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Structural analysis of full-length SARS-CoV-2 spike protein from an advanced vaccine candidate

By Sandhya Bangaru, Gabriel Ozorowski, Hannah L. Turner, Aleksandar Antanasijevic, Deli Huang, Xiaoning Wang, Jonathan L. Torres, Jolene K. Diedrich, Jing-Hui Tian, Alyse D Portnoff, Nita Patel, Michael J Massare, John R. Yates, David Nemazee, James C. Paulson, Greg Glenn, Gale Smith, Andrew B Ward

Posted 06 Aug 2020
bioRxiv DOI: 10.1101/2020.08.06.234674

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. ### Competing Interest Statement Authors J.H.T, A.D.P, N.P, M.J.M, G.G, and G.S are current employees of Novavax, Inc., a for-profit organization, and these authors own stock or hold stock options. These interests do not alter the authors adherence to policies on sharing data and materials. All other authors have no competing interests to declare.

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