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Two linear epitopes on the SARS-CoV-2 spike protein that elicit neutralising antibodies in COVID-19 patients

Authors :
Lisa F. P. Ng
Yee Sin Leo
Nicholas Kim-Wah Yeo
Cheryl Yi-Pin Lee
Cheng-I Wang
Rhonda Sin-Ling Chee
Barnaby Edward Young
Siew Yee Thien
Siew-Wai Fong
Guillaume Carissimo
Seow Yen Tan
Shirin Kalimuddin
Mark I-Cheng Chen
Anthony Torres-Ruesta
Chek Meng Poh
Shirley Seah Gek Kheng
Bei Wang
Laurent Rénia
Louis Yi Ann Chai
David C. Lye
Brendon J. Hanson
Wen Hsin Lee
Siti Naqiah Amrun
Source :
Nature Communications, Vol 11, Iss 1, Pp 1-7 (2020), Nature Communications
Publication Year :
2020
Publisher :
Springer Science and Business Media LLC, 2020.

Abstract

Given the ongoing SARS-CoV-2 pandemic, identification of immunogenic targets against the coronavirus spike glycoprotein will provide crucial advances towards the development of sensitive diagnostic tools and potential vaccine candidate targets. In this study, using pools of overlapping linear B-cell peptides, we report two IgG immunodominant regions on SARS-CoV-2 spike glycoprotein that are recognised by sera from COVID-19 convalescent patients. Notably, one is specific to SARS-CoV-2, which is located in close proximity to the receptor binding domain. The other region, which is localised at the fusion peptide, could potentially function as a pan-SARS target. Functionally, antibody depletion assays demonstrate that antibodies targeting these immunodominant regions significantly alter virus neutralisation capacities. Taken together, identification and validation of these neutralising B-cell epitopes will provide insights towards the design of diagnostics and vaccine candidates against this high priority coronavirus.<br />Characterisation of the human antibody response to SARS-CoV-2 can help the design of serological tests and vaccines. Here, the authors identify two linear epitopes in SARS-CoV-2 spike protein that elicit neutralising antibodies in several patients and could thus be useful for serology and vaccine development.

Details

ISSN :
20411723
Volume :
11
Database :
OpenAIRE
Journal :
Nature Communications
Accession number :
edsair.doi.dedup.....2640c34238c15442b36b3df7dbec3883