Large-scale analysis of SARS-CoV-2 envelope protein sequences reveals universally conserved residues | ||||
| Microbes and Infectious Diseases | ||||
| Article 4, Volume 3, Issue 4, November 2022, Page 780-783 PDF (286.67 K) | ||||
| Document Type: Short Reports (case reports) | ||||
| DOI: 10.21608/mid.2022.148868.1340 | ||||
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| Author | ||||
Vivek Darapaneni  
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| Department of virology and computational biochemistry, Anvek Institute of Biomolecular Research, Visakhapatnam, India | ||||
| Abstract | ||||
| Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is responsible for the ongoing COVID-19 pandemic that has devastated mankind with an unprecedented impact on both health and economic condition globally. The envelope protein of SARS-CoV-2 is a multifunctional viroporin across endoplasmic reticulum-Golgi intermediate compartment. SARS-CoV-2 envelope (E) protein plays a crucial role in the virus life cycle. The objective of the present study was to identify the residue conservation in the SARS-CoV-2 E protein. The study was based on 2,654,250 amino acid sequences for the E protein. On the whole, this study exposed residues that are universally conserved among different strains of SARS-CoV-2. These universally conserved residues might be involved in either structure stabilizing or protein-protein interactions. The conserved residues identified in the present study in conjunction with structural analysis of the E protein could form the basis for designing universal anti-SARS-CoV-2 drugs which are resistant to mutations arising in the future. | ||||
| Keywords | ||||
| SARS-CoV-2; Envelope protein; Viroporin; Conserved; COVID-19 | ||||
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