CoV-2 N (201-419)
Description
Viral RNA Packaging
The CTD dimer binds RNA nonspecifically via a positively charged surface . Mutations in the linker region (e.g., P199L, S202R) reduce phosphorylation and enhance particle assembly efficiency by ~10-fold compared to ancestral strains .
Host Interactions
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Phosphorylation: Residues S202 and R203 in the SR-rich linker are phosphorylated, modulating RNA binding and genome replication .
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Arginine Methylation: R95 and R177 (outside 201–419) are methylated by PRMT1, affecting RNA packaging .
Evolutionary Mutations in Variants of Concern
Mutations in CoV-2 N (201-419) are linked to enhanced viral fitness:
Antibody and Drug Interactions
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Monoclonal Antibodies: nCoV396 binds N-terminal residues (Q163, L167, K169) but induces allosteric changes in the CTD, destabilizing RNA binding .
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Small-Molecule Inhibitors: PJ34 and rapamycin disrupt CTD dimerization and RNA binding, respectively .
Post-Translational Modifications (PTMs)
Research Implications
CoV-2 N (201-419) is a hotspot for therapeutic targeting due to its conserved regions across β-coronaviruses . Structural insights from cryo-EM (resolution: 1.5–1.8 Å) and mutagenesis studies provide a roadmap for designing broad-spectrum antivirals. For example, stabilizing CTD dimers with PJ34-like compounds could inhibit viral assembly, while phosphorylation mimics might suppress replication .
Product Specs
The 2019 novel coronavirus (2019-nCoV), a human-infecting coronavirus causing viral pneumonia, emerged in a Wuhan, Hubei province, China fish market in December 2019.
2019-nCoV shares 87% identity with the bat-derived severe acute respiratory syndrome coronavirus 2018 (SARS-CoV-2) found in Zhoushan, eastern China. Despite some amino acid variations, 2019-nCoV possesses a similar receptor-binding domain (RBD) structure to 2018 SARS-CoV, suggesting a potential binding capability to the human angiotensin-converting enzyme 2 (ACE2) receptor protein.
Although bats are considered a likely natural reservoir for 2019-nCoV, researchers speculate that a marine animal sold at the seafood market may have acted as an intermediate host. Reverse genetics analysis indicates 2019-nCoV could be a recombinant virus, with its spike glycoprotein originating from a combination of bat coronavirus and an unidentified coronavirus.
This recombinant protein, expressed in E. coli, encompasses the C-terminal domain of the Coronavirus 2019 nucleocapsid protein (amino acids 201-419). It is fused with a 6xHis tag at the C-terminus and has a molecular weight of 23.9 kDa.
The CoV 2019 Nucleocapsid-c-terminal domain protein solution is supplied in 1x PBS (phosphate-buffered saline).
The CoV 2019 Nucleocapsid c-terminal domain protein is shipped with ice packs to maintain a cool temperature. Upon receipt, store the protein at -20°C.
The purity of the CoV 2019 Nucleocapsid-c-terminal domain protein is greater than 90%, as determined by SDS-PAGE analysis.
Reactivity with SARS infected individuals not tested.
Product Science Overview
The Coronavirus 2019 Nucleocapsid (N) protein, specifically the segment spanning amino acids 201-419, plays a crucial role in the structure and function of the SARS-CoV-2 virus, which causes COVID-19. This recombinant protein is of significant interest for research and diagnostic purposes due to its immunogenic properties and involvement in viral replication and packaging.
The Nucleocapsid protein of SARS-CoV-2 is a highly conserved RNA-binding protein that is essential for the virus’s life cycle. It is composed of 419 amino acids and has a molecular weight of approximately 45.6 kDa . The protein is predominantly found in the nucleus and is involved in several critical functions:
- RNA Binding: The N protein binds to the viral RNA genome, forming a ribonucleoprotein complex that is crucial for the packaging of the viral genome into new virions .
- Replication and Transcription: It plays a role in the regulation of viral RNA synthesis during replication and transcription .
- Immunogenicity: The N protein is highly immunogenic, making it a valuable target for diagnostic assays and vaccine development .
The Nucleocapsid protein is known for its strong immunogenicity, which means it can elicit a robust immune response. High levels of IgG antibodies against the N protein have been detected in the sera of COVID-19 patients . This makes the N protein a promising candidate for serological tests to detect past infections and for vaccine development.
Recombinant Nucleocapsid proteins are produced using various expression systems to study their structure, function, and potential applications in diagnostics and therapeutics. The segment spanning amino acids 201-419 is particularly significant because it includes regions that are important for the protein’s immunogenicity and RNA-binding capabilities .
- Diagnostics: The recombinant N protein is used in serological assays to detect antibodies against SARS-CoV-2, helping to identify individuals who have been exposed to the virus .
- Vaccine Development: Due to its immunogenic properties, the N protein is being explored as a potential component of vaccines aimed at eliciting a protective immune response .
- Research: Studying the recombinant N protein helps researchers understand the molecular mechanisms of SARS-CoV-2 replication and pathogenesis, which can inform the development of antiviral therapies .
