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10.1101/2020.05.18.102087 http://scihub22266oqcxt.onion/10.1101/2020.05.18.102087 32511343!7252579!32511343     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       bioRxiv 2020 ; ä (ä): ä Nephropedia Template TP {{tp|p=32511343|t=2020. Controlling the SARS-CoV-2 Spike Glycoprotein Conformation |pdf=|usr=}}{{32511343}} gab.com Text Controlling the SARS-CoV-2 Spike Glycoprotein Conformation JO: bioRxiv http://www.kidney.de/pget.php?&tw=1&pmid=32511343 #FOAvip The coronavirus (CoV) viral host cell fusion spike (S) protein 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. We found that despite overall similarity in domain organization, different beta-CoV strains display distinct S-protein configurations. Based on this analysis, we developed two soluble ectodomain constructs in which the highly immunogenic and mobile receptor binding domain (RBD) is locked in either the all-RBDs 'down' position or is induced to display a previously unobserved in SARS-CoV-2 2-RBDs 'up' configuration. These results demonstrate that the conformation of the S-protein can be controlled via rational design and provide a framework for the development of engineered coronavirus spike proteins for vaccine applications. Twit Text FOAVip Controlling the SARS-CoV-2 Spike Glycoprotein Conformation ????bioRxiv http://www.kidney.de/pget.php?&tw=1&pmid=32511343 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=32511343 #FOAvip English Wikipedia <ref>{{Cite pmid|32511343}}</ref> Controlling the SARS-CoV-2 Spike Glycoprotein Conformation #MMPMID32511343 Henderson R; Edwards RJ; Mansouri K; Janowska K; Stalls V; Gobeil S; Kopp M; Hsu A; Borgnia M; Parks R; Haynes BF; Acharya P bioRxiv 2020[May]; ä (ä): ä PMID32511343show ga The coronavirus (CoV) viral host cell fusion spike (S) protein 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. We found that despite overall similarity in domain organization, different beta-CoV strains display distinct S-protein configurations. Based on this analysis, we developed two soluble ectodomain constructs in which the highly immunogenic and mobile receptor binding domain (RBD) is locked in either the all-RBDs 'down' position or is induced to display a previously unobserved in SARS-CoV-2 2-RBDs 'up' configuration. These results demonstrate that the conformation of the S-protein can be controlled via rational design and provide a framework for the development of engineered coronavirus spike proteins for vaccine applications. äControlling the SARS-CoV-2 Spike Glycoprotein Conformation (epmc).pdf DeepDyve Pubget Overpricing