Structural Analysis of the SARS-CoV-2 Omicron Variant Proteins

Bibliographic Details
Title: Structural Analysis of the SARS-CoV-2 Omicron Variant Proteins
Authors: Qiangzhen Yang, Ali Alamdar Shah Syed, Aamir Fahira, Yongyong Shi
Source: Research, Vol 2021 (2021)
Publisher Information: American Association for the Advancement of Science (AAAS), 2021.
Publication Year: 2021
Collection: LCC:Science
Subject Terms: Science
More Details: 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.
Document Type: article
File Description: electronic resource
Language: English
ISSN: 2639-5274
Relation: https://doaj.org/toc/2639-5274
DOI: 10.34133/2021/9769586
Access URL: https://doaj.org/article/632442a8c4b14837906744d505910f78
Accession Number: edsdoj.632442a8c4b14837906744d505910f78
Database: Directory of Open Access Journals
More Details
ISSN:26395274
DOI:10.34133/2021/9769586
Published in:Research
Language:English