期刊
BIOLOGY-BASEL
卷 11, 期 5, 页码 -出版社
MDPI
DOI: 10.3390/biology11050797
关键词
Omicron; spike protein; receptor-binding domain; binding mechanism; computational analysis
类别
资金
- Taif University in the Kingdom of Saudi Arabia (KSA) [TURSP2020/91]
A computational study revealed that the interaction between the receptor-binding domain (RBD) of Omicron BA.2 and human angiotensin-converting enzyme 2 (hACE2) is stronger than that of Omicron BA.1, indicating potential interventions against the Omicron variant.
Simple Summary The Omicron variant has recently been divided into BA.1, BA.2, and BA.3 subvariants. In the present study, we focused on comparing the interaction between the receptor-binding domain (RBD) of BA.1 and BA.2 spike proteins with human angiotensin-converting enzyme 2 (hACE2) using a computational approach. The RBD BA.2 was modeled after the BA.1. The results from molecular docking and molecular dynamics studies showed that RBD BA.2 has a higher and more stable affinity for hACE2 compared to RBD BA.1. Concerns have been raised about the high number of mutations in the spike protein of the new emergence of the highly transmissible Omicron variant (B.1.1529 lineage) of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). This variant's extraordinary ability to evade antibodies would significantly impair the current vaccination program. This present study aimed to computationally analyze the interaction between the receptor-binding domain (RBD) in the spike protein of Omicron variants and human angiotensin-converting enzyme 2 (hACE2). The docking results indicated that Omicron BA.2 has exceptionally strong interactions with hACE2 in comparison to Omicron BA.1, Delta, and wild-type, as indicated by various parameters such as salt bridge, hydrogen bond, and non-bonded interactions. The results of the molecular dynamics simulation study corroborate these findings, indicating that Omicron BA.2 has a strong and stable interaction with hACE2. This study provides insight into the development of an effective intervention against this variant.
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