SARS-CoV-2 immune evasion by the B.1.427/B.1.429 variant of concern

被引:310
作者
McCallum, Matthew [1 ]
Bassi, Jessica [2 ]
De Marco, Anna [2 ]
Chen, Alex [3 ]
Walls, Alexandra C. [1 ]
Di Iulio, Julia [3 ]
Tortorici, M. Alejandra [1 ]
Navarro, Mary-Jane [1 ]
Silacci-Fregni, Chiara [2 ]
Saliba, Christian [2 ]
Sprouse, Kaitlin R. [1 ]
Agostini, Maria [3 ]
Pinto, Dora [2 ]
Culap, Katja [2 ]
Bianchi, Siro [2 ]
Jaconi, Stefano [2 ]
Cameroni, Elisabetta [2 ]
Bowen, John E. [1 ]
Tilles, Sasha W. [4 ]
Pizzuto, Matteo Samuele [2 ]
Guastalla, Sonja Bernasconi
Bona, Giovanni [5 ]
Pellanda, Alessandra Franzetti [5 ]
Garzoni, Christian [6 ]
Van Voorhis, Wesley C. [4 ]
Rosen, Laura E. [3 ]
Snell, Gyorgy [3 ]
Telenti, Amalio [3 ]
Virgin, Herbert W. [3 ]
Piccoli, Luca [2 ]
Corti, Davide [2 ]
Veesler, David [1 ]
机构
[1] Univ Washington, Dept Biochem, Seattle, WA 98195 USA
[2] Humabs Biomed SA, CH-6500 Bellinzona, Switzerland
[3] Vir Biotechnol, San Francisco, CA 94158 USA
[4] Univ Washington, Ctr Emerging & Reemerging Infect Dis, Dept Med, Div Allergy & Infect Dis,Sch Med, Seattle, WA 98195 USA
[5] Clin Luganese Moncucco, Clin Res Unit, CH-6900 Lugano, Switzerland
[6] Clin Luganese Moncucco, Clin Internal Med & Infect Dis, CH-6900 Lugano, Switzerland
基金
加拿大自然科学与工程研究理事会;
关键词
RECEPTOR-BINDING DOMAIN; SPIKE; VALIDATION; MICROSCOPY; RESOLUTION; VISUALIZATION; SOFTWARE; SYSTEM; MODEL; ACE2;
D O I
10.1126/science.abi7994
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
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.
引用
收藏
页码:648 / +
页数:41
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