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Effect of deletion of htpG on global proteomic profile of M. tuberculosis H37Rv

ABSTRACT: The main objective of this study is to understand the effect of deletion of htpG on protein expression profile of M. tuberculosis H37Rv. Whole cell lysates were prepared from 4 biological replicates of the wild-type control and the ∆htpG knockout strains by bead beating in 1X PBS containing protease inhibitors and subjected to 8-plex iTRAQ.

INSTRUMENT(S): TripleTOF 5600

ORGANISM(S): Mycobacterium Tuberculosis H37rv

SUBMITTER: Nisheeth Agarwal

LAB HEAD: Nisheeth Agarwal

PROVIDER: PXD039393 | Pride | 2023-07-20

REPOSITORIES: Pride

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Publications

HtpG Is a Metal-Dependent Chaperone Which Assists the DnaK/DnaJ/GrpE Chaperone System of Mycobacterium tuberculosis via Direct Association with DnaJ2.

Mangla Nikita N Singh Ramandeep R Agarwal Nisheeth N

Microbiology spectrum 20230406 3

Protein folding is a crucial process in maintaining protein homeostasis, also known as proteostasis, in the cell. The requirement for the assistance of molecular chaperones in the appropriate folding of several proteins has already called into question the previously held view of spontaneous protein folding. These chaperones are highly ubiquitous cellular proteins, which not only help in mediating the proper folding of other nascent polypeptides but are also involved in refolding of the misfolde ...[more]

PMID: 37022172

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2017-11-03 | PXD007146 | Pride

M. tuberculosis H37Rv: mutant expressing foreign peptide SL3 Vs control H37Rv

Project description:Transcriptional profiling of M.tb H37Rv cells comparing control wild type H37Rv with H37Rv cells electroporated with constitutive expression plasmid pVV16 expressing ESAT-6 binding peptide SL3. The expression of SL3 makes H37Rv less virulent during ex vivo and BalB/c mice infections, sequesters ESAT-6 inside M.tb cells and cause severe defects in mycobacterial morphology. Goal was to determine the effects of SL3 expression on global H37Rv gene expression. Two color Experiment,Organism: Mycobacterium Tuberculosis, ilife Discoveries designed Custom Mycobacterium tuberculosis on 8x15k GE Microarray. Two-condition experiment, H37Rv vs. H37Rv/SL3. Biological replicates: 2 biological control H37RV replicates labelled with Cy3, 2 SL3 biological expressing replicates labelled with Cy5.

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Proteomic profiling of MDC1A muscle using TMT quantitation, Bruno Oliveira

Project description:SUMMARY Congenital muscular dystrophy with laminin á2 chain-deficiency (MDC1A) is one of the most severe forms of muscular disease and is characterized by decreased muscle tone at birth, reduced movements and contractures. The genetic basis of MDC1A is well-known, yet the secondary mechanisms ultimately leading to muscle degeneration and subsequent connective tissue infiltration are not fully understood. In order to obtain new insights into the molecular mechanisms underlying MDC1A, we performed a comparative proteomic analysis of affected muscles (diaphragm and gastrocnemius) from laminin á2 chain-deficient dy3K/dy3K mice, using the multidimensional protein identification technology combined with tandem mass tags. Out of the around 700 identified proteins, 113 and 101 proteins, respectively, were differentially expressed in the diseased gastrocnemius and diaphragm muscles compared to normal muscles. A large portion of these proteins are involved in different metabolic processes, bind calcium or are expressed in the extracellular matrix. Our findings suggest that metabolic alterations and calcium dysregulation could be novel mechanisms that underlie MDC1A and might be targets that should be explored for therapy. Also, detailed knowledge of the composition of fibrotic tissue, rich in extracellular matrix proteins, in laminin á2 chain-deficient muscle may help to design future anti-fibrotic treatment.

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