Structural and Functional Characterization of SARS-CoV-2 RBD Domains Produced in Mammalian Cells
Christoph Gstöttner, Tao Zhang, Anja Resemann, Sophia Ruben, Stuart Pengelley, Detlev Suckau, Tim Welsink, Manfred Wuhrer, Elena Domínguez‐Vega
Abstract
-glycans. Additionally, using an alternative approach based on N-terminal cleavage of the O-glycosylation, the previously unknown O-glycosylation site was localized at T323. For both RBDs, the binding to SARS-CoV-2 antibodies of positive patients and affinity to the ACE2 receptor was addressed showing comparable results. This work not only offers insights into RBD structural and functional features but also provides an analytical workflow for characterization of new RBDs and batch-to-batch comparison.
Topics & Concepts
Chinese hamster ovary cellChemistryGlycosylationHEK 293 cellsGlycanFucosylationRecombinant DNAComputational biologyAngiotensin-converting enzyme 2ReceptorBiochemistryCoronavirus disease 2019 (COVID-19)GlycoproteinGeneBiologyMedicineDiseaseInfectious disease (medical specialty)PathologySARS-CoV-2 and COVID-19 ResearchInfluenza Virus Research StudiesAnimal Virus Infections Studies