Centre for Algal Biotechnology, Mangosuthu University of Technology, P.O. Box 12363, Durban 4026, South Africa.
Bioinformatics Facility, Department of Botany, University of North Bengal, Siliguri 734013, India.
Molecules. 2021 Aug 24;26(17):5114. doi: 10.3390/molecules26175114.
The emergence of COVID-19 continues to pose severe threats to global public health. The pandemic has infected over 171 million people and claimed more than 3.5 million lives to date. We investigated the binding potential of antiviral cyanobacterial proteins including cyanovirin-N, scytovirin and phycocyanin with fundamental proteins involved in attachment and replication of SARS-CoV-2. Cyanovirin-N displayed the highest binding energy scores (-16.8 ± 0.02 kcal/mol, -12.3 ± 0.03 kcal/mol and -13.4 ± 0.02 kcal/mol, respectively) with the spike protein, the main protease (M) and the papainlike protease (PL) of SARS-CoV-2. Cyanovirin-N was observed to interact with the crucial residues involved in the attachment of the human ACE2 receptor. Analysis of the binding affinities calculated employing the molecular mechanics-Poisson-Boltzmann surface area (MM-PBSA) approach revealed that all forms of energy, except the polar solvation energy, favourably contributed to the interactions of cyanovirin-N with the viral proteins. With particular emphasis on cyanovirin-N, the current work presents evidence for the potential inhibition of SARS-CoV-2 by cyanobacterial proteins, and offers the opportunity for in vitro and in vivo experiments to deploy the cyanobacterial proteins as valuable therapeutics against COVID-19.
新冠疫情的持续蔓延，对全球公共卫生构成严重威胁。截至目前，该疫情已感染超过 1.71 亿人，并导致超过 350 万人死亡。我们研究了抗病毒蓝藻蛋白（包括 、 和藻蓝蛋白）与新冠病毒 2 型（SARS-CoV-2）附着和复制相关基本蛋白的结合潜力。 与 SARS-CoV-2 的刺突蛋白、主蛋白酶（M）和木瓜蛋白酶样蛋白酶（PL）的结合能评分最高（分别为-16.8±0.02 kcal/mol、-12.3±0.03 kcal/mol 和-13.4±0.02 kcal/mol）。 与参与人类 ACE2 受体附着的关键残基相互作用。使用分子力学-泊松-玻尔兹曼表面面积（MM-PBSA）方法计算的结合亲和力分析表明，除极性溶剂化能外，所有形式的能量都有利于 与病毒蛋白的相互作用。特别强调了 ，目前的工作为蓝藻蛋白可能抑制 SARS-CoV-2 提供了证据，并为体外和体内实验提供了机会，以将蓝藻蛋白作为治疗 COVID-19 的有价值的治疗方法。
