SARS Core (340-390)
Description
Table 1: Comparative Analysis of SARS Core (340-390) Products
Immunological Applications
This region is widely used in serological assays due to its ability to elicit strong antibody responses:
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Diagnostic Utility: Detects IgG antibodies in SARS-infected individuals with minimal cross-reactivity . Studies in Uganda reported an 87.5% seroprevalence using this antigen in ELISA .
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Cross-Reactivity: Shares homology with nucleoproteins of other human coronaviruses (e.g., HCoV-OC43, HCoV-229E), enabling broad detection .
Antigenic Performance
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Immunodominance: Bioinformatic analyses identified residues 349–399 and 405–419 as critical B-cell epitopes, overlapping with the 340–390 region .
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Surface Accessibility: Hydrophilicity and solvent accessibility enhance antibody binding .
Clinical Validation
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A 2025 study using the 340–390 antigen in Uganda demonstrated its efficacy in detecting historical SARS-CoV exposures, with higher seropositivity in children aged 1–5 years (46.97%) .
Limitations and Future Directions
Product Specs
Escherichia Coli.
SARS Core protein was purified by proprietary chromatographic technique.
SARS Core protein is Immunoreactive with sera of SARS-infected individuals.
Q&A
Here’s a structured FAQ collection for researchers studying the SARS-CoV-2 nucleocapsid core region (340-390 aa), based on academic research scenarios and methodological rigor:
Advanced Research Questions
How can researchers resolve discrepancies in binding affinity data for SARS Core (340-390) across different experimental setups?
What strategies optimize the solubility and stability of recombinant SARS Core (340-390) in in vitro assays?
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Fusion tags: Use GST or His-tags to enhance solubility during E. coli expression .
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Storage: Aliquot in 50% glycerol at -20°C to prevent freeze-thaw degradation .
How does phosphorylation of serine residues in the 340-390 region affect viral replication kinetics?
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Mass spectrometry: Identifies post-translational modification sites.
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Reverse genetics: Generates phosphorylation-defective mutants to compare viral titer in Vero E6 cells .
Data Contradiction Analysis
Conflicting reports on RNA-binding efficiency of 340-390: How to address this?
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Source of variance: Differences in protein truncation (e.g., 1-422 aa vs. 340-390 aa constructs alter RNA affinity) .
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Resolution: Use full-length N-protein controls in parallel experiments to contextualize results .
Key Structural and Functional Insights
Domain Features of 340-390 aa Region
Product Science Overview
The SARS-Associated Coronavirus (SARS-CoV) nucleocapsid (N) protein is a critical structural component of the virus. It plays a pivotal role in the viral life cycle, including RNA genome packaging, replication, and transcription. The nucleocapsid protein is highly immunogenic and has been a target for diagnostic and therapeutic interventions.
The nucleocapsid protein of SARS-CoV is composed of multiple domains, each contributing to its function. The region spanning amino acids 340-390 is part of the C-terminal domain, which is involved in RNA binding and oligomerization. This region is crucial for the formation of the ribonucleoprotein complex, which is essential for the encapsidation of the viral RNA genome .
The recombinant nucleocapsid core (340-390 a.a) is a synthesized fragment of the N protein, often used in research and diagnostic applications. This recombinant protein is produced using various expression systems, such as bacterial or mammalian cells, to ensure high yield and purity. The recombinant fragment retains the functional properties of the native protein, making it a valuable tool for studying the virus’s biology and developing diagnostic assays .
- Diagnostic Development: The recombinant nucleocapsid core is used in serological assays to detect antibodies against SARS-CoV. Its high immunogenicity makes it an ideal candidate for developing sensitive and specific diagnostic tests .
- Vaccine Research: The nucleocapsid protein is a potential target for vaccine development. Studies have shown that the N protein can elicit strong immune responses, making it a promising candidate for inclusion in vaccine formulations .
- Therapeutic Research: Understanding the structure and function of the nucleocapsid protein can aid in the development of antiviral drugs. Inhibitors targeting the N protein’s RNA-binding domain could potentially disrupt the viral life cycle .
