ArticleFEBS open bio2020
Disorder-to-order transition in PE-PPE proteins of Mycobacterium tuberculosis augments the pro-pathogen immune response.
Article in FEBS open bio, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 31 citations in OpenAlex.
- An in silico approach for screening non-synonymous SNPs in Mycobacterium tuberculosis PPE68 protein and impact on structure.Scientific reports · 2025Article
- Analyzing the distribution of virulence factors ofVirulence · 2025Article
- Mycobacterium tuberculosis uses intrinsically disordered, fast evolving proteins to interact with conserved host factors.Genome biology · 2025Article
- Evolution of the PE_PGRS Proteins of Mycobacteria: Are All Equal or Are Some More Equal than Others?Biology · 2025Review
- Deciphering the functional roles of PE18 and PPE26 proteins in modulatingFrontiers in immunology · 2025Article
- C-terminal region of Rv1039c (PPE15) protein of Mycobacterium tuberculosis targets host mitochondria to induce macrophage apoptosis.Apoptosis : an international journal on programmed cell death · 2024Article
- Expression of a uniqueFrontiers in microbiology · 2024Article
- Pangenome Reconstruction ofMicroorganisms · 2023Article
- Article
- The exploitation of host autophagy and ubiquitin machinery byAutophagy · 2023Review
- Immunological effects of the PE/PPE family proteins ofFrontiers in immunology · 2023Review
- Immunogenicity of PE18, PE31, and PPE26 proteins fromFrontiers in immunology · 2023Article
- TheInternational journal of molecular sciences · 2022Review
- PGRS Domain of Rv0297 ofInternational journal of molecular sciences · 2021Article
- Article
- Article
- Comparative Genomics ofFrontiers in veterinary science · 2021Article
- The unfoldase ClpC1 ofThe Journal of biological chemistry · 2020Article
- PGRS Domain of Rv0297 ofFrontiers in cellular and infection microbiology · 2020Article
- ImmunodominantFrontiers in immunology · 2020Article
Corrections and comments
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Authors and funding
9 authors at 4 institutions in 2 countries.
Funding
Abstract
A growing body of evidence supports the hypothesis that intrinsically disordered proteins often mediate host-pathogen interactions and modulate host functions for pathogen survival and virulence. Mycobacterium tuberculosis (M.tb) has evolved largely through reductive evolution, with a few exceptions such as the glycine-alanine-rich PE-PPE/PGRS protein family, which has been expanding in pathogenic mycobacteria. Here, our analyses of the M.tb proteome and secretome revealed that the PE-PGRS subfamily is enriched for disordered regions and disordered binding sites, pointing to their importance in host-pathogen interactions. As a case study, the secondary structure of PE35-PPE68 and PE32-PPE65 of the pathogenesis-related RD1 and RD8 regions was analyzed through Fourier-transform infrared spectroscopy. These disordered proteins displayed a considerable structural shift from disordered to ordered while engaged in the formation of complexes. While these proteins are immunogenic individually and enhance the pro-pathogen response, their corresponding complexes enhanced the responses manifold as displayed here by PE35 and PPE68. It is likely that M.tb exploits such disorder-order structural dynamics as a strategy to mount a pro-pathogen response and subvert host defense for productive infection. This functional gain also serves as a means to compensate genomic content loss due to reductive evolution.
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