{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Gondelaud F"],"funding":["Agence Nationale de la Recherche","Fondation pour la Recherche Médicale"],"pagination":["e70085"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11917119"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["34(4)"],"pubmed_abstract":["The Hendra (HeV) and Nipah (NiV) viruses are high-priority, biosafety level-4 pathogens that cause fatal neurological and respiratory disease. Their P gene encodes not only the P protein, an essential polymerase cofactor, but also the virulence factors V and W. We previously showed that the W protein of HeV (W<sup>HeV</sup>) forms amyloid-like fibrils and that one of its subdomains, PNT3, fibrillates in isolation. However, the fibrillation kinetics is much faster in the case of the full-length W<sup>HeV</sup> compared to PNT3, suggesting that another W<sup>HeV</sup> region contributes to the fibrillation process. In this work, we identified the region spanning residues 2-110 (PNT1) as the crucial region implicated in W<sup>HeV</sup> fibrillation. Through site-directed mutagenesis, combined"],"journal":["Protein science : a publication of the Protein Society"],"pubmed_title":["A conserved motif in Henipavirus P/V/W proteins drives the fibrillation of the W protein from Hendra virus."],"pmcid":["PMC11917119"],"funding_grant_id":["ANR‐21‐CE11‐ 0012‐01","MND202310017898","ANR‐10‐INSB‐ 0005","ANR-10-INSB- 0005","ANR-21-CE11- 0012-01"],"pubmed_authors":["Gondelaud F","Bignon C","Carriere F","Ptchelkine D","Longhi S"],"additional_accession":[]},"is_claimable":false,"name":"A conserved motif in Henipavirus P/V/W proteins drives the fibrillation of the W protein from Hendra virus.","description":"The Hendra (HeV) and Nipah (NiV) viruses are high-priority, biosafety level-4 pathogens that cause fatal neurological and respiratory disease. Their P gene encodes not only the P protein, an essential polymerase cofactor, but also the virulence factors V and W. We previously showed that the W protein of HeV (W<sup>HeV</sup>) forms amyloid-like fibrils and that one of its subdomains, PNT3, fibrillates in isolation. However, the fibrillation kinetics is much faster in the case of the full-length W<sup>HeV</sup> compared to PNT3, suggesting that another W<sup>HeV</sup> region contributes to the fibrillation process. In this work, we identified the region spanning residues 2-110 (PNT1) as the crucial region implicated in W<sup>HeV</sup> fibrillation. Through site-directed mutagenesis, combined","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Apr","modification":"2026-06-02T07:19:29.531Z","creation":"2025-04-21T16:53:32.688Z"},"accession":"S-EPMC11917119","cross_references":{"pubmed":["40100133"],"doi":["10.1002/pro.70085"]}}