M.Pneumoniae P116
Greater than 95% as determined by 10% PAGE (Coomassie staining).
Description
The Recombinant Mycoplasma Pneumoniae P116 was expressed in E. coli having an Mw of 116 kDa. P116 is fused to a His-Tag.
Product Specs
The recombinant fusion protein was purified by GSH affinity chromatography technique.
Product Science Overview
Mycoplasma pneumoniae is a significant human pathogen responsible for respiratory tract infections, particularly atypical pneumonia. This bacterium belongs to the class Mollicutes, characterized by the absence of a cell wall, which makes it inherently resistant to β-lactam antibiotics. M. pneumoniae primarily affects children and young adults, causing symptoms that range from mild respiratory distress to severe pneumonia .
The P116 protein is one of the major surface adhesins of Mycoplasma pneumoniae. It plays a crucial role in the bacterium’s ability to adhere to the respiratory epithelium, facilitating colonization and infection. The P116 protein, along with other adhesins like P1 and P30, forms part of the tip-like attachment organelle that is essential for the pathogen’s virulence .
Recombinant P116 protein is a laboratory-produced version of the natural P116 protein. It is created using recombinant DNA technology, which involves inserting the gene encoding the P116 protein into a suitable expression system, such as bacteria or yeast, to produce the protein in large quantities. This recombinant protein is then purified for use in various applications, including research and diagnostics .
The recombinant P116 protein has shown promise in the serodiagnosis of Mycoplasma pneumoniae infections. Serological tests, such as enzyme-linked immunosorbent assays (ELISA), utilize recombinant P116 to detect specific antibodies in patient serum samples. These tests are valuable for diagnosing acute M. pneumoniae infections, as they can distinguish between current and past infections and reduce the risk of cross-reactivity with other pathogens .
Research on the P116 protein has provided insights into its structure and function. Studies have shown that the N-terminal fragment of P116 is particularly useful for serodiagnosis. Additionally, the recombinant P116 protein has been used to study the immune response to M. pneumoniae, helping to identify potential targets for vaccine development.
