Structural and Functional Characterization of SARS-CoV-2 RBD Domains Produced in Mammalian Cells.
Journal
Analytical chemistry
ISSN: 1520-6882
Titre abrégé: Anal Chem
Pays: United States
ID NLM: 0370536
Informations de publication
Date de publication:
04 05 2021
04 05 2021
Historique:
pubmed:
20
4
2021
medline:
22
6
2021
entrez:
19
4
2021
Statut:
ppublish
Résumé
As the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) pandemic is still ongoing and dramatically influences our life, the need for recombinant viral proteins for diagnostics, vaccine development, and research is very high. The spike (S) protein, and particularly its receptor-binding domain (RBD), mediates the interaction with the angiotensin-converting enzyme 2 (ACE2) receptor on host cells and may be modulated by its structural features. Therefore, well-characterized recombinant RBDs are essential. We have performed an in-depth structural and functional characterization of RBDs expressed in Chinese hamster ovary (CHO) and human embryonic kidney 293 (HEK293) cells. To structurally characterize the native RBDs (comprising
Identifiants
pubmed: 33871970
doi: 10.1021/acs.analchem.1c00893
pmc: PMC8078197
doi:
Substances chimiques
Spike Glycoprotein, Coronavirus
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
6839-6847Références
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