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Omicron SARS-CoV-2 variant: Unique features and their impact on pre-existing antibodies.
Kannan, Saathvik R; Spratt, Austin N; Sharma, Kalicharan; Chand, Hitendra S; Byrareddy, Siddappa N; Singh, Kamal.
  • Kannan SR; Bond Life Sciences Center, University of Missouri, Columbia, MO, USA.
  • Spratt AN; Bond Life Sciences Center, University of Missouri, Columbia, MO, USA.
  • Sharma K; Delhi Pharmaceutical Sciences and Research University, New Delhi, India.
  • Chand HS; Department of Immunology and Nano-Medicine, Herbert Wertheim College of Medicine, Florida International University, Miami, FL, 33199, USA.
  • Byrareddy SN; Department of Pharmacology and Experimental Neuroscience, University of Nebraska Medical Center, Omaha, NE, USA; Department of Genetics, Cell Biology and Anatomy, University of Nebraska Medical Center, Omaha, NE, USA; Department of Biochemistry and Molecular Biology, University of Nebraska Medical C
  • Singh K; Bond Life Sciences Center, University of Missouri, Columbia, MO, USA; Delhi Pharmaceutical Sciences and Research University, New Delhi, India; Division of Clinical Microbiology, Department of Laboratory Medicine, Karolinska Institute, Stockholm, Sweden; Department of Veterinary Pathobiology, Univers
J Autoimmun ; 126: 102779, 2022 01.
Article in English | MEDLINE | ID: covidwho-1561067
ABSTRACT
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. Twenty-three 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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Full text: Available Collection: International databases Database: MEDLINE Main subject: SARS-CoV-2 / COVID-19 / Antibodies, Viral Type of study: Experimental Studies / Observational study / Randomized controlled trials Topics: Variants Limits: Humans Language: English Journal: J Autoimmun Journal subject: Allergy and Immunology Year: 2022 Document Type: Article Affiliation country: J.jaut.2021.102779

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Full text: Available Collection: International databases Database: MEDLINE Main subject: SARS-CoV-2 / COVID-19 / Antibodies, Viral Type of study: Experimental Studies / Observational study / Randomized controlled trials Topics: Variants Limits: Humans Language: English Journal: J Autoimmun Journal subject: Allergy and Immunology Year: 2022 Document Type: Article Affiliation country: J.jaut.2021.102779