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Novel compounds modulating Mycobacterium marinum ESX-5 secretion display anti-mycobacterial activity in vivo

ABSTRACT: We observed through Western blot that Mycobacterium marinum secreted more highly abundant PE-PGRS proteins that are above 130 kDa when treated with compound 36 than mock-treated bacteria. We would like to explore which PE-PGRS proteins are more secreted in this condition and whether other proteins are also differentially secreted between two conditions.

INSTRUMENT(S):

ORGANISM(S): Mycobacterium Marinum Atcc Baa-535 Bacteria

DISEASE(S): Tuberculosis

SUBMITTER: Sander Piersma

LAB HEAD: Connie Jimenez

PROVIDER: PXD037981 | Pride | 2023-01-19

REPOSITORIES: Pride

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			Action	DRS
	Qe211220_OPL2014_RU_VH_medmic_compound36_A.raw	Raw
	Qe211220_OPL2014_RU_VH_medmic_compound36_A_211221083522.raw	Raw
	Qe211220_OPL2014_RU_VH_medmic_compound36_B.raw	Raw
	Qe211220_OPL2014_RU_VH_medmic_compound36_B_211221103805.raw	Raw
	Qe211220_OPL2014_RU_VH_medmic_compound36_C.raw	Raw

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Proteomics analysis of mycobacterium marinum culture filtrate

Project description:Mycobacterium marinum is a pathogenic bacterium that causes infections in both fish and humans. The PE/PPE protein family is unique to mycobacteria and has been implicated in various aspects of mycobacterial pathogenicity. Understanding the presence and potential function of these proteins in M. marinum is essential for unraveling the mechanisms underlying its virulence. In this study, we conducted a proteomics analysis to investigate the secretion and potential role of the PE/PPE protein family in the culture filtrate of M. marinum. To investigate the presence of PE/PPE proteins in the culture filtrate, we employed a proteomics approach combining Asp-N and trypsin based digestion. Cultures of M. marinum were grown under laboratory conditions, and the culture filtrate was collected and subjected to digestion and LC-MS injection. Our proteomics analysis revealed the secretion of about half PE/PPE proteins in the culture filtrate of M. marinum. Majority of these proteins are confirmed to be involved in EspG5 interaction. The identification of these proteins in the culture filtrate suggests their secretion and potential role in M. marinum. Our proteomics analysis highlights the presence of PE/PPE proteins in the culture filtrate of M. marinum, suggesting their secretion and potential involvement in the pathogenicity of this bacterium.

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EspM regulates gene expression in response to the ESX-1 system in Mycobacterium marinum

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The role of ESX-1 on infected and uninfected neutrophils in Mycobacterium marinum infection

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Characterization of ESX-1 components EccA1, EspG1 and EspH reveal pivotal role of Esp substrates in the Mycobacterium marinum infection cycle

Project description:The pathogen Mycobacterium tuberculosis employs a range of ESX-1 substrates to manipulate the host and build a successful infection. Although the importance of ESX-1 secretion in virulence is well established, the characterization of its individual components and the role of individual substrates is far from complete. Here, we describe the functional characterization of the accessory ESX-1 proteins EccA1, EspG1 and EspH, i.e. proteins that are not present in all five ESX system of mycobacteria. Proteomic analysis revealed that EspG1 is crucial for ESX-1 secretion, since all detectable ESX-1 substrates were absent from the cell surface and culture supernatant in an espG1 mutant. Deletion of eccA1 resulted in minor secretion defects, but interestingly, the severity of these secretion defects was dependent on the culture conditions. Finally, espH deletion showed a partial secretion defect, only secretion of EspE, EspF and EsxA/EsxB was blocked.

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Proteolytic-independent role of mycosins in stabilization of the ESX-1 and ESX-5 type VII secretion membrane complexes.

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