8DYA

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

8DYA の概要

• エントリーDOI: 10.2210/pdb8dya/pdb
• EMDBエントリー: 27779
• 分子名称: Spike glycoprotein, 2-acetamido-2-deoxy-beta-D-glucopyranose (2 entities in total)
• 機能のキーワード: sars-cov-2, covid-19, spike glycoprotein, fusion protein, neutralizing antibodies, structural genomics, seattle structural genomics center for infectious disease, ssgcid, viral protein
• 由来する生物種: Severe acute respiratory syndrome coronavirus 2
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 208516.10

構造登録者

Park, Y.J.,Seattle Structural Genomics Center for Infectious Disease (SSGCID),Veesler, D. (登録日: 2022-08-03, 公開日: 2022-11-30, 最終更新日: 2024-10-09)

主引用文献

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

実験手法

ELECTRON MICROSCOPY (3.67 Å)