8DYA

Structure of the SARS-CoV-2 spike glycoprotein S2 subunit

Summary for 8DYA

• Entry DOI: 10.2210/pdb8dya/pdb
• EMDB information: 27779
• Descriptor: Spike glycoprotein, 2-acetamido-2-deoxy-beta-D-glucopyranose (2 entities in total)
• Functional Keywords: sars-cov-2, covid-19, spike glycoprotein, fusion protein, neutralizing antibodies, structural genomics, seattle structural genomics center for infectious disease, ssgcid, viral protein
• Biological source: Severe acute respiratory syndrome coronavirus 2
• Total number of polymer chains: 3
• Total formula weight: 208516.10

Authors

Park, Y.J.,Seattle Structural Genomics Center for Infectious Disease (SSGCID),Veesler, D. (deposition date: 2022-08-03, release date: 2022-11-30, Last modification date: 2024-10-09)

Primary citation

Bowen, J.E.,Park, Y.J.,Stewart, C.,Brown, J.T.,Sharkey, W.K.,Walls, A.C.,Joshi, A.,Sprouse, K.R.,McCallum, M.,Tortorici, M.A.,Franko, N.M.,Logue, J.K.,Mazzitelli, I.G.,Nguyen, A.W.,Silva, R.P.,Huang, Y.,Low, J.S.,Jerak, J.,Tiles, S.W.,Ahmed, K.,Shariq, A.,Dan, J.M.,Zhang, Z.,Weiskopf, D.,Sette, A.,Snell, G.,Posavad, C.M.,Iqbal, N.T.,Geffner, J.,Bandera, A.,Gori, A.,Sallusto, F.,Maynard, J.A.,Crotty, S.,Van Voorhis, W.C.,Simmerling, C.,Grifantini, R.,Chu, H.Y.,Corti, D.,Veesler, D.
SARS-CoV-2 spike conformation determines plasma neutralizing activity elicited by a wide panel of human vaccines.
Sci Immunol, 7:eadf1421-eadf1421, 2022

PubMed Abstract: Numerous safe and effective coronavirus disease 2019 vaccines have been developed worldwide that use various delivery technologies and engineering strategies. We show here that vaccines containing prefusion-stabilizing S mutations elicit antibody responses in humans with enhanced recognition of S and the S subunit relative to postfusion S as compared with vaccines lacking these mutations or natural infection. Prefusion S and S antibody binding titers positively and equivalently correlated with neutralizing activity, and depletion of S-directed antibodies completely abrogated plasma neutralizing activity. We show that neutralizing activity is almost entirely directed to the S subunit and that variant cross-neutralization is mediated solely by receptor binding domain-specific antibodies. Our data provide a quantitative framework for guiding future S engineering efforts to develop vaccines with higher resilience to the emergence of variants than current technologies.

PubMed: 36356052
DOI: 10.1126/sciimmunol.adf1421

Experimental method

ELECTRON MICROSCOPY (3.67 Å)