Purified by proprietary chromatographic technique.
Treponema pallidum is a gram-negative spirochete bacterium responsible for syphilis, a chronic and complex sexually transmitted disease. The bacterium is known for its helical structure, which allows it to move in a corkscrew motion through viscous mediums such as mucus. Treponema pallidum has a notably small genome, reflecting its adaptation to the rich environment of mammalian tissue .
One of the major immunoreactive proteins of Treponema pallidum is the lipoprotein TmpA. This protein is produced as a 46-kDa precursor and is cleaved during maturation, resulting in a 44-kDa protein in SDS-PAGE gels . TmpA is known for its immunodominant regions, specifically the amino acid sequences 23-41 and 288-325 .
Recombinant TmpA (partial) is produced using E. coli and contains the immunodominant regions of the protein. This recombinant protein is used in various diagnostic applications, including ELISA and Western Blot, to detect antibodies against Treponema pallidum in infected individuals . The recombinant protein is typically supplied in a liquid form and is highly purified, with a molecular weight of 68 kDa .
The performance of recombinant Treponema pallidum proteins, including TmpA, has been evaluated for their diagnostic potential in syphilis serodiagnosis. Studies have shown that TmpA exhibits high specificity, making it a reliable marker for detecting Treponema pallidum infections . However, the sensitivity of TmpA can vary, and it is often used in combination with other recombinant proteins such as TpN17 and TpN47 to improve diagnostic accuracy .
Recombinant TmpA is used in various immunoassays, including: