The Recombinant Bovine coronavirus Spike glycoprotein (S) is produced using a mammalian cell expression system, ensuring proper folding and post-translational modifications. This protein represents a partial sequence from amino acids 314 to 634 and includes a C-terminal 6xHis-tag for simplified purification and detection. The purity level exceeds 85%, as confirmed by SDS-PAGE, which makes it suitable for various research applications.
Bovine coronavirus relies heavily on its Spike glycoprotein (S) to infect host cells. This protein mediates attachment to host cell receptors, playing what appears to be a pivotal role in viral entry and the overall viral life cycle. Research into the structure and function of this protein may be essential for understanding viral pathogenesis and developing therapeutic interventions.
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.
The protein is expressed in a mammalian cell system (e.g., CHO or HEK293 cells), which supports native-like folding and post-translational modifications (PTMs)—including glycosylation—critical for the bovine coronavirus Spike (S) protein fragment (314–634 aa). The C-terminal 6xHis tag minimally disrupts structure, and the full-length S context (though truncated here) improves solubility compared to prokaryotic systems. However, no direct evidence confirms native secondary/tertiary structure (e.g., circular dichroism for disulfide bonds, thermal shift assays for stability) or retention of functional conformations (e.g., receptor-binding domain [RBD] geometry, if present in 314–634 aa). The fragment’s biological role (e.g., receptor binding, fusion activity, or interaction with other viral NSPs) is untested—mammalian expression does not guarantee the fragment retains native functional interfaces.
1. Antibody Development and Characterization
This recombinant S fragment (314–634 aa) can serve as an immunogen for generating antibodies, and mammalian glycosylation may enhance conformational epitope recognition. However, antibody specificity must be validated against native full-length S—the fragment may present non-native epitopes, and antibodies may not cross-react with intact viral particles. The His tag simplifies ELISA screening, but results require confirmation with native protein to ensure relevance.
2. Protein-Protein Interaction Studies
Pull-down assays using the His tag can identify interactors, but results reflect fragment-specific interactions, not full-length S biology—mammalian folding improves native-like binding, but identified partners must be validated via co-IP or functional assays (e.g., replicon assays) to rule out artifacts. The fragment’s defined region supports domain-specific mapping, but broader viral mechanisms remain unaddressed.
3. Structural and Biochemical Characterization
This fragment supports domain-focused biophysical studies (e.g., CD for secondary structure, DLS for stability) and glycosylation analysis (relevant to mammalian expression). However, results cannot be extrapolated to full-length S—truncation may alter oligomerization or conformational dynamics. Limited proteolysis can probe local structure, but interpretation requires caution due to missing domains.
4. Comparative Coronavirus Research
This fragment enables cross-species comparisons (e.g., with SARS-CoV-2 or MERS-CoV S), but findings are fragment-specific—evolutionary insights require complementary full-length protein data to avoid misinterpreting truncation-driven artifacts. Glycosylation differences between species may also confound antigenic comparisons.
Final Recommendation & Action Plan
This mammalian-expressed bovine coronavirus S fragment (314–634 aa) is a strong candidate for antibody development and domain-specific studies but requires rigorous validation first, confirm folding/stability via circular dichroism/thermal shift assays; second, validate bioactivity (e.g., receptor binding, if applicable) using co-IP or cell-based assays; third, for comparative research, pair with full-length proteins to contextualize fragment results. Optimize expression (e.g., use glycoengineered cell lines) to enhance native-like glycosylation. If folding/bioactivity fails, use a viral replication system to produce native protein—this fragment’s utility depends on validating its structural and functional integrity relative to the full-length S protein.
