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Description

SARS-CoV-2 Nucleoprotein (UniProt: P0DTC9, also known as N, Nucleocapsid protein, NC, Protein N) is encoded by the N gene (Gene ID: 43740575) in SARS-CoV-2 virus. The SARS-CoV-2 is a positive-strand RNA virus that causes severe respiratory syndrome in human. The mature SARS-CoV-2 contains 4 structural proteins: Envelope (E), Membrane (M), Nucleocapsid (N), and the Spike protein (S). E and M proteins help in viral assembly and N protein is needed for RNA synthesis. The S protein is a single-pass type I, homotrimeric, membrane glycoprotein that is responsible for virus binding and entry into host cell. The N protein packages the positive strand viral genome RNA into a helical ribonucleocapsid (RNP) and plays a fundamental role during virion assembly through its interactions with the viral genome and membrane protein M. It plays an important role in enhancing the efficiency of subgenomic viral RNA transcription as well as viral replication. The RNA binding region of SARS-CoV-2 is localized to amino acids 41-186 and its dimerization domain is in amino acids 258-361. Lack of cysteine is one of the common features in nucleoprotein from different coronaviruses. The complete N protein of SARS-CoV and COV-2 is a highly basic with positive net charges and high pI (10.11). Its N-terminal region is more basic with positive charge, while the C-terminal region is acidic with negative charge. The middle region of nucleoprotein displays relatively higher hydrophobicity and the two termini display greater hydrophilicity. Nucleoprotein can undergo phosphorylation at multiple serines and threonines and some of these phosphorylation events are essential for RNA binding, oligomerization and localization to nucleoli. Phosphorylation is also required for recruitment of host RNA helicase DDX1 (DEAD-Box Helicase 1) that facilitates template readthrough and enables longer subgenomic mRNA synthesis. Clone 6H3-G1 shows reactivity with both SARS-CoV-2 and SARS-CoV-1.