Recombinant African swine fever virus Major structural protein p17 (Ba71V-107) has been produced through an in vitro E. coli expression system, spanning the complete protein sequence from amino acids 1 to 117. The product carries an N-terminal 10xHis tag, which streamlines both purification and detection processes. SDS-PAGE analysis confirms that the protein achieves purity levels above 85%, making it well-suited for diverse research applications.
The Major structural protein p17 appears to be a crucial component of the African swine fever virus, likely playing an important role in maintaining structural integrity and coordinating assembly. Understanding how p17 functions and interacts with other components may be vital for unraveling the viral assembly pathway and developing antiviral strategies. Research into this protein seems essential for virology studies, particularly when investigating viral replication and pathogenesis mechanisms.
Potential Applications
Note: The applications listed below are based on what we know about this protein's biological functions, published research, and experience from experts in the field. However, we haven't fully tested all of these applications ourselves yet. We'd recommend running some preliminary tests first to make sure they work for your specific research goals.
African swine fever virus p17 is a major structural protein that requires precise folding, proper oligomerization, and specific protein-protein interactions for its role in viral capsid assembly. The in vitro E. coli expression system (cell-free) provides a controlled environment but cannot ensure proper eukaryotic folding patterns or the complex oligomerization required for this viral structural protein. While cell-free systems can produce soluble proteins, the probability of correct folding with functional capsid assembly activity requires experimental validation. The N-terminal 10xHis-tag may potentially interfere with the protein's oligomerization interfaces or functional domains.
1. Antibody Development and Validation Studies
This application is highly suitable as antibody development primarily relies on linear epitope recognition rather than functional protein folding. The full-length protein (1-117aa) provides comprehensive epitope coverage for generating antibodies against p17. The high purity (>85%) ensures minimal contamination-related issues during immunization protocols.
2. Protein-Protein Interaction Studies
This application carries a significant risk without proper folding validation. p17 interactions with other viral structural proteins require precise tertiary structure and proper oligomerization. If correctly folded and active (verified), the protein may be suitable for interaction studies. If misfolded/unverified, there is a high risk of non-specific binding or failure to identify genuine physiological interactions important for viral assembly.
3. Structural and Biochemical Characterization
These studies are essential priority applications for determining folding status. Techniques should include size-exclusion chromatography to assess oligomeric state, circular dichroism spectroscopy to evaluate secondary structure, and thermal shift assays to determine stability. These analyses provide critical quality control data for this protein itself, not the native p17.
4. Immunoassay Development and Optimization
This application is well-suited as immunoassays depend on epitope recognition rather than functional conformation. The protein can serve as a reliable standard for quantitative assay development, and the His-tag provides flexible detection options for assay optimization.
5. Viral Assembly and Morphogenesis Studies
This application carries a high risk without functional validation. Viral capsid assembly requires precise oligomerization and protein-protein interactions that depend on native conformation. If incorrectly folded, the protein will not exhibit proper self-assembly characteristics, making morphogenesis studies biologically misleading.
Final Recommendation & Action Plan
The in vitro E. coli expression system provides a controlled production environment for this viral structural protein, but the folding status and functional competence require experimental validation before meaningful biological applications. Begin with Application 3 (Structural Characterization) to assess folding quality through SEC (oligomerization state), CD spectroscopy, and validate self-assembly capability if possible. Applications 1 and 4 (antibody development and immunoassay) can proceed immediately. For Applications 2 and 5 (interaction studies and assembly research), first confirm proper folding and oligomerization through biophysical characterization. Always include appropriate controls and consider using eukaryotic expression systems for critical functional studies requiring authentic viral protein behavior.
