Evaluation of Aro-Tal-AST Complex Protein as a Marker for Differential Diagnosis of Mycobacterium Avium Infection

PURPOSE: Conventional diagnostic techniques for detecting Mycobacterium avium infection are far from satisfactory. As serodiagnostic tests for M. avium infection have been shown to be simple and rapid, the present study was carried out to identify and evaluate M. avium secretory protein(s) of diagnostic potential. MATERIALS AND METHODS: Initially, by differential immunoblotting, a specific protein band of 45–50 kDa was recognized. Anion exchange column chromatography was used for purification of proteins. After fractionation, blast search was carried out. Further immunoreactivity studies were done with M. avium and Mycobacterium tuberculosis infected mice sera. Clinical utilization was confirmed by conducting indirect enzyme-linked immunosorbent assay (ELISA) with serum samples from mycobacterial infected patients. RESULTS: A complex of three proteins (Aro-Tal-AST) of molecular weight ~48 kDa, shown to be Aro A homologue (Aro), transaldolase (Tal) and aspartate transaminase (AST) by blast search was separated. Immunoreactivity studies of purified complex protein with mice sera confirmed it to be specific for M. avium infection. Indirect ELISA with patient samples further confirmed it to be M. avium infection specific. CONCLUSION: Aro-Tal-AST protein is specifically recognized by patients infected with M. avium and can be used as a marker for simple and rapid ELISA based tests for differential diagnosis of M. avium infection in patients with M. avium complex (MAC).