宿主-病毒相互作用的分子基础解释SARS-CoV-2的Omicron和Delta变体引起的相对传播和严重程度

IF 0.7 Q4 MICROBIOLOGY Journal of Pure and Applied Microbiology Pub Date : 2023-09-01 DOI:10.22207/jpam.17.3.22
Vinod Joshi, B. Shareef, B. Angel, Annette Angel, Ramesh Joshi, A. Khan, Poorna Khaneja, N. Peer, Bhawna Sharma, Neha Singh, Satinder Pal Singh, Shilpa Barthwal, Komal Tomar, Kiran Yadav
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引用次数: 0

摘要

在印度和其他受影响国家,与德尔塔病毒相比,SARS-CoV-2的欧米克隆变种传播速度更快,但临床严重程度较低。本研究旨在探讨Omicron变异体刺突蛋白的分子变化是如何增加其传播但降低疾病严重程度的。我们报道了Delta和Omicron变体的刺突蛋白与ACE-2受体的分子相互作用,以解释突变的Omicron变体氨基酸的化学和物理性质的变化如何影响病毒进入宿主细胞的内化能力。利用研究合作实验室结构生物信息学(RCSB)和蛋白质数据库(PDB)构建ACE2-Spike蛋白相互作用。观察了组粒和δ变异刺突蛋白与ACE2受体的结合亲和力。对Omicron突变体的刺突蛋白进行分析,发现与Delta菌株共存在93个氨基酸差异,其中15个氨基酸差异位于其受体结合域(RBD)。我们的研究表明,Delta变异的RBD中只含有1个疏水氨基酸,而Omicron变异的RBD中含有6个疏水氨基酸。我们报道了Omicron变体RBD中疏水氨基酸数量的增加影响其与ACE2受体的结合进入细胞。病毒内化失败增加了鼻咽区细胞外病毒粒子的浓度,导致咳嗽或打喷嚏时更快地排出感染飞沫,增加传播,但降低了感染的严重程度。报告的观察结果可能被证明具有公共卫生和治疗意义。
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Molecular Basis of Host-Virus Interactions to Explain Relative Transmission and Severity Caused by Omicron and Delta variants of SARS-CoV-2
In India and other affected countries, Omicron variant of SARS-CoV-2 has shown faster transmission but less clinical severities when compared to Delta strain. Present study was aimed to investigate how molecular changes in the spike proteins of Omicron variant has increased its transmission but reduced the disease severity. We report molecular interactions of Spike proteins of Delta and Omicron variants with ACE-2 receptor to explain how change in chemical and physical nature of mutated amino acids of Omicron variant has affected the internalization competence of virus into host cell. The Research Collaboratory Structural Bioinformatics (RCSB) and Protein Data Bank (PDB) were used to construct ACE2-Spike Protein interaction. The binding affinity of both omicron and delta variant spike proteins with human ACE2 receptor was observed. Spike protein of Omicron variants has revealed total number of 93 dissimilarities of amino acids from Delta strain,15 of which are in its Receptor Binding Domain (RBD). Our study showed that RBD of Delta variant contained only one hydrophobic amino acid whereas there were 6 hydrophobic amino acids in the RBD of Omicron variant. We report that increased number of Hydrophobic Amino Acids in RBD of Omicron variant affects its binding with ACE2 receptor to enter into the cell. The failure of internalization of virus has increased concentration of extracellular virions at nasopharyngeal region leading to faster expulsion of infective droplets during coughing or sneezing to increase transmission but has reduced the severity of infection. The reported observations could prove to be of public health and therapeutic significance.
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来源期刊
Journal of Pure and Applied Microbiology
Journal of Pure and Applied Microbiology BIOTECHNOLOGY & APPLIED MICROBIOLOGY-MICROBIOLOGY
CiteScore
2.00
自引率
0.00%
发文量
266
审稿时长
11 months
期刊介绍: Journal of Pure and Applied Microbiology (JPAM) is a peer-reviewed, open access international journal of microbiology aims to advance and disseminate research among scientists, academics, clinicians and microbiologists around the world. JPAM publishes high-quality research in all aspects of microbiology in both online and print form on quarterly basis.
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