ArticleNature communications2023
A type VII-secreted lipase toxin with reverse domain arrangement.
Article in Nature communications, 2023. 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.
- Article
- 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
- A Type VII-secreted toxin enables inter-mycobacterial competition.Nature communications · 2026Article
- A toxic effector of T7SS facilitates bacterial competition and virulence through membrane damage in Streptococcus suis.Veterinary research · 2026Article
- Pseudomonadota bridge cross-trophic interactions to suppress plant pathogens.The ISME journal · 2026Article
- A novel reverse lipase toxin substrate of themicroLife · 2026Article
- Streptococcus gordonii type VII secretion system substrate EsxA induces neutrophil extracellular trap formation in infective endocarditis.Scientific reports · 2025Article
- TheMicrobiology (Reading, England) · 2025Article
- Distinct immunity protein families mediate compartment-specific neutralization of a bacterial toxin.Cell reports · 2025Article
- Review
- A LXG toxin stabilized by DUF4176 contributes to Streptococcus suis competition and pathogenicity.BMC biology · 2025Article
- A widespread family of molecular chaperones promotes the intracellular stability of type VIIb secretion system-exported toxins.Proceedings 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
- Identifying a type of toxic effectors exported by the type VII secretion system to enhance competitive fitness inFrontiers in cellular and infection microbiology · 2025Article
- High-throughput functional analysis provides novel insight into type VII secretion inOpen biology · 2024Article
- A group B streptococcal type VII secreted LXG toxin mediates interbacterial competition and colonization of the female genital tract.bioRxiv : the preprint server for biology · 2024Article
- Meeting report 'Microbiology 2023: from single cell to microbiome and host', an international interacademy conference in Würzburg.microLife · 2024Article
- The role of proteinaceous toxins secreted byFEMS microbes · 2024Review
- Article
Corrections and comments
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Authors and funding
11 authors.
Funding
Abstract
The type VII protein secretion system (T7SS) is found in many Gram-positive bacteria and in pathogenic mycobacteria. All T7SS substrate proteins described to date share a common helical domain architecture at the N-terminus that typically interacts with other helical partner proteins, forming a composite signal sequence for targeting to the T7SS. The C-terminal domains are functionally diverse and in Gram-positive bacteria such as Staphylococcus aureus often specify toxic anti-bacterial activity. Here we describe the first example of a class of T7 substrate, TslA, that has a reverse domain organisation. TslA is widely found across Bacillota including Staphylococcus, Enterococcus and Listeria. We show that the S. aureus TslA N-terminal domain is a phospholipase A with anti-staphylococcal activity that is neutralised by the immunity lipoprotein TilA. Two small helical partner proteins, TlaA1 and TlaA2 are essential for T7-dependent secretion of TslA and at least one of these interacts with the TslA C-terminal domain to form a helical stack. Cryo-EM analysis of purified TslA complexes indicate that they share structural similarity with canonical T7 substrates. Our findings suggest that the T7SS has the capacity to recognise a secretion signal present at either end of a substrate.
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