T.pallidum p17

The p17 protein is a fragment of the Treponema pallidum subsp. pallidum strain Nichols. It is expressed in Escherichia coli to produce recombinant forms of the protein . The recombinant p17 protein is typically purified to a high degree, often exceeding 90% purity, making it suitable for various applications such as ELISA (Enzyme-Linked Immunosorbent Assay) and Western Blotting .

Recombinant p17 protein is widely used in research and diagnostic applications. It plays a significant role in the serological diagnosis of syphilis. The protein is used to develop immunoassays that detect antibodies against Treponema pallidum in human serum. These assays are critical for accurate and reliable diagnosis of syphilis, especially in cases where clinical symptoms are ambiguous .

Studies have shown that recombinant Treponema pallidum proteins, including p17, exhibit high diagnostic accuracy. For instance, the sensitivity and specificity of p17 in serological tests are quite high, making it a reliable marker for syphilis diagnosis . The protein’s performance in diagnostic tests is often evaluated using Receiver Operating Characteristic (ROC) curves, which help in determining the diagnostic potential of the protein .

The production of recombinant p17 protein involves cloning the gene encoding the mature lipoprotein of Treponema pallidum into an expression vector, which is then introduced into Escherichia coli. The bacteria express the protein, which is subsequently purified using various chromatographic techniques to achieve the desired purity .