National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
米国
引用
ジャーナル: Science / 年: 2021 タイトル: SARS-CoV-2 immune evasion by the B.1.427/B.1.429 variant of concern. 著者: Matthew McCallum / Jessica Bassi / Anna De Marco / Alex Chen / Alexandra C Walls / Julia Di Iulio / M Alejandra Tortorici / Mary-Jane Navarro / Chiara Silacci-Fregni / Christian Saliba / ...著者: Matthew McCallum / Jessica Bassi / Anna De Marco / Alex Chen / Alexandra C Walls / Julia Di Iulio / M Alejandra Tortorici / Mary-Jane Navarro / Chiara Silacci-Fregni / Christian Saliba / Kaitlin R Sprouse / Maria Agostini / Dora Pinto / Katja Culap / Siro Bianchi / Stefano Jaconi / Elisabetta Cameroni / John E Bowen / Sasha W Tilles / Matteo Samuele Pizzuto / Sonja Bernasconi Guastalla / Giovanni Bona / Alessandra Franzetti Pellanda / Christian Garzoni / Wesley C Van Voorhis / Laura E Rosen / Gyorgy Snell / Amalio Telenti / Herbert W Virgin / Luca Piccoli / Davide Corti / David Veesler / 要旨: 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 ...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.