Sequence and Functional Analysis of PPE Proteins from Mycobacterium Leprae

Abstract

Antigenic variation in an infectious organism such as a protozoan, bacterium or virus alters its surface proteins in order to evade a host immune response. The consequences of this variation results in a heterogenic pathogenic population, in which individual cells either express the phase-variable protein(s) or express one of multiple antigenic forms of the protein, respectively [1]. This form of regulation has been identified for a wide variety of surface structures in animal pathogens and is implicated as a virulence strategy in diseases caused by mycobacterial genus. Antigenic variation in mycobacterial proteins have been identified due to the expression of PE/PPE proteins [2], which are unique to bacterial species and are absent in higher eukaryotes such as mouse and human genomes. Hence, inhibiting these proteins using suitable inhibitors may prevent this antigenic variation, which facilitates the bacterial recognition by the host immune system. An in-depth sequence analysis of PE/PPE proteins in Mycobacterium Leprae is presented in this paper for understanding its function and the paper concludes with design of inhibitors used to target these proteins using computational drug design approach