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

Overview of attention for article published in bioRxiv, April 2021
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Title
SARS-CoV-2 immune evasion by variant B.1.427/B.1.429
Published in
bioRxiv, April 2021
DOI 10.1101/2021.03.31.437925
Pubmed ID
Authors

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, 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

Abstract

SARS-CoV-2 entry is mediated by the spike (S) glycoprotein which contains the receptor-binding domain (RBD) and the N-terminal domain (NTD) as the two main targets of neutralizing antibodies (Abs). A novel variant of concern (VOC) named CAL.20C (B.1.427/B.1.429) was originally detected in California and is currently spreading throughout the US and 29 additional countries. It is unclear whether antibody responses to SARS-CoV-2 infection or to the prototypic Wuhan-1 isolate-based vaccines will be impacted by the three B.1.427/B.1.429 S mutations: S13I, W152C and L452R. Here, we assessed neutralizing Ab responses following natural infection or mRNA vaccination using pseudoviruses expressing the wildtype or the B.1.427/B.1.429 S protein. Plasma from vaccinated or convalescent individuals exhibited neutralizing titers, which were reduced 3-6 fold against the B.1.427/B.1.429 variant relative to wildtype pseudoviruses. The RBD L452R mutation reduced or abolished neutralizing activity of 14 out of 35 RBD-specific monoclonal antibodies (mAbs), including three clinical-stage mAbs. Furthermore, we observed a complete loss of B.1.427/B.1.429 neutralization for a panel of mAbs targeting the N-terminal domain due to a large structural rearrangement of the NTD antigenic supersite involving an S13I-mediated shift of the signal peptide cleavage site. These data warrant closer monitoring of signal peptide variants and their involvement in immune evasion and show that Abs directed to the NTD impose a selection pressure driving SARS-CoV-2 viral evolution through conventional and unconventional escape mechanisms.

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Geographical breakdown

Country Count As %
Unknown 154 100%

Demographic breakdown

Readers by professional status Count As %
Researcher 30 19%
Student > Ph. D. Student 20 13%
Student > Master 14 9%
Student > Doctoral Student 6 4%
Professor 6 4%
Other 22 14%
Unknown 56 36%
Readers by discipline Count As %
Biochemistry, Genetics and Molecular Biology 30 19%
Immunology and Microbiology 17 11%
Medicine and Dentistry 14 9%
Agricultural and Biological Sciences 13 8%
Chemistry 5 3%
Other 20 13%
Unknown 55 36%