6y6p

Structure of Hantaan virus envelope glycoprotein Gn

spinqualitylabelsall models 6y6p, resolution 1.94Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6y6p is a 1 chain structure with sequence from Hantaan orthohantavirus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.938Å Ligands: NAG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function GP_HANTV Glycoprotein N and Glycoprotein C interact with each. other and are present at the surface of the virion. They are able to attach the virion to host cell receptors. This attachment induces virion internalization predominantly through clathrin-dependent endocytosis. Also promote fusion of viral membrane with host endosomal membrane after endocytosis of the virion. Glycoprotein N contains an ITAM motif which is likely to dysregulate normal immune and endothelial cell responses and contribute to virus pathogenesis (By similarity). Publication Abstract from PubMed Hantaviruses are rodent-borne viruses causing serious zoonotic outbreaks worldwide for which no treatment is available. Hantavirus particles are pleomorphic and display a characteristic square surface lattice. The envelope glycoproteins Gn and Gc form heterodimers that further assemble into tetrameric spikes, the lattice building blocks. The glycoproteins, which are the sole targets of neutralizing antibodies, drive virus entry via receptor-mediated endocytosis and endosomal membrane fusion. Here we describe the high-resolution X-ray structures of the heterodimer of Gc and the Gn head and of the homotetrameric Gn base. Docking them into an 11.4-A-resolution cryoelectron tomography map of the hantavirus surface accounted for the complete extramembrane portion of the viral glycoprotein shell and allowed a detailed description of the surface organization of these pleomorphic virions. Our results, which further revealed a built-in mechanism controlling Gc membrane insertion for fusion, pave the way for immunogen design to protect against pathogenic hantaviruses. The Hantavirus Surface Glycoprotein Lattice and Its Fusion Control Mechanism.,Serris A, Stass R, Bignon EA, Muena NA, Manuguerra JC, Jangra RK, Li S, Chandran K, Tischler ND, Huiskonen JT, Rey FA, Guardado-Calvo P Cell. 2020 Sep 9. pii: S0092-8674(20)31064-3. doi: 10.1016/j.cell.2020.08.023. PMID:32937107 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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