creators_name: Kumar, Ajay 
creators_name: Boradia, Vishant Mahendra
creators_name: Mahajan, Apurwa
creators_name: Kumaran , S 
creators_name: Raje , Maonj
creators_name: Raje, Chaaya Iyengar
type: article
datestamp: 2024-07-16 05:39:48
lastmod: 2024-07-16 05:39:48
metadata_visibility: show
title: Mycobacterium tuberculosis H37Rv enolase (Rv1023)- expression, characterization and effect of host dependent modifications on protein functionality 
ispublished: pub
subjects: QR
keywords: Biofilm; Enolase; Enzyme activity; Mycobacterium tuberculosis; Protein expression; Protein multifunctionality
note: The copyright of this article belongs to Elsevier Science
abstract: Mycobacterium tuberculosis enolase is an essential glycolytic enzyme that catalyzes the conversion of 2, phosphoglycerate (PGA) to phosphoenol pyruvate (PEP). It is also a crucial link between glycolysis and the tricarboxylic acid (TCA) pathway. The depletion of PEP has recently been associated with the emergence of non-replicating drug resistant bacteria. Enolase is also known to exhibit multiple alternate functions, such as promoting tissue invasion via its role as a plasminogen (Plg) receptor. In addition, proteomic studies have identified the presence of enolase in the Mtb degradosome and in biofilms. However, the precise role in these processes has not been elaborated. The enzyme was recently identified as a target for 2-amino thiazoles - a novel class of anti-mycobacterials. In vitro assays and characterization of this enzyme were unsuccessful due to the inability to obtain functional recombinant protein. In the present study, we report the expression and characterization of enolase using Mtb H37Ra as a host strain. Our study demonstrates that the enzyme activity and alternate functions of this protein are significantly impacted by the choice of expression host (Mtb H37Ra or E. coli). Detailed analysis of the protein from each source revealed subtle differences in the post-translational modifications. Lastly, our study confirms the role of enolase in Mtb biofilm formation and describes the potential for inhibiting this process.


date: 2023-11
date_type: published
publication: Biochimie
volume: 214
publisher: Elsevier Science
pagerange: 102-113
id_number: https://doi.org/10.1016/j.biochi.2023.06.012
refereed: TRUE
issn: 0300-9084
official_url: https://sciencedirect.com/science/article/pii/S0300908423001505?via%3Dihub
citation:   Kumar, Ajay  and Boradia, Vishant Mahendra and Mahajan, Apurwa and Kumaran , S  and Raje , Maonj and Raje, Chaaya Iyengar  (2023) Mycobacterium tuberculosis H37Rv enolase (Rv1023)- expression, characterization and effect of host dependent modifications on protein functionality.  Biochimie, 214.  pp. 102-113.  ISSN 0300-9084