7N8H

SARS-CoV-2 S (B.1.429 / epsilon variant) + S2M11 + S2L20 Global Refinement

7N8H の概要

• エントリーDOI: 10.2210/pdb7n8h/pdb
• EMDBエントリー: 24236
• 分子名称: Spike glycoprotein, S2M11 Fab Light Chain variable region, S2M11 Fab Heavy Chain variable region, ... (9 entities in total)
• 機能のキーワード: coronavirus, antibody, california, structural genomics, seattle structural genomics center for infectious disease, ssgcid, viral protein, viral protein-immune system complex, viral protein/immune system
• 由来する生物種: Severe acute respiratory syndrome coronavirus 2 (2019-nCoV, SARS-CoV-2); 詳細
• タンパク質・核酸の鎖数: 15
• 化学式量合計: 587379.76

構造登録者

McCallum, M.,Veesler, D.,Seattle Structural Genomics Center for Infectious Disease (SSGCID) (登録日: 2021-06-14, 公開日: 2021-07-14, 最終更新日: 2024-11-13)

主引用文献

McCallum, M.,Bassi, J.,De Marco, A.,Chen, A.,Walls, A.C.,Di Iulio, J.,Tortorici, M.A.,Navarro, M.J.,Silacci-Fregni, C.,Saliba, C.,Sprouse, K.R.,Agostini, M.,Pinto, D.,Culap, K.,Bianchi, S.,Jaconi, S.,Cameroni, E.,Bowen, J.E.,Tilles, S.W.,Pizzuto, M.S.,Guastalla, S.B.,Bona, G.,Pellanda, A.F.,Garzoni, C.,Van Voorhis, W.C.,Rosen, L.E.,Snell, G.,Telenti, A.,Virgin, H.W.,Piccoli, L.,Corti, D.,Veesler, D.
SARS-CoV-2 immune evasion by the B.1.427/B.1.429 variant of concern.
Science, 373:648-654, 2021

PubMed Abstract: A novel variant of concern (VOC) named CAL.20C (B.1.427/B.1.429), which was originally detected in California, carries spike glycoprotein mutations S13I in the signal peptide, W152C in the N-terminal domain (NTD), and L452R in the receptor-binding domain (RBD). Plasma from individuals vaccinated with a Wuhan-1 isolate-based messenger RNA vaccine or from convalescent individuals exhibited neutralizing titers that were reduced 2- to 3.5-fold against the B.1.427/B.1.429 variant relative to wild-type pseudoviruses. The L452R mutation reduced neutralizing activity in 14 of 34 RBD-specific monoclonal antibodies (mAbs). The S13I and W152C mutations resulted in total loss of neutralization for 10 of 10 NTD-specific mAbs because the NTD antigenic supersite was remodeled by a shift of the signal peptide cleavage site and the formation of a new disulfide bond, as revealed by mass spectrometry and structural studies.

PubMed: 34210893
DOI: 10.1126/science.abi7994

実験手法

ELECTRON MICROSCOPY (2.3 Å)