ArticlePloS one2014
WXG100 protein superfamily consists of three subfamilies and exhibits an α-helical C-terminal conserved residue pattern.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 69 papers.
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69 citing papers in PubMed.
- Variation in multiple classes of simple sequence repeats can alter drug susceptibility inbioRxiv : the preprint server for biology · 2026Article
- Type VIIb secretion systems in Lactobacillales: insights from streptococci and enterococci.Journal of bacteriology · 2026Review
- EsxA is required for antibacterial toxin export by the type VIIb secretion system.The Journal of biological chemistry · 2026Article
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- Immunogenicity and protective potential of a mucosal protein-only vaccine candidate for tuberculosis.Frontiers in immunology · 2026Article
- Protein-Mediated Virulence in Mycobacterium tuberculosis.Advances in experimental medicine and biology · 2026Review
- Sigma factor M induces an ESX-4-focused regulon inFrontiers in tuberculosis · 2026Article
- Streptococcus gordonii type VII secretion system substrate EsxA induces neutrophil extracellular trap formation in infective endocarditis.Scientific reports · 2025Article
- Immunopeptidomics can inform the design of mRNA vaccines for the delivery ofScience translational medicine · 2025Article
- Loss of the ESX-5 secretion locus inProceedings of the National Academy of Sciences of the United States of America · 2025Article
- PPE50 variants as novel phylogeographic signatures of host-pathogen co-evolution in tuberculosis.Communications biology · 2025Article
- The PE/PPE family proteins ofFrontiers in immunology · 2025Review
- EsxA, a type VII secretion system-dependent effector, reveals a novel function in the sporulation of Bacillus cereus ATCC14579.BMC microbiology · 2024Article
- ESAT-6 undergoes self-association at phagosomal pH and an ESAT-6-specific nanobody restrictseLife · 2024Article
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- ESAT-6 undergoes self-association at phagosomal pH and an ESAT-6 specific nanobody restricts M. tuberculosis growth in macrophages.bioRxiv : the preprint server for biology · 2024Article
- Integrated sequence and -omic features reveal novel small proteome ofFrontiers in microbiology · 2024Article
- Interbacterial competition mediated by the type VIIb secretion system.Microbiology (Reading, England) · 2023Review
- Heterogeneity of the group B streptococcal type VII secretion system and influence on colonization of the female genital tract.Molecular microbiology · 2023Article
9 more citing papers are in PubMed but not listed here.
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5 authors.
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Abstract
Members of the WXG100 protein superfamily form homo- or heterodimeric complexes. The most studied proteins among them are the secreted T-cell antigens CFP-10 (10 kDa culture filtrate protein, EsxB) and ESAT-6 (6 kDa early secreted antigen target, EsxA) from Mycobacterium tuberculosis. They are encoded on an operon within a gene cluster, named as ESX-1, that encodes for the Type VII secretion system (T7SS). WXG100 proteins are secreted in a full-length form and it is known that they adopt a four-helix bundle structure. In the current work we discuss the evolutionary relationship between the homo- and heterodimeric WXG100 proteins, the basis of the oligomeric state and the key structural features of the conserved sequence pattern of WXG100 proteins. We performed an iterative bioinformatics analysis of the WXG100 protein superfamily and correlated this with the atomic structures of the representative WXG100 proteins. We find, firstly, that the WXG100 protein superfamily consists of three subfamilies: CFP-10-, ESAT-6- and sagEsxA-like proteins (EsxA proteins similar to that of Streptococcus agalactiae). Secondly, that the heterodimeric complexes probably evolved from a homodimeric precursor. Thirdly, that the genes of hetero-dimeric WXG100 proteins are always encoded in bi-cistronic operons and finally, by combining the sequence alignments with the X-ray data we identify a conserved C-terminal sequence pattern. The side chains of these conserved residues decorate the same side of the C-terminal α-helix and therefore form a distinct surface. Our results lead to a putatively extended T7SS secretion signal which combines two reported T7SS recognition characteristics: Firstly that the T7SS secretion signal is localized at the C-terminus of T7SS substrates and secondly that the conserved residues YxxxD/E are essential for T7SS activity. Furthermore, we propose that the specific α-helical surface formed by the conserved sequence pattern including YxxxD/E motif is a key component of T7SS-substrate recognition.
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