Author: Bangaru, Sandhya; Ozorowski, Gabriel; Turner, Hannah L.; Antanasijevic, Aleksandar; Huang, Deli; Wang, Xiaoning; Torres, Jonathan L.; Diedrich, Jolene K.; Tian, Jing-Hui; Portnoff, Alyse D.; Patel, Nita; Massare, Michael J.; Yates, John R.; Nemazee, David; Paulson, James C.; Glenn, Greg; Smith, Gale; Ward, Andrew B.
Title: Structural analysis of full-length SARS-CoV-2 spike protein from an advanced vaccine candidate Cord-id: 6wo2o5pp Document date: 2020_8_6
ID: 6wo2o5pp
Snippet: 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. Here, 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
Document: 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. Here, 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. Interestingly, 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.
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