Recombinant Staphylococcus aureus Staphylococcal secretory antigen ssaA1 represents a full-length mature protein produced through yeast expression systems. The construct includes an N-terminal 6xHis-tag, which appears to simplify both purification and detection processes. This particular protein variant covers amino acids 27 to 255 and demonstrates purity levels exceeding 90% when analyzed by SDS-PAGE—characteristics that likely make it appropriate for research requiring high-quality protein preparations.
The biological significance of Staphylococcal secretory antigen ssaA1 in S. aureus remains an area of active investigation. This bacterium has earned considerable attention due to its complex relationship with human health and disease. Within the bacterial secretory machinery, ssaA1 may contribute to processes affecting bacterial virulence and immune system recognition, though the precise mechanisms are still being unraveled. These properties suggest it could serve as a useful model for examining microbial pathogenesis and the intricate dynamics between pathogens and their hosts.
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.
Based on the provided information, the folding state and bioactivity of this recombinant ssaA1 protein are unknown and cannot be assumed. While the protein is expressed as the full-length mature sequence (27-255aa) in a yeast system (which can provide eukaryotic folding machinery), SsaA1 is a bacterial protein that may require specific bacterial chaperones or modifications for correct folding. The presence of an N-terminal 6xHis tag could potentially interfere with the protein's structure or function. The >90% purity indicates minimal contaminants but does not confirm correct tertiary structure or biological activity. Therefore, applications that depend on specific biological interactions or native conformation are speculative without experimental validation.
1. Antibody Development and Immunological Studies
This recombinant ssaA1 is suitable as an immunogen for generating antibodies. The His-tag facilitates purification and immobilization for screening. Antibodies generated will be against this recombinant form. Their ability to recognize the native ssaA1 protein produced by S. aureus in its natural context must be empirically validated. The recombinant ssaA1 protein is reliable for developing detection tools, but antibody functionality (e.g., neutralization) requires confirmation.
2. Protein-Protein Interaction Studies
The His-tagged recombinant ssaA1 protein can be used in pull-down assays. However, the utility for identifying biological interaction partners is entirely contingent on correct folding. If the protein is misfolded, it will not present native binding surfaces, leading to potential false negatives or identification of non-specific interactors. Results from such studies must be interpreted as preliminary and require confirmation with native protein or functional assays.
3. ELISA-Based Binding Assays
The recombinant ssaA1 protein can be used in ELISA development. However, its application for studying interactions with "host cell receptors or other bacterial components" is not valid without confirmed bioactivity. The assay is primarily suitable for detecting antibodies against the immunogen itself or for quality control of the recombinant ssaA1 protein. Binding studies with physiological partners should not be attempted without prior validation of the protein's native structure.
4. Biochemical Characterization Studies
This recombinant ssaA1 protein is well-suited for biochemical characterization of its physical properties, including oligomerization state and stability. This application is valid as it focuses on intrinsic biophysical properties. The note about potential differences from the native bacterial environment is appropriate and important for context.
Final Recommendation & Action Plan
The immediate priority is to validate the protein's folding and bioactivity before investing in functional studies. For ssaA1, this could involve testing its known functions (if any are established in literature) or using circular dichroism to assess secondary structure. Antibody development (Application 1) and biochemical characterization (Application 4) can proceed with the understanding that results characterize the recombinant protein itself. Protein interaction studies (Application 2) and functional binding assays (Application 3) should be considered exploratory until activity is confirmed, with any findings requiring validation through complementary methods using native bacterial proteins or functional assays.
