title: 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.
authors.affiliation: CSIR-Institute of Genomics and Integrative Biology, Council of Scientific and Industrial Research, Mall Road, Delhi, 110007, India.
authors.lastname: Monu
authors.affiliation: CSIR-Institute of Genomics and Integrative Biology, Council of Scientific and Industrial Research, Mall Road, Delhi, 110007, India. meena@igib.res.in.
authors.forename: Laxman S
authors.initials: LS
authors.lastname: Meena
mesh_terms: D000595:Amino Acid Sequence; D002087:Butyrates / Q000378:metabolism; D002265:Carboxylic Ester Hydrolases / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism / Q000627:therapeutic use; D005670:Fusarium / Q000201:enzymology / Q000235:genetics*; D006801:Humans; D006868:Hydrolysis; D008066:Lipolysis; D008563:Membrane Lipids / Q000737:chemistry / Q000378:metabolism; D009169:Mycobacterium tuberculosis / Q000201:enzymology* / Q000235:genetics / Q000472:pathogenicity; D017386:Sequence Homology, Amino Acid; D014304:Triolein / Q000737:chemistry* / Q000378:metabolism; D014376:Tuberculosis / Q000201:enzymology / Q000235:genetics* / Q000628:therapy
chemical_list: D002087:Butyrates; D008563:Membrane Lipids; D014304:Triolein; C033592:4-nitrophenyl butyrate; C000521:cutin; D002265:Carboxylic Ester Hydrolases; C019952:cutinase
keywords: Cutinase-like protein; Lipid droplets; M. tuberculosis; Macrophages; Triolein