Asset Details
Do you wish to reserve the book?
Structural basis for potent neutralization of SARS-CoV-2 and role of antibody affinity maturation
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 potent neutralization of SARS-CoV-2 and role of antibody affinity maturation
Do you wish to request the book?
Structural basis for potent neutralization of SARS-CoV-2 and role of antibody affinity maturation
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 potent neutralization of SARS-CoV-2 and role of antibody affinity maturation
2020
Overview
SARS-CoV-2 is a betacoronavirus virus responsible for the COVID-19 pandemic. Here, we determine the X-ray crystal structure of a potent neutralizing monoclonal antibody, CV30, isolated from a patient infected with SARS-CoV-2, in complex with the receptor binding domain. The structure reveals that CV30 binds to an epitope that overlaps with the human ACE2 receptor binding motif providing a structural basis for its neutralization. CV30 also induces shedding of the S1 subunit, indicating an additional mechanism of neutralization. A germline reversion of CV30 results in a substantial reduction in both binding affinity and neutralization potential indicating the minimal somatic mutation is needed for potently neutralizing antibodies against SARS-CoV-2.
Currently there is neither a vaccine nor an effective treatment strategy available for COVID19. Here, Hurlburt et al. provide the crystal structure of a patient-derived monoclonal antibody neutralizing SARS-CoV-2 via shedding of the S1 subunit and competing for the receptor binding domain.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
Subject
/ 13/106
/ 82/80
/ 82/83
/ ACE2
/ Affinity
/ Angiotensin-Converting Enzyme 2
/ Antibodies, Blocking - chemistry
/ Antibodies, Blocking - immunology
/ Antibodies, Monoclonal - chemistry
/ Antibodies, Monoclonal - immunology
/ Antibodies, Neutralizing - chemistry
/ Antibodies, Neutralizing - immunology
/ Betacoronavirus - immunology
/ Binding
/ Coronavirus Infections - immunology
/ COVID-19
/ Domains
/ Epitopes
/ Humanities and Social Sciences
/ Humans
/ Mutation
/ Peptidyl-Dipeptidase A - chemistry
/ Peptidyl-Dipeptidase A - metabolism
/ Pneumonia, Viral - immunology
/ Protein Interaction Domains and Motifs
/ Science
/ Severe acute respiratory syndrome coronavirus 2
/ Shedding
/ Somatic Hypermutation, Immunoglobulin
/ Spike Glycoprotein, Coronavirus - chemistry
