8x50

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Current revision (08:26, 14 August 2024) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 8x50 is ON HOLD until Paper Publication
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==BA.2.86 Spike Trimer with ins483V mutation (1 RBD up)==
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<StructureSection load='8x50' size='340' side='right'caption='[[8x50]], [[Resolution|resolution]] 3.82&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[8x50]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Severe_acute_respiratory_syndrome_coronavirus_2 Severe acute respiratory syndrome coronavirus 2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8X50 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8X50 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.82&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8x50 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8x50 OCA], [https://pdbe.org/8x50 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8x50 RCSB], [https://www.ebi.ac.uk/pdbsum/8x50 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8x50 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/SPIKE_SARS2 SPIKE_SARS2] attaches the virion to the cell membrane by interacting with host receptor, initiating the infection (By similarity). Binding to human ACE2 receptor and internalization of the virus into the endosomes of the host cell induces conformational changes in the Spike glycoprotein (PubMed:32142651, PubMed:32075877, PubMed:32155444). Uses also human TMPRSS2 for priming in human lung cells which is an essential step for viral entry (PubMed:32142651). Proteolysis by cathepsin CTSL may unmask the fusion peptide of S2 and activate membranes fusion within endosomes.[HAMAP-Rule:MF_04099]<ref>PMID:32075877</ref> <ref>PMID:32142651</ref> <ref>PMID:32155444</ref> mediates fusion of the virion and cellular membranes by acting as a class I viral fusion protein. Under the current model, the protein has at least three conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes.[HAMAP-Rule:MF_04099] Acts as a viral fusion peptide which is unmasked following S2 cleavage occurring upon virus endocytosis.[HAMAP-Rule:MF_04099]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Selective pressures have given rise to a number of SARS-CoV-2 variants during the prolonged course of the COVID-19 pandemic. Recently evolved variants differ from ancestors in additional glycosylation within the spike protein receptor-binding domain (RBD). Details of how the acquisition of glycosylation impacts viral fitness and human adaptation are not clearly understood. Here, we dissected the role of N354-linked glycosylation, acquired by BA.2.86 sub-lineages, as a RBD conformational control element in attenuating viral infectivity. The reduced infectivity is recovered in the presence of heparin sulfate, which targets the 'N354 pocket' to ease restrictions of conformational transition resulting in a 'RBD-up' state, thereby conferring an adjustable infectivity. Furthermore, N354 glycosylation improved spike cleavage and cell-cell fusion, and in particular escaped one subset of ADCC antibodies. Together with reduced immunogenicity in hybrid immunity background, these indicate a single spike amino acid glycosylation event provides selective advantage in humans through multiple mechanisms.
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Authors: Yue, C., Liu, P.
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Spike N354 glycosylation augments SARS-CoV-2 fitness for human adaptation through structural plasticity.,Liu P, Yue C, Meng B, Xiao T, Yang S, Liu S, Jian F, Zhu Q, Yu Y, Ren Y, Wang P, Li Y, Wang J, Mao X, Shao F, Wang Y, Gupta RK, Cao Y, Wang X Natl Sci Rev. 2024 Jun 14;11(7):nwae206. doi: 10.1093/nsr/nwae206. eCollection , 2024 Jul. PMID:39071099<ref>PMID:39071099</ref>
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Description: BA.2.86 Spike Trimer with ins483V mutation (1 RBD up)
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Yue, C]]
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<div class="pdbe-citations 8x50" style="background-color:#fffaf0;"></div>
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[[Category: Liu, P]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Severe acute respiratory syndrome coronavirus 2]]
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[[Category: Liu P]]
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[[Category: Yue C]]

Current revision

BA.2.86 Spike Trimer with ins483V mutation (1 RBD up)

PDB ID 8x50

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OCA

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