Analysis of predicted amino acid biosynthesis in Rv3344c in Mycobacterium tuberculosis H37 Rv using bioinformatics tools.

According to World Health Organization (WHO) report, Mycobacterium tuberculosis H37 Rv (M. tuberculosis) affects one-third population of the world. Emergence of effective treatment/research against this disease is need of the hour. Therefore, we present some important aspects of Rv3344c, which is a PE_PGRS protein. Evidence shows that PE_PGRS proteins show fibronectin binding activity. This protein has affinity for calcium and also shows motifs of GTP-binding protein. It also shows the presence of sites for ribose-5-phosphate binding and motifs of aspartate-beta-semialdehyde dehydrogenase, both of which are involved in amino acid biosynthesis. Thus, this protein might be targeted to block the amino acid biosynthesis in M. tuberculosis. This article takes into consideration some important aspects of Rv3344c protein as its function is still unknown. This study includes retrieval of protein sequence database, multiple sequence alignment, protein-protein interaction, epitope prediction, localization, function prediction, phosphorylation site prediction, model building and its validation, ligand-binding prediction along with mutational analysis. Hence, this study might be an important step in the development of new drugs and treatment of tuberculosis.