DNA vaccines have been used with great success in experimental and some clinical therapy. However, the mechanisms of activation of the immune system by these vaccines are not utterly understood yet. Hsp65 is aMycobacterium leprae chaperone whose gene has been efficiently used as experimental DNA vaccine against tuberculosis and clinical trial against tumor. Since little is know about the three-dimensional (3D) structure of hsp65 and modeling of 3D protein structure can increase the information to improve the knowledge about the mechanism action as well as the design of new DNA vaccine formulation, here we used the bioinformatics to get the design in silico of hsp65 (heat shock protein) molecule. The determination of hsp65 3D structure was obtained by homology using the software Modeller (Eswar et al., 2001). It was used two proteins as models: 1SJP, a 60- kDa chaperonin from Mycobacterium tuberculosis in the PDB, and the 1WE3, the crystal structure of the chaperonin complex Cpn60/Cpn10/(ADP)7 from Thermus thermophilus). Our results showed an interesting structure in Hsp65 that could be important in development or modulation of immune response.
Citation: Rossetti RAM, Lorenzi JCC, Giuliatti S, Silva CL, Coelho C AAM (2008) In Silico Prediction of the Tertiary Structure of M. leprae Hsp65 Protein Shows an Unusual Structure in Carboxy-terminal Region. J Comput Sci Syst Biol 1: 126-131. doi: 10.4172/jcsb.1000012