4.7 Article

Omicron SARS-CoV-2 variant: Unique features and their impact on pre-existing antibodies

期刊

JOURNAL OF AUTOIMMUNITY
卷 126, 期 -, 页码 -

出版社

ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jaut.2021.102779

关键词

B; 1; 1; 529; Omicron variant; SARS-CoV-2; COVID-19; Variants

资金

  1. National Institute of Allergy and Infectious Diseases [R01 AI129745, R01 AI113883, DA052845, R37 AI076119, 3R21AI144374-02S1]
  2. National Strategic Research Institute (NSRI) at the University of Nebraska
  3. Bond Life Sciences Center (Early Concept grant)

向作者/读者索取更多资源

The Omicron variant of concern (VOC) has a large number of mutations, with 46 high prevalence mutations, which may affect the binding affinities of antibodies to the S protein.
Severe Acute Respiratory Coronavirus (SARS-CoV-2) has been emerging in the form of different variants since its first emergence in early December 2019. A new Variant of Concern (VOC) named the Omicron variant (B.1.1.529) was reported recently. This variant has a large number of mutations in the S protein. To date, there exists a limited information on the Omicron variant. Here we present the analyses of mutation distribution, the evolutionary relationship of Omicron with previous variants, and probable structural impact of mutations on antibody binding. Our analyses show the presence of 46 high prevalence mutations specific to Omicron. Twentythree of these are localized within the spike (S) protein and the rest localized to the other 3 structural proteins of the virus, the envelope (E), membrane (M), and nucleocapsid (N). Phylogenetic analysis showed that the Omicron is closely related to the Gamma (P.1) variant. The structural analyses showed that several mutations are localized to the region of the S protein that is the major target of antibodies, suggesting that the mutations in the Omicron variant may affect the binding affinities of antibodies to the S protein.

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