5n11: Difference between revisions
New page: '''Unreleased structure''' The entry 5n11 is ON HOLD Authors: Bakkers, M.J.G., Feitsma, L.J., de Groot, R.J., Huizinga, E.G. Description: Crystal structure of Human beta1-coronavirus O... |
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==Crystal structure of Human beta1-coronavirus OC43 NL/A/2005 Hemagglutinin-Esterase== | |||
<StructureSection load='5n11' size='340' side='right'caption='[[5n11]], [[Resolution|resolution]] 2.45Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5n11]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_coronavirus_OC43 Human coronavirus OC43]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5N11 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5N11 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.45Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5n11 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5n11 OCA], [https://pdbe.org/5n11 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5n11 RCSB], [https://www.ebi.ac.uk/pdbsum/5n11 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5n11 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q4VID6_CVHOC 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] | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:28279346</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Bakkers | <div class="pdbe-citations 5n11" style="background-color:#fffaf0;"></div> | ||
[[Category: Feitsma | |||
[[Category: Huizinga | ==See Also== | ||
[[Category: De Groot | *[[Hemagglutinin-esterase 3D structures|Hemagglutinin-esterase 3D structures]] | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Human coronavirus OC43]] | |||
[[Category: Large Structures]] | |||
[[Category: Bakkers MJG]] | |||
[[Category: Feitsma LJ]] | |||
[[Category: Huizinga EG]] | |||
[[Category: De Groot RJ]] | |||
Latest revision as of 20:56, 8 November 2023
Structural highlights
FunctionQ4VID6_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 PubMedHuman 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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