Recombinant Human herpesvirus 2 Tegument protein VP22 (UL49) gets produced in an E. coli expression system. The construct contains a partial protein segment spanning amino acids 170 to 300. An N-terminal 6xHis-tag has been added to make purification and detection more straightforward. SDS-PAGE analysis indicates the protein achieves over 90% purity, which appears to make it suitable for various research applications.
VP22, a tegument protein found in Human herpesvirus 2, seems to play a critical role in how the virus assembles and exits cells. The protein is involved in moving viral components around inside infected cells, which likely helps with efficient viral particle assembly. VP22 may also be significant for studying how viruses cause disease and modulate immune responses. This makes it an important target for virology research.
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.
Human herpesvirus 2 VP22 is a viral tegument protein that requires specific eukaryotic post-translational modifications and proper folding for its functional role in viral assembly and host interaction. The E. coli expression system cannot provide the necessary eukaryotic folding environment or modifications. The expressed fragment (170-300aa) represents only a partial domain, which may lack the structural context needed for native folding. The 6xHis tag may further interfere with proper structure formation. Therefore, this recombinant protein is highly unlikely to be correctly folded or functionally active.
1. Antibody Development and Immunoassay Research
This recombinant VP22 fragment serves as an excellent immunogen for generating antibodies specific to this region of HSV-2 VP22. The defined sequence (170-300aa) allows for targeted antibody production against linear epitopes. The high purity and His-tag facilitate purification and screening. However, antibodies may not recognize conformational epitopes on the full-length, natively folded protein in viral contexts.
2. Biochemical Characterization and Biophysical Analysis
This is the essential first step to assess the physical properties of this specific protein preparation. Techniques like size-exclusion chromatography can determine oligomeric state, while circular dichroism can analyze secondary structure content. These studies provide critical quality control data but characterize a misfolded fragment, not the native protein.
3. Comparative Viral Protein Studies
This protein can be used for sequence-based comparisons and immunological cross-reactivity studies between HSV-1 and HSV-2 VP22 proteins. However, comparative functional studies would be invalid due to the protein's misfolded state. Structural comparisons via Western blotting or epitope mapping are feasible.
Final Recommendation & Action Plan
This recombinant VP22 fragment is primarily valuable as an antigen for antibody development and for biochemical characterization of the bacterially expressed protein itself, but it is unsuitable for functional interaction studies. The immediate priority is Application 2 (Biochemical Characterization) to understand the physical properties of this reagent. Application 1 (Antibody Development) can proceed confidently. This protein is useful for structural and immunological analyses but not for functional comparative studies requiring native protein structure. Viral protein interactions require a precise tertiary and quaternary structure that this misfolded fragment cannot provide. For functional VP22 studies, a full-length protein expressed in eukaryotic systems or a native viral protein is essential.
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