Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Bacterial Gastroenteritis

Bacterial Gastroenteritis

Bacterial gastroenteritis, characterized by diarrhea, abdominal cramps, and vomiting, is often caused by ingestion of contaminated food or water and is frequently associated with pathogenic Escherichia coli strains. These microbes exploit two principal mechanisms to inflict disease.Shiga toxin–producing E. coli, also referred to as STEC—notably O157:H7—release Shiga toxins that target ribosomes, blocking protein synthesis. The B subunit of the toxin binds the host glycolipid receptor...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

A novel robot for CT-guided bone needle insertion with a rotational drilling and force-feedback speed control mechanism: preliminary evaluation in swine.

Japanese journal of radiology·2026

Same author

Repurposing caspofungin as a small-molecule inhibitor of Clostridium perfringens α-toxin for treatment of gas gangrene.

Communications medicine·2026

Same author

Temperature-driven metabolic acceleration independent of cell growth enables high-level production of D-ribulose and shinorine in Streptomyces lividans.

Biotechnology for biofuels and bioproducts·2026

Same author

Comparison of robotic versus manual needle insertion for CT-guided intervention: prospective randomized trial.

Radiology advances·2025

Same author

Identification of amino acids essential for angulin-1/3 binding of the tricellular tight junction binder, angubindin-1.

FEBS open bio·2025

Same author

Oral and transdermal administration of lipopolysaccharide safely enhances self-healing ability through the macrophage network.

Frontiers in immunology·2025

Search research articles

Related Experiment Video

Updated: Jun 15, 2026

Live Imaging Assay for Assessing the Roles of Ca2+ and Sphingomyelinase in the Repair of Pore-forming Toxin Wounds

Live Imaging Assay for Assessing the Roles of Ca²⁺ and Sphingomyelinase in the Repair of Pore-forming Toxin Wounds

Published on: August 25, 2013

Hemolysis induced by Bacillus cereus sphingomyelinase.

Masataka Oda¹, Masaya Takahashi, Takayuki Matsuno

¹Department of Microbiology, Faculty of Pharmaceutical Sciences, Tokushima Bunri University, Yamashiro-cho, Tokushima, Japan 770-8514.

Biochimica Et Biophysica Acta

|March 11, 2010

Summary

Bacillus cereus sphingomyelinase (Bc-SMase) causes sheep red blood cell lysis by producing ceramide. Unlike alpha-toxin, Bc-SMase acts on whole membranes, forming ceramide-rich domains and reducing fluidity.

More Related Videos

Separation of the Cell Envelope for Gram-negative Bacteria into Inner and Outer Membrane Fractions with Technical Adjustments for Acinetobacter baumannii

Separation of the Cell Envelope for Gram-negative Bacteria into Inner and Outer Membrane Fractions with Technical Adjustments for Acinetobacter baumannii

Published on: April 10, 2020

Intravitreal Injection and Quantitation of Infection Parameters in a Mouse Model of Bacterial Endophthalmitis

Intravitreal Injection and Quantitation of Infection Parameters in a Mouse Model of Bacterial Endophthalmitis

Published on: February 6, 2021

Related Experiment Videos

Last Updated: Jun 15, 2026

Live Imaging Assay for Assessing the Roles of Ca2+ and Sphingomyelinase in the Repair of Pore-forming Toxin Wounds

Live Imaging Assay for Assessing the Roles of Ca²⁺ and Sphingomyelinase in the Repair of Pore-forming Toxin Wounds

Published on: August 25, 2013

Separation of the Cell Envelope for Gram-negative Bacteria into Inner and Outer Membrane Fractions with Technical Adjustments for Acinetobacter baumannii

Separation of the Cell Envelope for Gram-negative Bacteria into Inner and Outer Membrane Fractions with Technical Adjustments for Acinetobacter baumannii

Published on: April 10, 2020

Intravitreal Injection and Quantitation of Infection Parameters in a Mouse Model of Bacterial Endophthalmitis

Intravitreal Injection and Quantitation of Infection Parameters in a Mouse Model of Bacterial Endophthalmitis

Published on: February 6, 2021

Area of Science:

Microbiology
Biochemistry
Cell Biology

Background:

Bacillus cereus sphingomyelinase (Bc-SMase) is known to lyse sheep erythrocytes.
Sheep erythrocytes are rich in sphingomyelin, a substrate for Bc-SMase.
Clostridium perfringens alpha-toxin also induces hemolysis, offering a comparative model.

Purpose of the Study:

To elucidate the mechanism of Bc-SMase-induced hemolysis.
To compare the hemolytic mechanism of Bc-SMase with that of Clostridium perfringens alpha-toxin.
To investigate the role of ceramide production and membrane changes in Bc-SMase hemolysis.

Main Methods:

Comparative analysis of hemolysis inhibition using specific toxins and inhibitors.
Investigation of toxin binding to membrane fractions (whole membranes vs. lipid rafts).
Quantification of ceramide production in erythrocytes and liposomes.
Confocal laser microscopy and photobleaching analysis to assess membrane changes.

Main Results:

Bc-SMase hemolysis was not inhibited by Gi-specific inhibitors, ceramidase, or sphingosine kinase inhibitors, unlike alpha-toxin.
Bc-SMase bound to whole membranes, whereas alpha-toxin targeted lipid rafts.
Bc-SMase induced significantly higher ceramide production in erythrocytes compared to alpha-toxin at similar hemolysis levels.
Bc-SMase treatment led to the formation of ceramide-rich domains and reduced membrane fluidity.

Conclusions:

Bc-SMase-induced hemolysis is mechanistically distinct from alpha-toxin-induced hemolysis.
Ceramide production and subsequent formation of ceramide-rich domains are key to Bc-SMase activity.
Bc-SMase alters membrane properties, leading to erythrocyte lysis through domain interface formation.