tetano
Editor, Senior Moderator
Glycobiology
. 2020 Sep 3;cwaa085.
doi: 10.1093/glycob/cwaa085. Online ahead of print.
Site-specific characterisation of SARS-CoV-2 spike glycoprotein receptor binding domain
Aristotelis Antonopoulos[SUP] 1 [/SUP], Steven Broome[SUP] 2 [/SUP], Victor Sharov[SUP] 2 [/SUP], Christopher Ziegenfuss[SUP] 2 [/SUP], Richard L Easton[SUP] 3 [/SUP], Maria Panico[SUP] 1 2 3 [/SUP], Anne Dell[SUP] 1 [/SUP], Howard R Morris[SUP] 1 2 3 [/SUP], Stuart M Haslam[SUP] 1 [/SUP]
Affiliations
Abstract
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 characterise 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.
Keywords: Glycoproteomics; Mass Spectrometry; SARS-CoV-2; Spike Glycoprotein.
. 2020 Sep 3;cwaa085.
doi: 10.1093/glycob/cwaa085. Online ahead of print.
Site-specific characterisation of SARS-CoV-2 spike glycoprotein receptor binding domain
Aristotelis Antonopoulos[SUP] 1 [/SUP], Steven Broome[SUP] 2 [/SUP], Victor Sharov[SUP] 2 [/SUP], Christopher Ziegenfuss[SUP] 2 [/SUP], Richard L Easton[SUP] 3 [/SUP], Maria Panico[SUP] 1 2 3 [/SUP], Anne Dell[SUP] 1 [/SUP], Howard R Morris[SUP] 1 2 3 [/SUP], Stuart M Haslam[SUP] 1 [/SUP]
Affiliations
- PMID: 32886791
- DOI: 10.1093/glycob/cwaa085
Abstract
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 characterise 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.
Keywords: Glycoproteomics; Mass Spectrometry; SARS-CoV-2; Spike Glycoprotein.