Recombinant Human respiratory syncytial virus A Fusion glycoprotein F0 is produced in E. coli and contains the extracellular domain from amino acids 27 to 529. The protein carries an N-terminal 6xHis-tag, which helps with purification and detection. SDS-PAGE analysis shows purity levels greater than 85%, making it appropriate for various research applications. Low endotoxin levels are maintained in the final product, which appears important for sensitive experimental work.
The Fusion glycoprotein F0 of Human respiratory syncytial virus A seems to play a central role in how the virus infects cells by mediating membrane fusion and viral entry into host cells. This protein has become a key target for research into viral pathogenesis and vaccine development, since it likely initiates the infection process. Understanding how this protein works may be critical for developing therapeutic interventions and grasping the mechanisms behind viral entry.
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.
1. Antibody Development and Characterization Studies
This recombinant RSV F0 protein extracellular domain can work as an immunogen for creating monoclonal or polyclonal antibodies against RSV fusion protein. The N-terminal 6xHis tag makes purification and immobilization easier for antibody screening assays. Researchers might find this protein useful in ELISA-based screening to identify high-affinity antibodies from hybridoma supernatants or phage display libraries. Since the extracellular domain represents the native antigenic surface exposed during viral infection, it appears well-suited for developing research-grade antibodies for RSV studies.
2. Protein-Protein Interaction Studies
The 6xHis-tagged RSV F0 protein could be valuable in pull-down assays to identify cellular proteins that interact with the viral fusion protein during infection. The histidine tag allows for efficient immobilization on nickel-based resins, which helps capture potential binding partners from cell lysates. This approach may help researchers map the molecular interactions between RSV fusion protein and host cell surface receptors or intracellular proteins. Studies like these contribute to our understanding of how RSV enters cells and causes disease.
3. Structural and Biophysical Characterization
This recombinant protein provides material for structural biology studies, including X-ray crystallography, NMR spectroscopy, or cryo-electron microscopy analysis of the RSV F0 extracellular domain. The expressed region (27-529aa) covers the major antigenic and functional domains of the fusion protein. Researchers can examine conformational changes, protein folding, and domain organization through techniques such as circular dichroism spectroscopy or dynamic light scattering. The purified protein also makes possible thermal stability studies and binding kinetics analysis through surface plasmon resonance.
4. Vaccine Antigen Research and Immunogenicity Studies
The recombinant F0 extracellular domain might be evaluated as a potential vaccine antigen in preclinical animal studies to assess immunogenicity and immune response profiles. Researchers could formulate this protein with various adjuvants to study antibody responses, T-cell activation, and protective immunity in mouse or other animal models. The protein may also prove useful for developing virus-like particles or other vaccine delivery platforms for RSV research. Comparative immunogenicity studies between different RSV strains or protein variants could be conducted using this standardized antigen preparation.
