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Structural Analysis of the SARS-CoV-2 Omicron Variant Proteins 被引量:4

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摘要 The spread of the latest SARS-CoV-2 variant Omicron is particularly concerning because of the large number of mutations present in its genome and lack of knowledge about how these mutations would affect the current SARS-CoV-2 vaccines and treatments.Here,by performing phylogenetic analysis using the Omicron spike(S)protein sequence,we found that the Omicron S protein presented the longest evolutionary distance in relation to the other SARS-CoV-2 variants.We predicted the structures of S,M,and N proteins of the Omicron variant using AlphaFold2 and investigated how the mutations have affected the S protein and its parts,S1 NTD and RBD,in detail.We found many amino acids on RBD were mutated,which may influence the interactions between the RBD and ACE2,while also showing the S309 antibody could still be capable of neutralizing Omicron RBD.The Omicron S1 NTD structures display significant differences from the original strain,which could lead to reduced recognition by antibodies resulting in potential immune escape and decreased effectiveness of the existing vaccines.However,this study of the Omicron variant was mainly limited to structural predictions,and these findings should be explored and verified by subsequent experiments.This study provided basic data of the Omicron protein structures that lay the groundwork for future studies related to the SARS-CoV-2 Omicron variant.
出处 《Research》 SCIE EI CAS CSCD 2021年第1期759-762,共4页 研究(英文)
基金 supported by the Shanghai Municipal Science and Technology Commission Major Project(2017 SHZDZX01) Natural Science Foundation of China(32070679,U1804284,and 81871055) National Key R&D Program of China(2019YFA0905400,2017YFC0908105) Taishan Scholar Program of Shandong Province(tsqn201812153) Natural Science Foundation of Shandong Province(ZR2019YQ14).
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