5n11 | pdb_00005n11

Crystal structure of Human beta1-coronavirus OC43 NL/A/2005 Hemagglutinin-Esterase

spinqualitylabelsall models 5n11, resolution 2.45Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5n11 is a 2 chain structure with sequence from Cvhoc. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ACY, BMA, NAG, MAN Gene: HE (CVHOC) Activity: Sialate O-acetylesterase, with EC number 3.1.1.53 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [Q4VID6_CVHOC] May serve as a secondary viral attachment protein for initiating infection, the spike protein being the major one. Structural protein that makes short spikes at the surface of the virus. Contains receptor binding and receptor-destroying activities. Seems to be a 'luxury' protein that is not absolutely necessary for virus infection in culture.[RuleBase:RU361278] Publication Abstract from PubMed Human beta1-coronavirus (beta1CoV) OC43 emerged relatively recently through a single zoonotic introduction. Like related animal beta1CoVs, OC43 uses 9-O-acetylated sialic acid as receptor determinant. beta1CoV receptor binding is typically controlled by attachment/fusion spike protein S and receptor-binding/receptor-destroying hemagglutinin-esterase protein HE. We show that following OC43's introduction into humans, HE-mediated receptor binding was selected against and ultimately lost through progressive accumulation of mutations in the HE lectin domain. Consequently, virion-associated receptor-destroying activity toward multivalent glycoconjugates was reduced and altered such that some clustered receptor populations are no longer cleaved. Loss of HE lectin function was also observed for another respiratory human coronavirus, HKU1. This thus appears to be an adaptation to the sialoglycome of the human respiratory tract and for replication in human airways. The findings suggest that the dynamics of virion-glycan interactions contribute to host tropism. Our observations are relevant also to other human respiratory viruses of zoonotic origin, particularly influenza A virus. Betacoronavirus Adaptation to Humans Involved Progressive Loss of Hemagglutinin-Esterase Lectin Activity.,Bakkers MJ, Lang Y, Feitsma LJ, Hulswit RJ, de Poot SA, van Vliet AL, Margine I, de Groot-Mijnes JD, van Kuppeveld FJ, Langereis MA, Huizinga EG, de Groot RJ Cell Host Microbe. 2017 Mar 8;21(3):356-366. doi: 10.1016/j.chom.2017.02.008. PMID:28279346 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Hemagglutinin-esterase 3D structures

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