ArticleThe Journal of biological chemistry2011
Conserved Pro-Glu (PE) and Pro-Pro-Glu (PPE) protein domains target LipY lipases of pathogenic mycobacteria to the cell surface via the ESX-5 pathway.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 papers.
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Who cites it
72 citing papers in PubMed, 140 citations in OpenAlex.
- Conserved immune recognition hierarchy of mycobacterial PE/PPE proteins during infection in natural hosts.PloS one · 2012Trial
- The mycomembrane proteins PorH and ProtX are inserted at polar growth zones and linked to the cell wall.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Multiple aspartic proteases process PE and PPE proteins on the mycobacterial surface of pathogenic mycobacteria.The Journal of biological chemistry · 2026Article
- Contribution of Proteins to Membrane and Cell Wall Structures in Mycobacterium tuberculosis.Advances in experimental medicine and biology · 2026Review
- Review
- The PE/PPE family proteins ofFrontiers in immunology · 2025Review
- PE/PPE mutations in the transmission of Mycobacterium tuberculosis in China revealed by whole genome sequencing.BMC microbiology · 2024Article
- Roles of Lipolytic enzymes inFrontiers in microbiology · 2024Review
- TargetingRSC medicinal chemistry · 2023Review
- Lipid droplets: a cellular organelle vital in cancer cells.Cell death discovery · 2023Review
- Sequence and Structural Motifs Controlling the Broad Substrate Specificity of the Mycobacterial Hormone-Sensitive Lipase LipN.ACS omega · 2023Article
- The ESX-1 Substrate PPE68 Has a Key Function in ESX-1-Mediated Secretion in Mycobacterium marinum.mBio · 2022Article
- Virulence-Associated Secretion inFrontiers in immunology · 2022Review
- PE_PGRS3 ensures provision of the vital phospholipids cardiolipin and phosphatidylinositols by promoting the interaction betweenVirulence · 2021Article
- PE_PGRS proteins ofVirulence · 2020Review
- Mycobacteriosis and Infections with Non-tuberculous Mycobacteria in Aquatic Organisms: A Review.Microorganisms · 2020Review
- Species-specific secretion of ESX-5 type VII substrates is determined by the linker 2 of EccCMolecular microbiology · 2020Article
- Article
- New insights into the mycobacterial PE and PPE proteins provide a framework for future research.Molecular microbiology · 2020Review
- Type VII Secretion Substrates of Pathogenic Mycobacteria Are Processed by a Surface Protease.mBio · 2019Article
12 more citing papers are in PubMed but not listed here.
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Authors and funding
10 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The type VII secretion system ESX-5 is a major pathway for export of PE and PPE proteins in pathogenic mycobacteria. These mycobacteria-specific protein families are characterized by conserved N-terminal domains of 100 and 180 amino acids, which contain the proline-glutamic acid (PE) and proline-proline-glutamic acid (PPE) motifs after which they are named. Here we investigated secretion of the triacylglycerol lipase LipY, which in fast-growing mycobacteria contains a signal sequence, but in slow-growing species appears to have replaced the signal peptide with a PE or PPE domain. Selected LipY homologues were expressed in wild-type Mycobacterium marinum and its corresponding ESX-5 mutant, and localization of the proteins was investigated by immunoblotting and electron microscopy. Our study shows that Mycobacterium tuberculosis PE-LipY (LipY(tub)) and M. marinum PPE-LipY (LipY(mar)) are both secreted to the bacterial surface in an ESX-5-dependent fashion. After transport, the PE/PPE domains are removed by proteolytic cleavage. In contrast, Mycobacterium gilvum LipY, which has a signal sequence, is not transported to the cell surface. Furthermore, we show that LipY(tub) and LipY(mar) require their respective PE and PPE domains for ESX-5-dependent secretion. The role of the PE domain in ESX-5 secretion was confirmed in a whole cell lipase assay, in which wild-type bacteria expressing full-length LipY(tub), but not LipY(tub) lacking its PE domain, were shown to hydrolyze extracellular lipids. In conclusion, both PE and PPE domains contain a signal required for secretion of LipY by the ESX-5 system, and these domains are proteolytically removed upon translocation.
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