8eqf: Difference between revisions

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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=8eqf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8eqf OCA], [https://pdbe.org/8eqf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8eqf RCSB], [https://www.ebi.ac.uk/pdbsum/8eqf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8eqf ProSAT]</span></td></tr>
 </table>
-== Function ==
+<div style="background-color:#fffaf0;">
-[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]
+== Publication Abstract from PubMed ==
+The COVID-19 pandemic remains a significant public health concern for the global population; the development and characterization of therapeutics, especially ones that are broadly effective, will continue to be essential as severe acute respiratory syndrome-coronavirus-2 (SARS-CoV-2) variants emerge. Neutralizing monoclonal antibodies remain an effective therapeutic strategy to prevent virus infection and spread so long as they recognize and interact with circulating variants. The epitope and binding specificity of a neutralizing anti-SARS-CoV-2 Spike receptor-binding domain antibody clone against many SARS-CoV-2 variants of concern were characterized by generating antibody-resistant virions coupled with cryo-EM structural analysis and VSV-spike neutralization studies. This workflow can serve to predict the efficacy of antibody therapeutics against emerging variants and inform the design of therapeutics and vaccines.
+An in vitro experimental pipeline to characterize the epitope of a SARS-CoV-2 neutralizing antibody.,Atanasoff KE, Brambilla L, Adelsberg DC, Kowdle S, Stevens CS, Slamanig S, Hung C-T, Fu Y, Lim R, Tran L, Allen R, Sun W, Duty JA, Bajic G, Lee B, Tortorella D mBio. 2024 Jan 16;15(1):e0247723. doi: 10.1128/mbio.02477-23. Epub 2023 Dec 6. PMID:38054729<ref>PMID:38054729</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 8eqf" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>