ArticleScientific reports2021
Characterisation of a tripartite α-pore forming toxin from Serratia marcescens.
Article in Scientific reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
What it found
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Who cites it
13 citing papers in PubMed, 17 citations in OpenAlex.
- NheABC is a pH-dependent cytotoxin that targets mitochondria and contributes to the virulence of Bacillus cereus in wound infections.Cell communication and signaling : CCS · 2026Article
- Cryo-EM structure of detergent-boundbioRxiv : the preprint server for biology · 2026Article
- Bacterial pore-forming toxins: mechanisms and implications for host immunity.Bioscience reports · 2026Review
- Bacterial infection elicits theOpen biology · 2025Article
- Characterization of a novelMicrobiology spectrum · 2025Article
- A new understanding of Acanthamoeba castellanii: dispelling the role of bacterial pore-forming toxins in cyst formation and amoebicidal actions.Cell death discovery · 2025Article
- Article
- MakC and MakD are two proteins associated with a tripartite toxin ofFrontiers in microbiology · 2024Article
- V. cholerae MakA is a cholesterol-binding pore-forming toxin that induces non-canonical autophagy.The Journal of cell biology · 2022Article
- A Genomic Island of Vibrio cholerae Encodes a Three-Component Cytotoxin with Monomer and Protomer Forms Structurally Similar to Alpha-Pore-Forming Toxins.Journal of bacteriology · 2022Article
- Bacterial pore-forming toxins.Microbiology (Reading, England) · 2022Article
- Article
- A tripartite cytolytic toxin formed byProceedings of the National Academy of Sciences of the United States of America · 2021Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
Tripartite members of the ClyA family of α-PFTs have recently been identified in a number of pathogenic Gram-negative bacteria, including the human pathogen Serratia marcescens. Structures of a Gram-negative A component and a tripartite α-PFT complete pore are unknown and a mechanism for pore formation is still uncertain. Here we characterise the tripartite SmhABC toxin from S. marcescens and propose a mechanism of pore assembly. We present the structure of soluble SmhA, as well as the soluble and pore forms of SmhB. We show that the β-tongue soluble structure is well conserved in the family and propose two conserved latches between the head and tail domains that are broken on the soluble to pore conformational change. Using the structures of individual components, sequence analysis and docking predictions we illustrate how the A, B and C protomers would assemble on the membrane to produce a complete tripartite α-PFT pore.
Identifiers
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.