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 == Publication Abstract from PubMed ==
-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.
+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.
-Controlling the SARS-CoV-2 Spike Glycoprotein Conformation.,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 18. doi: 10.1101/2020.05.18.102087. PMID:32511343<ref>PMID:32511343</ref>
+Controlling the SARS-CoV-2 spike glycoprotein conformation.,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 Jul 22. pii: 10.1038/s41594-020-0479-4. doi:, 10.1038/s41594-020-0479-4. PMID:32699321<ref>PMID:32699321</ref>
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>