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Y380Q novel mutation in receptor-binding domain of SARS-CoV-2 spike protein together with C379W interfere in the neutralizing antibodies interaction

Authors :
Ivaine Tais Sauthier Sartor
Fernanda Hammes Varela
Mariana Rost Meireles
Luciane Beatriz Kern
Thaís Raupp Azevedo
Gabriela Luchiari Tumioto Giannini
Mariana Soares da Silva
Meriane Demoliner
Juliana Schons Gularte
Paula Rodrigues de Almeida
Juliane Deise Fleck
Gabriela Oliveira Zavaglia
Ingrid Rodrigues Fernandes
Caroline Nespolo de David
Amanda Paz Santos
Walquiria Aparecida Ferreira de Almeida
Victor Bertollo Gomes Porto
Marcelo Comerlato Scotta
Gustavo Fioravanti Vieira
Fernando Rosado Spilki
Renato T. Stein
Márcia Polese-Bonatto
Source :
Diagnostic Microbiology and Infectious Disease, Repositório Institucional do Centro Universitário La Salle, Universidade La Salle (UNILASALLE), instacron:UNILASALLE
Publication Year :
2022
Publisher :
Elsevier Inc., 2022.

Abstract

We aimed to describe the SARS-CoV-2 lineages circulating early pandemic among samples with S gene dropout and characterize the receptor-binding domain (RBD) of viral spike protein. Adults and children older than 2 months with signs and symptoms of COVID-19 were prospectively enrolled from May to October in Porto Alegre, Brazil. All participants performed RT-PCR assay, and samples with S gene dropout and cycle threshold < 30 were submitted to high-throughput sequencing (HTS). 484 out of 1,557 participants tested positive for SARS-CoV-2. The S gene dropout was detected in 7.4% (36/484) and a peak was observed in August. The B.1.1.28, B.1.91 and B.1.1.33 lineages were circulating in early pandemic. The RBD novel mutation (Y380Q) was found in one sample occurring simultaneously with C379W and V395A, and the B.1.91 lineage in the spike protein. The Y380Q and C379W may interfere with the binding of neutralizing antibodies (CR3022, EY6A, H014, S304).

Details

Language :
English
ISSN :
18790070 and 07328893
Database :
OpenAIRE
Journal :
Diagnostic Microbiology and Infectious Disease
Accession number :
edsair.doi.dedup.....1d18ecd60c88d68ad0c16d89cc83c917