Proteomics

Dataset Information

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Proteomic study of the effect of Callyaerin B derivativs on M. tuberculosis H37Rv

ABSTRACT: The natural cyclopeptide Callyaerin B (CalB) exhibits highly specific antitubercular activity. The aim of this project is to study the proteome dysregulation induced by CalB treatment of M. tuberculosis H37Rv wild type cells using a whole proteome comparison approach. In addition, it has been shown, that the susceptibility of M. tuberculosis H37Rv to CalB is highly dependent on the expression of the putative membrane protein Rv2113. A gene deletion mutation of this protein (Δrv2113) was used to identify unspecific changes in the proteome upon CalB treatment. For this purpose, M. tuberculosis H37Rv wild type or Δrv2113 cells were treated with 31.3 µM CalB (equivalent to a 10-fold MIC90 concentration) at 37 °C for 48 hours and the proteome was compared to a corresponding solvent control (0.31% DMSO)(ACE_0685). As an additional control, the proteosomal changes after treatment of M. tuberculosis H37Rv wild type cells with a modified CalB-derivative CalB_R3β-hIle were studied in a similar setup (ACE_0641).

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Mycobacterium Tuberculosis H37rv

SUBMITTER: Farnusch Kaschani  

LAB HEAD: Farnusch Kaschani

PROVIDER: PXD050763 | Pride | 2024-07-25

REPOSITORIES: Pride

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ACE_0641_DP01.raw Raw
ACE_0641_DP02-02.raw Raw
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ACE_0641_DP04.raw Raw
ACE_0641_DP05.raw Raw
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Publications

Spread of antimicrobial resistances urges a need for new drugs against Mycobacterium tuberculosis (Mtb) with mechanisms differing from current antibiotics. Previously, callyaerins were identified as promising anti-tubercular agents, representing a class of hydrophobic cyclopeptides with an unusual (Z)-2,3-di-aminoacrylamide unit. Here, we investigated the molecular mechanisms underlying their antimycobacterial properties. Structure-activity relationship studies enabled the identification of stru  ...[more]

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