Selection, biophysical and structural analysis of synthetic nanobodies that effectively neutralize SARS-CoV-2.
Angiotensin-Converting Enzyme 2
Antibodies, Monoclonal
/ immunology
Antibodies, Neutralizing
/ immunology
Antibodies, Viral
/ immunology
Betacoronavirus
/ immunology
COVID-19
Coronavirus Infections
/ prevention & control
Cryoelectron Microscopy
Humans
Neutralization Tests
Pandemics
/ prevention & control
Peptidyl-Dipeptidase A
/ metabolism
Pneumonia, Viral
/ prevention & control
Protein Binding
Protein Conformation
Protein Domains
/ immunology
Receptors, Virus
/ metabolism
SARS-CoV-2
Single-Domain Antibodies
/ immunology
Spike Glycoprotein, Coronavirus
/ immunology
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
04 11 2020
04 11 2020
Historique:
received:
16
06
2020
accepted:
01
10
2020
entrez:
5
11
2020
pubmed:
6
11
2020
medline:
18
11
2020
Statut:
epublish
Résumé
The coronavirus SARS-CoV-2 is the cause of the ongoing COVID-19 pandemic. Therapeutic neutralizing antibodies constitute a key short-to-medium term approach to tackle COVID-19. However, traditional antibody production is hampered by long development times and costly production. Here, we report the rapid isolation and characterization of nanobodies from a synthetic library, known as sybodies (Sb), that target the receptor-binding domain (RBD) of the SARS-CoV-2 spike protein. Several binders with low nanomolar affinities and efficient neutralization activity were identified of which Sb23 displayed high affinity and neutralized pseudovirus with an IC
Identifiants
pubmed: 33149112
doi: 10.1038/s41467-020-19204-y
pii: 10.1038/s41467-020-19204-y
pmc: PMC7642358
doi:
Substances chimiques
Antibodies, Monoclonal
0
Antibodies, Neutralizing
0
Antibodies, Viral
0
Receptors, Virus
0
Single-Domain Antibodies
0
Spike Glycoprotein, Coronavirus
0
spike protein, SARS-CoV-2
0
Peptidyl-Dipeptidase A
EC 3.4.15.1
ACE2 protein, human
EC 3.4.17.23
Angiotensin-Converting Enzyme 2
EC 3.4.17.23
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
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