{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["14(1)"],"submitter":["Isaacs A"],"pubmed_abstract":["In August 2022, a novel henipavirus (HNV) named Langya virus (LayV) was isolated from patients with severe pneumonic disease in China. This virus is closely related to Mòjiāng virus (MojV), and both are divergent from the bat-borne HNV members, Nipah (NiV) and Hendra (HeV) viruses. The spillover of LayV is the first instance of a HNV zoonosis to humans outside of NiV and HeV, highlighting the continuing threat this genus poses to human health. In this work, we determine the prefusion structures of MojV and LayV F proteins via cryogenic electron microscopy to 2.66 and 3.37 Å, respectively. We show that despite sequence divergence from NiV, the F proteins adopt an overall similar structure but are antigenically distinct as they do not react to known antibodies or sera. Glycoproteomic analysi"],"journal":["Nature communications"],"pagination":["3577"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10275869"],"repository":["biostudies-literature"],"pubmed_title":["Structure and antigenicity of divergent Henipavirus fusion glycoproteins."],"pmcid":["PMC10275869"],"pubmed_authors":["Schulz BL","Watterson D","Seitanidou J","Low YS","Macauslane KL","Modhiran N","Scott CAP","Liang B","Chappell KJ","Pegg CL","Isaacs A","Landsberg MJ","Cheung STM"],"additional_accession":[]},"is_claimable":false,"name":"Structure and antigenicity of divergent Henipavirus fusion glycoproteins.","description":"In August 2022, a novel henipavirus (HNV) named Langya virus (LayV) was isolated from patients with severe pneumonic disease in China. This virus is closely related to Mòjiāng virus (MojV), and both are divergent from the bat-borne HNV members, Nipah (NiV) and Hendra (HeV) viruses. The spillover of LayV is the first instance of a HNV zoonosis to humans outside of NiV and HeV, highlighting the continuing threat this genus poses to human health. In this work, we determine the prefusion structures of MojV and LayV F proteins via cryogenic electron microscopy to 2.66 and 3.37 Å, respectively. We show that despite sequence divergence from NiV, the F proteins adopt an overall similar structure but are antigenically distinct as they do not react to known antibodies or sera. Glycoproteomic analysi","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 Jun","modification":"2026-05-28T18:44:00.711Z","creation":"2025-04-03T22:51:08.637Z"},"accession":"S-EPMC10275869","cross_references":{"pubmed":["37328468"],"doi":["10.1038/s41467-023-39278-8"]}}