaccine.2008.05.016 · DOI
  63. 10.3201/eid2003.131159 · DOI
  64. 10.1126/science.1243283 · DOI · Paper page
  65. 10.1056/NEJMoa2213836 · DOI
  66. 2023, Bivalent Prefusion F Vaccine in Pregnancy to Prevent RSV Illness in Infants, N. Engl. J. Med, 388, 1451, 10.1056/NEJMoa2216480 · DOI
  67. 2020, SARS-CoV-2 mRNA vaccine design enabled by prototype pathogen preparedness, Nature, 586, 567, 10.1038/s41586-020-2622-0 · DOI · Paper page
  68. 10.1016/j.cell.2020.10.043 · DOI · Paper page
  69. 10.1371/journal.ppat.1000642 · DOI
  70. Di Rubbo, A. et al. Optimization and diagnostic evaluation of monoclonal antibody-based blocking ELISA formats for detection of neutralizing antibodies to Hendra virus in mammalian sera. J. Virol. Methods 274, 113731 (2019). · DOI
  71. 10.1016/j.jsb.2005.03.010 · DOI
  72. 10.1038/nmeth.4169 · DOI · Paper page
  73. 10.1007/978-1-59745-554-1_2 · DOI
  74. 10.1128/JVI.02253-15 · DOI
  75. 10.1126/science.1259530 · DOI
  76. 10.1017/S1431927603445911 · DOI
  77. 10.1017/S1431927618004816 · DOI
  78. 10.1038/s41592-020-00990-8 · DOI
  79. 2019, Real-time cryo-electron microscopy data preprocessing with Warp, Nat. Methods, 16, 1146, 10.1038/s41592-019-0580-y · DOI
  80. 10.1107/S205225251801463X · DOI
  81. Zivanov, J. et al. New tools for automated high-resolution cryo-EM structure determination in RELION-3. Elife 7, (2018). · DOI
  82. 10.1016/j.jmb.2003.07.013 · DOI · Paper page
  83. 10.1016/j.ultramic.2013.06.004 · DOI
  84. 10.1101/2023.05.16.541002 · DOI · Paper page
  85. 10.1002/pro.3235 · DOI · Paper page
  86. Emsley, P. , Lohkamp, B. , Scott, W. G. & Cowtan, K. Features and development of Coot. Acta Crystallogr. D Biol. Crystallogr. 66, 486–501 (2010). · DOI · Paper page
  87. 2020, Current developments in Coot for macromolecular model building of Electron Cryo-microscopy and Crystallographic Data, Protein Sci, 29, 1069
  88. 10.1038/nmeth.3286 · DOI
  89. 10.1016/j.str.2018.09.006 · DOI
  90. Wang, R. Y. et al. Automated structure refinement of macromolecular assemblies from cryo-EM maps using Rosetta. Elife 5, (2016). · DOI · Paper page
  91. 2019, Macromolecular structure determination using X-rays, neutrons and electrons: recent developments in Phenix, Acta Crystallogr D Struct Biol, 75, 861, 10.1107/S2059798319011471 · DOI · Paper page
  92. 2018, ISOLDE: a physically realistic environment for model building into low-resolution electron-density maps, Acta Crystallogr D Struct Biol, 74, 519, 10.1107/S2059798318002425 · DOI
  93. 10.1107/S0907444909042073 · DOI · Paper page
  94. 10.1038/nmeth.3541 · DOI · Paper page
  95. 10.1038/nsmb.3115 · DOI
  96. 10.1002/jcc.20084 · DOI

Metadata

Authors
Wang, Z., McCallum, M., Yan, L., 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
openRxiv
Published
2023-08-20
Volume
121
Issue
16
Pages
e2314990121-e2314990121
ISSN
0027-8424 (ISSN-L)
DOI
10.1101/2023.08.20.554025
PMC
PMC11032465
OpenAlex
W4394597800
Cited by
32
References
3
Citations by year
2026: 10 · 2025: 12 · 2024: 9 · 2023: 1
FWCI
9.46
Type
journal article
Language
en
Open access
Licence
cc-by
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
  • Burroughs Wellcome Fund
  • University of Washington
  • National Institutes of Health (S10 OD032290, 75N93022C00036)
  • National Institute of Allergy and Infectious Diseases (U19AI142764, DP1AI158186, 75N93022C00036, DP1AI158186 and 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

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review