8xpy

Structure of Nipah virus Malaysia string G protein ectodomain monomer bound to single-domain antibody n425 at 3.63 Angstroms overall resolution

spinqualitylabelsall models 8xpy, resolution 3.63Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8xpy is a 2 chain structure with sequence from Henipavirus nipahense and Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.63Å Ligands: BMA, MAN, NAG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function GLYCP_NIPAV Interacts with host ephrinB2/EFNB2 or ephrin B3/EFNB3 to provide virion attachment to target cell. This attachment induces virion internalization predominantly through clathrin-mediated endocytosis. Publication Abstract from PubMed Nipah virus infection, one of the top priority diseases recognized by the World Health Organization, underscores the urgent need to develop effective countermeasures against potential epidemics and pandemics. Here, we identify a fully human single-domain antibody that targets a highly conserved cryptic epitope situated at the dimeric interface of the Nipah virus G protein (receptor binding protein, RBP), as elucidated through structures by high-resolution cryo-electron microscopy (cryo-EM). This unique binding mode disrupts the tetramerization of the G protein, consequently obstructing the activation of the F protein and inhibiting viral membrane fusion. Furthermore, our investigations reveal that this compact antibody displays enhanced permeability across the blood-brain barrier (BBB) and demonstrates superior efficacy in eliminating pseudovirus within the brain in a murine model of Nipah virus infection, particularly compared to the well-characterized antibody m102.4 in an IgG1 format. Consequently, this single-domain antibody holds promise as a therapeutic candidate to prevent Nipah virus infections and has potential implications for vaccine development. Fully human single-domain antibody targeting a highly conserved cryptic epitope on the Nipah virus G protein.,Wang Y, Sun Y, Shen Z, Wang C, Qian J, Mao Q, Wang Y, Song W, Kong Y, Zhan C, Chen Z, Dimitrov DS, Yang Z, Jiang S, Wu F, Lu L, Ying T, Sun L, Wu Y Nat Commun. 2024 Aug 12;15(1):6892. doi: 10.1038/s41467-024-51066-6. PMID:39134522 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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