tetano
Editor, Senior Moderator
Cell Rep
. 2022 May 20;110924.
doi: 10.1016/j.celrep.2022.110924. Online ahead of print.
Functional properties of the spike glycoprotein of the emerging SARS-CoV-2 variant B.1.1.529
Qian Wang[SUP] 1 [/SUP], Saumya Anang[SUP] 2 [/SUP], Sho Iketani[SUP] 3 [/SUP], Yicheng Guo[SUP] 3 [/SUP], Lihong Liu[SUP] 3 [/SUP], Phinikoula S Katsamba[SUP] 4 [/SUP], Lawrence Shapiro[SUP] 5 [/SUP], David D Ho[SUP] 3 [/SUP], Joseph G Sodroski[SUP] 6 [/SUP]
Affiliations
Abstract
The recently emerged B.1.1.529 (Omicron) severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) variant has a highly divergent spike (S) glycoprotein. We compared the functional properties of B.1.1.529 BA.1 S with those of previous globally prevalent SARS-CoV-2 variants, D614G and B.1.617.2. Relative to these variants, B.1.1.529 S exhibits decreases in processing, syncytium formation, virion incorporation, and ability to mediate infection of cells with high TMPRSS2 expression. B.1.1.529 and B.1.617.2 S glycoproteins bind ACE2 with higher affinity than D614G S. The unliganded B.1.1.529 S trimer is less stable at low temperatures than the other SARS-CoV-2 Ss, a property related to its more "open" S conformation. Upon ACE2 binding, the B.1.1.529 S trimer sheds S1 at 37°C, but not at 0°C. B.1.1.529 pseudoviruses are relatively resistant to neutralization by sera from patients with coronavirus disease 2019 (COVID-19) and vaccinees. These properties of the B.1.1.529 S glycoprotein likely influence the transmission, cytopathic effects, and immune evasion of this emerging variant.
Keywords: ACE2 affinity; B.1.1.529; B.1.617.2; CP: Immunology; CP: Microbiology; Omicron; S1 shedding; SARS-CoV-2; neutralization sensitivity; stability; variants.
. 2022 May 20;110924.
doi: 10.1016/j.celrep.2022.110924. Online ahead of print.
Functional properties of the spike glycoprotein of the emerging SARS-CoV-2 variant B.1.1.529
Qian Wang[SUP] 1 [/SUP], Saumya Anang[SUP] 2 [/SUP], Sho Iketani[SUP] 3 [/SUP], Yicheng Guo[SUP] 3 [/SUP], Lihong Liu[SUP] 3 [/SUP], Phinikoula S Katsamba[SUP] 4 [/SUP], Lawrence Shapiro[SUP] 5 [/SUP], David D Ho[SUP] 3 [/SUP], Joseph G Sodroski[SUP] 6 [/SUP]
Affiliations
- PMID: 35658975
- DOI: 10.1016/j.celrep.2022.110924
Abstract
The recently emerged B.1.1.529 (Omicron) severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) variant has a highly divergent spike (S) glycoprotein. We compared the functional properties of B.1.1.529 BA.1 S with those of previous globally prevalent SARS-CoV-2 variants, D614G and B.1.617.2. Relative to these variants, B.1.1.529 S exhibits decreases in processing, syncytium formation, virion incorporation, and ability to mediate infection of cells with high TMPRSS2 expression. B.1.1.529 and B.1.617.2 S glycoproteins bind ACE2 with higher affinity than D614G S. The unliganded B.1.1.529 S trimer is less stable at low temperatures than the other SARS-CoV-2 Ss, a property related to its more "open" S conformation. Upon ACE2 binding, the B.1.1.529 S trimer sheds S1 at 37°C, but not at 0°C. B.1.1.529 pseudoviruses are relatively resistant to neutralization by sera from patients with coronavirus disease 2019 (COVID-19) and vaccinees. These properties of the B.1.1.529 S glycoprotein likely influence the transmission, cytopathic effects, and immune evasion of this emerging variant.
Keywords: ACE2 affinity; B.1.1.529; B.1.617.2; CP: Immunology; CP: Microbiology; Omicron; S1 shedding; SARS-CoV-2; neutralization sensitivity; stability; variants.