tetano
Editor, Senior Moderator
Sci Rep
. 2021 Dec 7;11(1):23561.
doi: 10.1038/s41598-021-02904-w.
N-glycosylation profiles of the SARS-CoV-2 spike D614G mutant and its ancestral protein characterized by advanced mass spectrometry
Dongxia Wang[SUP] 1 [/SUP], Bin Zhou[SUP] 2 [/SUP], Theodore R Keppel[SUP] 3 [/SUP], Maria Solano[SUP] 3 [/SUP], Jakub Baudys[SUP] 3 [/SUP], Jason Goldstein[SUP] 4 [/SUP], M G Finn[SUP] 5 [/SUP], Xiaoyu Fan[SUP] 2 [/SUP], Asheley P Chapman[SUP] 5 [/SUP], Jonathan L Bundy[SUP] 3 [/SUP], Adrian R Woolfitt[SUP] 3 [/SUP], Sarah H Osman[SUP] 3 [/SUP], James L Pirkle[SUP] 3 [/SUP], David E Wentworth[SUP] 2 [/SUP], John R Barr[SUP] 6 [/SUP]
Affiliations
Abstract
N-glycosylation plays an important role in the structure and function of membrane and secreted proteins. The spike protein on the surface of the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), the virus that causes COVID-19, is heavily glycosylated and the major target for developing vaccines, therapeutic drugs and diagnostic tests. The first major SARS-CoV-2 variant carries a D614G substitution in the spike (S-D614G) that has been associated with altered conformation, enhanced ACE2 binding, and increased infectivity and transmission. In this report, we used mass spectrometry techniques to characterize and compare the N-glycosylation of the wild type (S-614D) or variant (S-614G) SARS-CoV-2 spike glycoproteins prepared under identical conditions. The data showed that half of the N-glycosylation sequons changed their distribution of glycans in the S-614G variant. The S-614G variant showed a decrease in the relative abundance of complex-type glycans (up to 45%) and an increase in oligomannose glycans (up to 33%) on all altered sequons. These changes led to a reduction in the overall complexity of the total N-glycosylation profile. All the glycosylation sites with altered patterns were in the spike head while the glycosylation of three sites in the stalk remained unchanged between S-614G and S-614D proteins.
. 2021 Dec 7;11(1):23561.
doi: 10.1038/s41598-021-02904-w.
N-glycosylation profiles of the SARS-CoV-2 spike D614G mutant and its ancestral protein characterized by advanced mass spectrometry
Dongxia Wang[SUP] 1 [/SUP], Bin Zhou[SUP] 2 [/SUP], Theodore R Keppel[SUP] 3 [/SUP], Maria Solano[SUP] 3 [/SUP], Jakub Baudys[SUP] 3 [/SUP], Jason Goldstein[SUP] 4 [/SUP], M G Finn[SUP] 5 [/SUP], Xiaoyu Fan[SUP] 2 [/SUP], Asheley P Chapman[SUP] 5 [/SUP], Jonathan L Bundy[SUP] 3 [/SUP], Adrian R Woolfitt[SUP] 3 [/SUP], Sarah H Osman[SUP] 3 [/SUP], James L Pirkle[SUP] 3 [/SUP], David E Wentworth[SUP] 2 [/SUP], John R Barr[SUP] 6 [/SUP]
Affiliations
- PMID: 34876606
- DOI: 10.1038/s41598-021-02904-w
Abstract
N-glycosylation plays an important role in the structure and function of membrane and secreted proteins. The spike protein on the surface of the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), the virus that causes COVID-19, is heavily glycosylated and the major target for developing vaccines, therapeutic drugs and diagnostic tests. The first major SARS-CoV-2 variant carries a D614G substitution in the spike (S-D614G) that has been associated with altered conformation, enhanced ACE2 binding, and increased infectivity and transmission. In this report, we used mass spectrometry techniques to characterize and compare the N-glycosylation of the wild type (S-614D) or variant (S-614G) SARS-CoV-2 spike glycoproteins prepared under identical conditions. The data showed that half of the N-glycosylation sequons changed their distribution of glycans in the S-614G variant. The S-614G variant showed a decrease in the relative abundance of complex-type glycans (up to 45%) and an increase in oligomannose glycans (up to 33%) on all altered sequons. These changes led to a reduction in the overall complexity of the total N-glycosylation profile. All the glycosylation sites with altered patterns were in the spike head while the glycosylation of three sites in the stalk remained unchanged between S-614G and S-614D proteins.