학술논문
SARS-CoV-2 immune evasion by the B.1.427/B.1.429 variant of concern
CORONAVIRUS
CORONAVIRUS
Document Type
Academic Journal
Author
Mccallum, Matthew; Bassi, Jessica; de Marco, Anna; Chen, Alex; Walls, Alexandra C.; di Lulio, Julia; Tortorici, M. Alejandra; Navarro, Mary-Jane; Silacci-Fregni, Chiara; Saliba, Christian; Sprouse, Kaitlin R.; Agostini, Maria; Pinto, Dora; Culap, Katja; Bianchi, Siro; Jaconi, Stefano; Cameroni, Elisabetta; Bowen, John E.; Tilles, Sasha W.; Pizzuto, Matteo Samuele; Guastalla, Sonja Bernasconi; Bona, Giovanni; Pellanda, Alessandra Franzetti; Garzoni, Christian; van Voorhis, Wesley C.; Rosen, Laura E.; Snell, Gyorgy; Telenti, Amalio; Virgin, Herbert W.; Piccoli, Luca; Corti, Davide; Veesler, David
Source
Science. August 6, 2021, Vol. 373 Issue 6555, p648, 7 p.
Subject
Language
English
ISSN
0036-8075
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.