• TungH Y LimHYLPeptide and Protein Chemistry Research Laboratory, Nacbraht Biomedical Research Institute, 3164 21st Street Suite 122, Astoria (NYC), NY, 11106, USA. Electronic address: hyltung2010@nacbrahtbiomedresins.org. and Pierre Limtung.
• Peptide and Protein Chemistry Research Laboratory, Nacbraht Biomedical Research Institute, 3164 21st Street Suite 122, Astoria (NYC), NY, 11106, USA. Electronic address: hyltung2010@nacbrahtbiomedresins.org.
• Biochem. Biophys. Res. Commun. 2020 Oct 29; 532 (1): 134-138.

AbstractSARS-CoV-2 is the etiologic agent of COVID-19. There is currently no effective means of preventing infections by SARS-CoV-2, except through restriction of population movement and contact. An understanding of the origin, evolution and biochemistry (molecular biology) of SARS-CoV-2 is a prerequisite to its control. Mutations in the phosphorylation sites of SARS-CoV-2 encoded nucleocapsid protein isolated from various populations and locations, are described. Mutations occurred in the phosphorylation sites, all located within a stretch which forms a phosphorylation dependent interaction site, including C-TAK1 phosphorylation sites for 14-3-3. The consequences of these mutations are discussed and a structure-based model for the role of protein 14-3-3 in the sequestration and inhibition of SARS-CoV-2 nucleocapsid protein's function is presented. It is proposed that the phosphorylation of SARS-CoV-2 nucleocapsid protein and its sequestration by Protein 14-3-3 is a cellular response mechanism for the control and inhibition of the replication, transcription and packaging of the SARS-CoV-2 genome.Copyright © 2020 Elsevier Inc. All rights reserved.

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