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Deprecated: Implicit conversion from float 263.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Mol+Ther 2021 ; 29 (6): 1984-2000 Nephropedia Template TP
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Nanoluciferase complementation-based bioreporter reveals the importance of N-linked glycosylation of SARS-CoV-2 S for viral entry #MMPMID33578036
Azad T; Singaravelu R; Taha Z; Jamieson TR; Boulton S; Crupi MJF; Martin NT; Fekete EEF; Poutou J; Ghahremani M; Pelin A; Nouri K; Rezaei R; Marshall CB; Enomoto M; Arulanandam R; Alluqmani N; Samson R; Gingras AC; Cameron DW; Greer PA; Ilkow CS; Diallo JS; Bell JC
Mol Ther 2021[Jun]; 29 (6): 1984-2000 PMID33578036show ga
The ongoing COVID-19 pandemic has highlighted the immediate need for the development of antiviral therapeutics targeting different stages of the SARS-CoV-2 life cycle. We developed a bioluminescence-based bioreporter to interrogate the interaction between the SARS-CoV-2 viral spike (S) protein and its host entry receptor, angiotensin-converting enzyme 2 (ACE2). The bioreporter assay is based on a nanoluciferase complementation reporter, composed of two subunits, large BiT and small BiT, fused to the S receptor-binding domain (RBD) of the SARS-CoV-2 S protein and ACE2 ectodomain, respectively. Using this bioreporter, we uncovered critical host and viral determinants of the interaction, including a role for glycosylation of asparagine residues within the RBD in mediating successful viral entry. We also demonstrate the importance of N-linked glycosylation to the RBD's antigenicity and immunogenicity. Our study demonstrates the versatility of our bioreporter in mapping key residues mediating viral entry as well as screening inhibitors of the ACE2-RBD interaction. Our findings point toward targeting RBD glycosylation for therapeutic and vaccine strategies against SARS-CoV-2.