| Literature DB >> 34210893 |
Matthew McCallum1, Jessica Bassi2, Anna De Marco2, Alex Chen3, Alexandra C Walls1, Julia Di Iulio3, M Alejandra Tortorici1, Mary-Jane Navarro1, Chiara Silacci-Fregni2, Christian Saliba2, Kaitlin R Sprouse1, Maria Agostini3, Dora Pinto2, Katja Culap2, Siro Bianchi2, Stefano Jaconi2, Elisabetta Cameroni2, John E Bowen1, Sasha W Tilles4, Matteo Samuele Pizzuto2, Sonja Bernasconi Guastalla5, Giovanni Bona6, Alessandra Franzetti Pellanda6, Christian Garzoni7, Wesley C Van Voorhis4, Laura E Rosen3, Gyorgy Snell3, Amalio Telenti3, Herbert W Virgin3, Luca Piccoli8, Davide Corti8, David Veesler9.
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.Entities:
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Year: 2021 PMID: 34210893 DOI: 10.1126/science.abi7994
Source DB: PubMed Journal: Science ISSN: 0036-8075 Impact factor: 47.728