tetano
Editor, Senior Moderator
Science
. 2020 Oct 20;eabe1502.
doi: 10.1126/science.abe1502. Online ahead of print.
Structural analysis of full-length SARS-CoV-2 spike protein from an advanced vaccine candidate
Sandhya Bangaru[SUP] 1 [/SUP], Gabriel Ozorowski[SUP] 1 [/SUP], Hannah L Turner[SUP] 1 [/SUP], Aleksandar Antanasijevic[SUP] 1 [/SUP], Deli Huang[SUP] 2 [/SUP], Xiaoning Wang[SUP] 3 [/SUP], Jonathan L Torres[SUP] 1 [/SUP], Jolene K Diedrich[SUP] 3 [/SUP], Jing-Hui Tian[SUP] 4 [/SUP], Alyse D Portnoff[SUP] 4 [/SUP], Nita Patel[SUP] 4 [/SUP], Michael J Massare[SUP] 4 [/SUP], John R Yates 3rd[SUP] 3 [/SUP], David Nemazee[SUP] 2 [/SUP], James C Paulson[SUP] 2 3 [/SUP], Greg Glenn[SUP] 4 [/SUP], Gale Smith[SUP] 4 [/SUP], Andrew B Ward[SUP] 5 [/SUP]
Affiliations
Abstract
Vaccine efforts against the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) responsible for the current COVID-19 pandemic are focused on SARS-CoV-2 spike glycoprotein, the primary target for neutralizing antibodies. We performed cryo-EM and site-specific glycan analysis of one of the leading subunit vaccine candidates from Novavax based on a full-length spike protein formulated in polysorbate 80 (PS 80) detergent. Our studies reveal a stable prefusion conformation of the spike immunogen with slight differences in the S1 subunit compared to published spike ectodomain structures. We also observed novel interactions between the spike trimers allowing formation of higher order spike complexes. This study confirms the structural integrity of the full-length spike protein immunogen and provides a basis for interpreting immune responses to this multivalent nanoparticle immunogen.
. 2020 Oct 20;eabe1502.
doi: 10.1126/science.abe1502. Online ahead of print.
Structural analysis of full-length SARS-CoV-2 spike protein from an advanced vaccine candidate
Sandhya Bangaru[SUP] 1 [/SUP], Gabriel Ozorowski[SUP] 1 [/SUP], Hannah L Turner[SUP] 1 [/SUP], Aleksandar Antanasijevic[SUP] 1 [/SUP], Deli Huang[SUP] 2 [/SUP], Xiaoning Wang[SUP] 3 [/SUP], Jonathan L Torres[SUP] 1 [/SUP], Jolene K Diedrich[SUP] 3 [/SUP], Jing-Hui Tian[SUP] 4 [/SUP], Alyse D Portnoff[SUP] 4 [/SUP], Nita Patel[SUP] 4 [/SUP], Michael J Massare[SUP] 4 [/SUP], John R Yates 3rd[SUP] 3 [/SUP], David Nemazee[SUP] 2 [/SUP], James C Paulson[SUP] 2 3 [/SUP], Greg Glenn[SUP] 4 [/SUP], Gale Smith[SUP] 4 [/SUP], Andrew B Ward[SUP] 5 [/SUP]
Affiliations
- PMID: 33082295
- DOI: 10.1126/science.abe1502
Abstract
Vaccine efforts against the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) responsible for the current COVID-19 pandemic are focused on SARS-CoV-2 spike glycoprotein, the primary target for neutralizing antibodies. We performed cryo-EM and site-specific glycan analysis of one of the leading subunit vaccine candidates from Novavax based on a full-length spike protein formulated in polysorbate 80 (PS 80) detergent. Our studies reveal a stable prefusion conformation of the spike immunogen with slight differences in the S1 subunit compared to published spike ectodomain structures. We also observed novel interactions between the spike trimers allowing formation of higher order spike complexes. This study confirms the structural integrity of the full-length spike protein immunogen and provides a basis for interpreting immune responses to this multivalent nanoparticle immunogen.