ReviewMolecular microbiology2020
New insights into the mycobacterial PE and PPE proteins provide a framework for future research.
Review in Molecular microbiology, 2020. 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.
- 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
- Translation factors that keep the ribosome Pro-active.Microbiology and molecular biology reviews : MMBR · 2026Review
- Host-strain compatibility shapes host transcriptional responses in macrophageMicrobial genomics · 2026Article
- Multiple aspartic proteases process PE and PPE proteins on the mycobacterial surface of pathogenic mycobacteria.The Journal of biological chemistry · 2026Article
- Optimizing culture-free approaches to recover high-qualityMicrobial genomics · 2026Article
- Linear-time prediction of proteome-scale microbial protein interactions.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Complete genomes reveal a refined map of Mycobacterium tuberculosis genetic diversity across evolutionary scales.Nature communications · 2026Article
- Hybrid sequencing reveals incompleteness of the H37Rv reference genome and highlights lineage-specific genomic divergence inMicrobial genomics · 2026Article
- High-throughput characterization of Mycobacterium tuberculosis gene function across diverse conditions.PLoS biology · 2026Article
- Article
- A tiled amplicon protocol for culture-free whole-genome sequencing ofJournal of clinical microbiology · 2026Article
- Gene conversion is a key driver of diversity hotspots inbioRxiv : the preprint server for biology · 2026Article
- Sigma factor M induces an ESX-4-focused regulon inFrontiers in tuberculosis · 2026Article
- Protein-Mediated Virulence in Mycobacterium tuberculosis.Advances in experimental medicine and biology · 2026Review
- Protein Architecture and Composition in Mycobacterium tuberculosis.Advances in experimental medicine and biology · 2026Review
- Optimizing culture-free approaches to recover high qualitymedRxiv : the preprint server for health sciences · 2025Article
- PPE51 modulates membrane integrity inmBio · 2025Article
- Ongoing evolution of PE/PPE genes inmSystems · 2025Article
- ESX-5 Deletions inbioRxiv : the preprint server for biology · 2025Article
- Loss of the ESX-5 secretion locus inProceedings of the National Academy of Sciences of the United States of America · 2025Article
12 more citing papers are in PubMed but not listed here.
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1 author.
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Abstract
The PE and PPE proteins of Mycobacterium tuberculosis have been studied with great interest since their discovery. Named after the conserved proline (P) and glutamic acid (E) residues in their N-terminal domains, these proteins are postulated to perform wide-ranging roles in virulence and immune modulation. However, technical challenges in studying these proteins and their encoding genes have hampered the elucidation of molecular mechanisms and leave many open questions regarding the biological functions mediated by these proteins. Here, I review the shared and unique characteristics of PE and PPE proteins from a molecular perspective linking this information to their functions in mycobacterial virulence. I discuss how the different subgroups (PE_PGRS, PPE-PPW, PPE-SVP and PPE-MPTR) are defined and why this classification of paramount importance to understand the PE and PPE proteins as individuals and or groups. The goal of this MicroReview is to summarize and structure the existing information on this gene family into a simplified framework of thinking about PE and PPE proteins and genes. Thereby, I hope to provide helpful starting points in studying these genes and proteins for researchers with different backgrounds. This has particular implications for the design and monitoring of novel vaccine candidates and in understanding the evolution of the M. tuberculosis complex.
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