ArticlePloS one2013
The Bacillus cereus Hbl and Nhe tripartite enterotoxin components assemble sequentially on the surface of target cells and are not interchangeable.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.
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Who cites it
53 citing papers in PubMed, 102 citations in OpenAlex.
- Article
- Environmental modulation of cytotoxicity and virulence factor stability in psychrotolerant Bacillus cereus group isolates.Food microbiology · 2026Article
- 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
- Caveolin 1 is a conserved host factor mediating Bacillus cereus hemolysin BL toxin cytolytic toxicity.PLoS biology · 2026Article
- The major toxins of Bacillus cereus - Current knowledge on distribution, regulation and mechanism of action.EXCLI journal · 2026Review
- Proposal ofInternational journal of molecular sciences · 2025Article
- Article
- A new understanding of Acanthamoeba castellanii: dispelling the role of bacterial pore-forming toxins in cyst formation and amoebicidal actions.Cell death discovery · 2025Article
- MakC and MakD are two proteins associated with a tripartite toxin ofFrontiers in microbiology · 2024Article
- The quorum-sensing peptidic inhibitor rescues host immune system eradication: A novel infectivity mechanism.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Toxin-linked mobile genetic elements in major enteric bacterial pathogens.Gut microbiome (Cambridge, England) · 2023Review
- Article
- Categorizing Sequences of Concern by Function To Better Assess Mechanisms of Microbial Pathogenesis.Infection and immunity · 2022Review
- 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
- Seaweed-associated heterotrophic bacteria: are they future novel sources of antimicrobial agents against drug-resistant pathogens?Archives of microbiology · 2022Article
- Antibiotic-active heterotrophic Firmicutes sheltered in seaweeds: can they add new dimensions to future antimicrobial agents?Archives of microbiology · 2022Article
- Article
- Purification and characterization of antibacterial surfactin isoforms produced by Bacillus velezensis SK.AMB Express · 2022Article
- Prevalence, distribution, enterotoxin profiles, antimicrobial resistance, and genetic diversity ofFrontiers in microbiology · 2022Article
- Prevalence and antimicrobial-resistant characterization ofFrontiers in microbiology · 2022Article
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Bacillus cereus is a spore-forming, Gram-positive bacterium commonly associated with outbreaks of food poisoning. It is also known as an opportunistic pathogen causing clinical infections such as bacteremia, meningitis, pneumonia, and gas gangrene-like cutaneous infections, mostly in immunocompromised patients. B. cereus secretes a plethora of toxins of which four are associated with the symptoms of food poisoning. Two of these, the non-hemolytic enterotoxin Nhe and the hemolysin BL (Hbl) toxin, are predicted to be structurally similar and are unique in that they require the combined action of three toxin proteins to induce cell lysis. Despite their dominant role in disease, the molecular mechanism of their toxic function is still poorly understood. We report here that B. cereus strain ATCC 10876 harbors not only genes encoding Nhe, but also two copies of the hbl genes. We identified Hbl as the major secreted toxin responsible for inducing rapid cell lysis both in cultured cells and in an intraperitoneal mouse toxicity model. Antibody neutralization and deletion of Hbl-encoding genes resulted in significant reductions of cytotoxic activity. Microscopy studies with Chinese Hamster Ovary cells furthermore showed that pore formation by both Hbl and Nhe occurs through a stepwise, sequential binding of toxin components to the cell surface and to each other. This begins with binding of Hbl-B or NheC to the eukaryotic membrane, and is followed by the recruitment of Hbl-L1 or NheB, respectively, followed by the corresponding third protein. Lastly, toxin component complementation studies indicate that although Hbl and Nhe can be expressed simultaneously and are predicted to be structurally similar, they are incompatible and cannot complement each other.
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