Nanoscopic Assessment of Anti-SARS-CoV-2 Spike Neutralizing Antibody Using High-Speed AFM.
SARS-CoV-2 spike nanoparticle
SARS-CoV-2 spike protein
antibody-dependent enhancement
antispike neutralizing antibody
high-speed atomic force microscopy
nanoimaging
receptor-binding domain
Journal
Nano letters
ISSN: 1530-6992
Titre abrégé: Nano Lett
Pays: United States
ID NLM: 101088070
Informations de publication
Date de publication:
25 01 2023
25 01 2023
Historique:
pubmed:
16
1
2023
medline:
27
1
2023
entrez:
15
1
2023
Statut:
ppublish
Résumé
Anti-spike neutralizing antibodies (S NAbs) have been developed for prevention and treatment against COVID-19. The nanoscopic characterization of the dynamic interaction between spike proteins and S NAbs remains difficult. By using high-speed atomic force microscopy (HS-AFM), we elucidate the molecular property of an S NAb and its interaction with spike proteins. The S NAb appeared as monomers with a Y conformation at low density and formed hexameric oligomers at high density. The dynamic S NAb-spike protein interaction at RBD induces neither RBD opening nor S1 subunit shedding. Furthermore, the interaction was stable at endosomal pH. These findings indicated that the S NAb could have a negligible risk of antibody-dependent enhancement. Dynamic movement of spike proteins on small extracellular vesicles (S sEV) resembled that on SARS-CoV-2. The sensitivity of variant S sEVs to S NAb could be evaluated using HS-AFM. Altogether, we demonstrate a nanoscopic assessment platform for evaluating the binding property of S NAbs.
Identifiants
pubmed: 36641798
doi: 10.1021/acs.nanolett.2c04270
pmc: PMC9881159
doi:
Substances chimiques
Spike Glycoprotein, Coronavirus
0
Antibodies, Viral
0
Antibodies, Neutralizing
0
spike protein, SARS-CoV-2
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
619-628Références
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