학술논문
Structural analysis of full-length SARS-CoV-2 spike protein from an advanced vaccine candidate
CORONAVIRUS
CORONAVIRUS
Document Type
Academic Journal
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., III; Nemazee, David; Paulson, James C.; Glenn, Greg; Smith, Gale; Ward, Andrew B.
Source
Science. Nov 27, 2020, Vol. 370 Issue 6520, p1089, 6 p.
Subject
Language
English
ISSN
0036-8075
Abstract
Vaccine efforts to combat the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), which is responsible for the current coronavirus disease 2019 (COVID-19) pandemic, are focused on SARS-CoV-2 spike glycoprotein, the primary target for neutralizing antibodies. We performed cryo-election microscopy and site-specific glycan analysis of one of the leading subunit vaccine candidates from Novavax, which is based on a full-length spike protein formulated in polysorbate 80 detergent. Our studies reveal a stable prefusion conformation of the spike immunogen with slight differences in the S1 subunit compared with published spike ectodomain structures. We also observed 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.