Roles of Triolein and Lipolytic Protein in the Pathogenesis and Survival of Mycobacterium tuberculosis: a Novel Therapeutic Approach

Abstract

Discovery of novel secreted enzymes and proteins in Mycobacterium tuberculosis (M. tuberculosis) are imperative to understanding the pathogenic system for pathogenesis requires attention. Till date, the groups of these secreted enzymes are not meaningfully characterized in terms of M. tuberculosis. In this way, cutinase, a small lipolytic protein, exists in both bacteria and fungi as well which have a potential catalytic activity. During our search, we have found a few genes of M. tuberculosis demonstrating a same significant lipase action as fungi Fusarium solani cutinase contain. Genome sequencing of M. tuberculosis uncover a lot of proteins, wherein (Rv1758, Rv1984c, Rv2301, Rv3451, Rv3452, Rv3724A, Rv3724B, and Rv3802c) genes have been noted which are exhibiting a cutinase-like activity and closely homologous to that of F. solani cutinase and having the ability to hydrolyze model substrates including p-nitrophenyl butyrate (p-PNB), cutin, triacylglycerols (TAGs), and triolein (TO), yet their biological significance in pathogenesis stays subtle and uncharacterized. In a basic perspective, the measure of cutinase expressed by M. tuberculosis and part of these small lipolytic enzymes in the pathologic discipline require thorough characterization. So, through focusing on cutinase-encoding genes in M. tuberculosis and their active catalytic motif could help to build up a novel therapeutic approach.

Enzymatic Degradation of <i>p</i>-Nitrophenyl Esters, Polyethylene Terephthalate, Cutin, and Suberin by Sub1, a Suberinase Encoded by the Plant Pathogen <i>Streptomyces scabies</i>

“…While Sub1 is conserved in only a few streptomycetes, it presents high homology not only with some fungal cutinases, but also with cutinase-like enzymes from animal pathogenic mycobacteria (Komeil et al, 2013). These bacteria do not encounter cutin or suberin in their environment; however, cutinases were identified as multifunctional enzymes that act on phospholipids, polysorbates, triacylglycerols, and triolein (Schué et al, 2010;Monu and Meena, 2016). As multifunctional enzymes, cutinases have a number of applications in industry (Carvalho et al, 1998).…”

Identification of positively selected genes in Mycobacterium tuberculosis from southern Xinjiang Uygur autonomous region of China

“…It was noteworthy that the cut1 gene with five codons under positive selection was only in the MDR strains but not in DS strains. cut1 ( Rv1758 ) encodes cutinase, which shows potential catalytic activity and is associated with the function of cell wall/membrane/envelope biogenesis ( Monu and Meena, 2016 ). The association between cut1 and drug resistance has not been reported.…”