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1879-00032192022Oct31International journal of biological macromoleculesInt J Biol MacromolOmicron (B.1.1.529) - A new heavily mutated variant: Mapped location and probable properties of its mutations with an emphasis on S-glycoprotein.980997980-99710.1016/j.ijbiomac.2022.07.254S0141-8130(22)01708-1Omicron, another SARS-CoV-2 variant, has been recorded and reported as a VoC. It has already spread across >30 countries and is a highly mutated variant. We tried to understand the role of mutations in the investigated variants by comparison with previous characterized VoC. We have mapped the mutations in Omicron S-glycoprotein's secondary and tertiary structure landscape using bioinformatics tools and statistical software and developed different models. In addition, we analyzed the effect of diverse mutations in antibody binding regions of the S-glycoprotein on the binding affinity of the investigated antibodies. This study has chosen eight significant mutations in Omicron (D614G, E484A, N501Y, Q493K, K417N, S477N, Y505H G496S), and seven of them are located in the RBD region. We also performed a comparative analysis of the ΔΔG score of these mutations to understand the stabilizing or destabilizing properties of the investigated mutations. The analysis outcome shows that D614G, Q493K, and S477N mutations are stable mutations with ΔΔG scores of 0.351 kcal/mol, 0.470 kcal/mol, and 0.628 kcal/mol, respectively, according to DynaMut estimations. While other mutations (E484A, N501Y, K417N, Y505H, G496S) showed destabilizing results. The D614G, E484A, N501Y, K417N, Y505H, and G496S mutations increased the molecular flexibility of S-glycoprotein to interact with the ACE2 receptor, increasing the variant's infectivity. Our study will contribute to research on the SARS-CoV-2 variant, Omicron, by providing information on the mutational pattern and exciting properties of these eight significant mutations, such as antibody escape and infectivity quotient (stabilizing or destabilizing; increased or decreased molecular flexibility of S-glycoprotein to interact with the human ACE2 receptor).Copyright © 2022 Elsevier B.V. All rights reserved.ChakrabortyChiranjibCDepartment of Biotechnology, School of Life Science and Biotechnology, Adamas University, Kolkata, West Bengal 700126, India. Electronic address: drchiranjib@yahoo.com.BhattacharyaManojitMDepartment of Zoology, Fakir Mohan University, Vyasa Vihar, Balasore 756020, Odisha, India.SharmaAshish RanjanARInstitute for Skeletal Aging & Orthopaedic Surgery, Hallym University-Chuncheon Sacred Heart Hospital, Chuncheon-si 24252, Gangwon-do, South Korea.MallikBidyutBDepartment of Applied Science, Galgotias College of Engineering and Technology, Knowledge Park-II, Greater Noida, Uttar Pradesh 201306, India.engJournal Article20220808
NetherlandsInt J Biol Macromol79095780141-81300GlycoproteinsEC 3.4.17.23Angiotensin-Converting Enzyme 2SARS-CoV-2 variantsIMAngiotensin-Converting Enzyme 2COVID-19geneticsGlycoproteinsHumansMutationSARS-CoV-2geneticsOmicronRBD mutationSARS-CoV-2 VoCSpike mutationnAb escapeDeclaration of competing interest The authors declare no competing interest.2022282022523202273120228126020229306020228111933202288ppublish35952818PMC935975810.1016/j.ijbiomac.2022.07.254S0141-8130(22)01708-1Chakraborty C., Bhattacharya M., Sharma A.R. Present variants of concern and variants of interest of severe acute respiratory syndrome coronavirus 2: their significant mutations in S-glycoprotein, infectivity, re-infectivity, immune escape and vaccines activity. Rev. Med. Virol. 2021;32:1–14. e2270.Chakraborty C., Sharma A.R., Bhattacharya M., Agoramoorthy G., Lee S.-S. Evolution, mode of transmission, and mutational landscape of newly emerging SARS-CoV-2 variants. 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