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Cell, 2022-02, Vol.185 (3), p.467-484.e15
2022

Details

Autor(en) / Beteiligte
Titel
SARS-CoV-2 Omicron-B.1.1.529 leads to widespread escape from neutralizing antibody responses
Ist Teil von
  • Cell, 2022-02, Vol.185 (3), p.467-484.e15
Ort / Verlag
United States: Elsevier Inc
Erscheinungsjahr
2022
Link zum Volltext
Quelle
Free E-Journal (出版社公開部分のみ)
Beschreibungen/Notizen
  • On 24th November 2021, the sequence of a new SARS-CoV-2 viral isolate Omicron-B.1.1.529 was announced, containing far more mutations in Spike (S) than previously reported variants. Neutralization titers of Omicron by sera from vaccinees and convalescent subjects infected with early pandemic Alpha, Beta, Gamma, or Delta are substantially reduced, or the sera failed to neutralize. Titers against Omicron are boosted by third vaccine doses and are high in both vaccinated individuals and those infected by Delta. Mutations in Omicron knock out or substantially reduce neutralization by most of the large panel of potent monoclonal antibodies and antibodies under commercial development. Omicron S has structural changes from earlier viruses and uses mutations that confer tight binding to ACE2 to unleash evolution driven by immune escape. This leads to a large number of mutations in the ACE2 binding site and rebalances receptor affinity to that of earlier pandemic viruses. [Display omitted] •Large reduction in Omicron neutralization titers, ameliorated by the 3rd booster vaccine•Failure of many potent mAbs to neutralize Omicron•Complex pattern of mutations balances ACE2 binding and antibody escape•Omicron RBD is structurally similar but the most antigenically distant variant A comprehensive analysis of sera from vaccinees, convalescent patients previously infected by multiple variants, and potent monoclonal antibodies from early in the COVID-19 pandemic reveals a substantial overall reduction in the ability to neutralize the SARS-CoV-2 Omicron variant, which seems to ameliorate with a third vaccine dose. Structural analyses of the Omicron RBD suggest that selective pressure balances key changes that increase affinity for ACE2 with other changes in the receptor-binding motif that disfavor ACE2 binding but facilitate immune escape.
Sprache
Englisch
Identifikatoren
ISSN: 0092-8674
eISSN: 1097-4172
DOI: 10.1016/j.cell.2021.12.046
Titel-ID: cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_8723827

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