Asset Details
Do you wish to reserve the book?
Structural basis for a conserved neutralization epitope on the receptor-binding domain of SARS-CoV-2
Hey, we have placed the reservation for you!
By the way, why not check out events that you can attend while you pick your title.
Oops! Something went wrong.
Looks like we were not able to place the reservation. Kindly try again later.
Are you sure you want to remove the book from the shelf?
Structural basis for a conserved neutralization epitope on the receptor-binding domain of SARS-CoV-2
Do you wish to request the book?
Structural basis for a conserved neutralization epitope on the receptor-binding domain of SARS-CoV-2
Please be aware that the book you have requested cannot be checked out. If you would like to checkout this book, you can reserve another copy
We have requested the book for you!
Your request is successful and it will be processed during the Library working hours. Please check the status of your request in My Requests.
Oops! Something went wrong.
Looks like we were not able to place your request. Kindly try again later.
Journal Article
Structural basis for a conserved neutralization epitope on the receptor-binding domain of SARS-CoV-2
2023
Overview
Antibody-mediated immunity plays a crucial role in protection against SARS-CoV-2 infection. We isolated a panel of neutralizing anti-receptor-binding domain (RBD) antibodies elicited upon natural infection and vaccination and showed that they recognize an immunogenic patch on the internal surface of the core RBD, which faces inwards and is hidden in the “down” state. These antibodies broadly neutralize wild type (Wuhan-Hu-1) SARS-CoV-2, Beta and Delta variants and some are effective against other sarbecoviruses. We observed a continuum of partially overlapping antibody epitopes from lower to upper part of the inner face of the RBD and some antibodies extend towards the receptor-binding motif. The majority of antibodies are substantially compromised by three mutational hotspots (S371L/F, S373P and S375F) in the lower part of the Omicron BA.1, BA.2 and BA.4/5 RBD. By contrast, antibody IY-2A induces a partial unfolding of this variable region and interacts with a conserved conformational epitope to tolerate all antigenic variations and neutralize diverse sarbecoviruses as well. This finding establishes that antibody recognition is not limited to the normal surface structures on the RBD. In conclusion, the delineation of functionally and structurally conserved RBD epitopes highlights potential vaccine and therapeutic candidates for COVID-19.
An antibody, IY-2A, identified from a panel of class-4 SARS-CoV-2-neutralizing antibodies isolated from convalescent and vaccinated individuals, targets and induces partial unfolding of a conserved epitope within the RBD. IY-2A retains activity against BA.4/5 subvariants and neutralizes diverse sarbecoviruses.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
Subject
/ 101/28
/ 82/1
/ Antigens
/ Binding
/ COVID-19
/ Domains
/ Epitopes
/ Humanities and Social Sciences
/ Humans
/ Science
/ Severe acute respiratory syndrome coronavirus 2
/ Severe acute respiratory syndrome-related coronavirus
/ Spike Glycoprotein, Coronavirus - genetics
