Site-specific characterization of SARS-CoV-2 spike glycoprotein receptor-binding domain.
Department of Life Sciences, Imperial College London, London, SW7 2AZ, UK.
BioPharmaSpec Inc, 363 Phoenixville Pike, Malvern, PA 19355, USA.
BioPharmaSpec Ltd, Suite 3.1, Lido Medical Centre, St. Saviour, Jersey, JE2 7LA, UK.
- Published Article
Oxford University Press
- Publication Date
Apr 01, 2021
The novel coronavirus SARS-CoV-2, the infective agent causing COVID-19, is having a global impact both in terms of human disease as well as socially and economically. Its heavily glycosylated spike glycoprotein is fundamental for the infection process, via its receptor-binding domains interaction with the glycoprotein angiotensin-converting enzyme 2 on human cell surfaces. We therefore utilized an integrated glycomic and glycoproteomic analytical strategy to characterize both N- and O- glycan site-specific glycosylation within the receptor-binding domain. We demonstrate the presence of complex-type N-glycans with unusual fucosylated LacdiNAc at both sites N331 and N343 and a single site of O-glycosylation on T323. © The Author(s) 2020. Published by Oxford University Press.
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This record was last updated on 04/18/2021 and may not reflect the most current and accurate biomedical/scientific data available from NLM.
The corresponding record at NLM can be accessed at https://www.ncbi.nlm.nih.gov/pubmed/32886791