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10.1038/s41594-020-0479-4 http://scihub22266oqcxt.onion/10.1038/s41594-020-0479-4 32699321!8581954!32699321     free     free     free Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Nat+Struct+Mol+Biol 2020 ; 27 (10): 925-933 Nephropedia Template TP {{tp|p=32699321|t=2020. Controlling the SARS-CoV-2 spike glycoprotein conformation |pdf=|usr=}}{{32699321}} gab.com Text Controlling the SARS-CoV-2 spike glycoprotein conformation JO: Nat Struct Mol Biol http://www.kidney.de/pget.php?&tw=1&pmid=32699321 #FOAvip The coronavirus (CoV) spike (S) protein, involved in viral-host cell fusion, is the primary immunogenic target for virus neutralization and the current focus of many vaccine design efforts. The highly flexible S-protein, with its mobile domains, presents a moving target to the immune system. Here, to better understand S-protein mobility, we implemented a structure-based vector analysis of available beta-CoV S-protein structures. Despite an overall similarity in domain organization, we found that S-proteins from different beta-CoVs display distinct configurations. Based on this analysis, we developed two soluble ectodomain constructs for the SARS-CoV-2 S-protein, in which the highly immunogenic and mobile receptor binding domain (RBD) is either locked in the all-RBDs 'down' position or adopts 'up' state conformations more readily than the wild-type S-protein. These results demonstrate that the conformation of the S-protein can be controlled via rational design and can provide a framework for the development of engineered CoV S-proteins for vaccine applications. Twit Text FOAVip Controlling the SARS-CoV-2 spike glycoprotein conformation ????Nat Struct Mol Biol http://www.kidney.de/pget.php?&tw=1&pmid=32699321 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=32699321 #FOAvip English Wikipedia <ref>{{Cite pmid|32699321}}</ref> Controlling the SARS-CoV-2 spike glycoprotein conformation #MMPMID32699321 Henderson R; Edwards RJ; Mansouri K; Janowska K; Stalls V; Gobeil SMC; Kopp M; Li D; Parks R; Hsu AL; Borgnia MJ; Haynes BF; Acharya P Nat Struct Mol Biol 2020[Oct]; 27 (10): 925-933 PMID32699321show ga The coronavirus (CoV) spike (S) protein, involved in viral-host cell fusion, is the primary immunogenic target for virus neutralization and the current focus of many vaccine design efforts. The highly flexible S-protein, with its mobile domains, presents a moving target to the immune system. Here, to better understand S-protein mobility, we implemented a structure-based vector analysis of available beta-CoV S-protein structures. Despite an overall similarity in domain organization, we found that S-proteins from different beta-CoVs display distinct configurations. Based on this analysis, we developed two soluble ectodomain constructs for the SARS-CoV-2 S-protein, in which the highly immunogenic and mobile receptor binding domain (RBD) is either locked in the all-RBDs 'down' position or adopts 'up' state conformations more readily than the wild-type S-protein. These results demonstrate that the conformation of the S-protein can be controlled via rational design and can provide a framework for the development of engineered CoV S-proteins for vaccine applications. |Binding Sites[MESH] |Cryoelectron Microscopy[MESH] |Microscopy, Electron/methods[MESH] |Models, Molecular[MESH] |Mutation[MESH] |Protein Conformation[MESH] |Protein Domains[MESH] |Protein Subunits/chemistry[MESH]Controlling the SARS-CoV-2 spike glycoprotein conformation (epmc).pdf DeepDyve Pubget Overpricing