Abstract
The Omicron variant of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), bearing an unusually high number of mutations, has become a dominant strain in many countries within several weeks. We report here structural, functional, and antigenic properties of its full-length spike (S) protein with a native sequence in comparison with those of previously prevalent variants. Omicron S requires a substantially higher level of host receptor ACE2 for efficient membrane fusion than other variants, possibly explaining its unexpected cellular tropism. Mutations not only remodel the antigenic structure of the N-terminal domain of the S protein but also alter the surface of the receptor-binding domain in a way not seen in other variants, consistent with its remarkable resistance to neutralizing antibodies. These results suggest that Omicron S has acquired an extraordinary ability to evade host immunity by excessive mutations, which also compromise its fusogenic capability.
Keywords: CP: Molecular biology; SARS-CoV-2; cryo-EM; spike protein; structure.
【저자키워드】 SARS-CoV-2, Spike protein, cryo-EM, structure., CP: Molecular biology, 【초록키워드】 ACE2, coronavirus, Molecular biology, S protein, Neutralizing antibodies, mutations, variant, severe acute respiratory syndrome Coronavirus, omicron, variants, Spike protein, Protein, Receptor-binding domain, Omicron variant, cryo-EM, membrane fusion, N-terminal domain, not seen, acute respiratory syndrome, antigenic structure, acute respiratory syndrome coronavirus, acute respiratory syndrome coronavirus 2, host receptor, other variants, host immunity, antigenic, sequence, full-length, cryo, dominant, cellular tropism, Alter, country, prevalent, functional, the receptor-binding domain, evade, the S protein, 【제목키워드】 spike mutation, functional,