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- Title
The puzzling mutational landscape of the SARS‐2‐variant Omicron.
- Authors
Fantini, Jacques; Yahi, Nouara; Colson, Philippe; Chahinian, Henri; La Scola, Bernard; Raoult, Didier
- Abstract
The recently emerging SARS‐CoV‐2 variant omicron displays an unusual association of 30 mutations, 3 deletions, and 1 insertion. To analyze the impact of this atypic mutational landscape, we constructed a complete structure of the omicron spike protein. Compared with the delta variant, the receptor‐binding domain (RBD) of omicron has an increased electrostatic surface potential, but a decreased affinity for the ACE‐2 receptor. The N‐terminal domain (NTD) has both a decreased surface potential and a lower affinity for lipid rafts. The omicron variant is predicted to be less fusogenic and thus less pathogenic than delta, due to a geometric reorganization of the S1‐S2 cleavage site. Overall, these virological parameters suggest that omicron does not have a significant infectivity advantage over the delta variant. However, in omicron, neutralizing epitopes are greatly affected, suggesting that current vaccines will probably confer little protection against this variant. In conclusion, the puzzling mutational pattern of the omicron variant combines contradictory properties which may either decrease (virological properties) or increase (immunological escape/facilitation) the transmission of this variant in the human population. This Janus‐like phenotype may explain some conflicting reports on the initial assessment of omicron and provide new insights about the molecular mechanisms controlling its dissemination and pathogenesis worldwide. HIGHLIGHTS: The spike protein of omicron is analyzed and compared with other SARS‐CoV‐2 variantsCompared with delta, omicron has a lower capacity to fuse with human host cellsLow activity of neutralizing antibodies suggests immunological escape of omicron
- Subjects
SARS-CoV-2 Omicron variant; SARS-CoV-2 Delta variant; LIPID rafts; SURFACE potential; SARS virus
- Publication
Journal of Medical Virology, 2022, Vol 94, Issue 5, p2019
- ISSN
0146-6615
- Publication type
Article
- DOI
10.1002/jmv.27577