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Related Concept Videos

Bacterial Toxins01:12

Bacterial Toxins

Bacterial toxins are sophisticated virulence factors that enable pathogenic bacteria to interact with, invade, and damage host tissues. These toxins fall broadly into two types: protein exotoxins, which are secreted into the environment and target specific host receptors, and lipopolysaccharide endotoxins, which are structural components of the bacterial outer membrane released primarily during bacterial lysis or membrane shedding. Exotoxins generally act more selectively, binding to cell...
Lysosomal Hydrolases01:22

Lysosomal Hydrolases

Lysosomes are the site for the degradation of macromolecules and biological polymers released during membrane trafficking events such as secretory, endocytic, autophagic, and phagocytic pathways. The membrane-enclosed area of the lysosome, called the lumen, contains hydrolytic enzymes active in an acidic environment. These acid hydrolases are functional at a pH between 4.5 and 5 and are involved in cellular processes such as cell signaling, energy metabolism, restoration of the plasma membrane,...
Botulism01:22

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Botulism is a life-threatening neuroparalytic condition caused by botulinum neurotoxin, which is produced by the bacterium Clostridium botulinum, a Gram-positive, spore-forming, obligate anaerobe.In adults, the toxin enters the body in different ways: in foodborne botulism, the preformed toxin is absorbed in the intestine. In wound botulism, spores grow in injured tissue and release the toxin into the blood. Infant botulism differs mechanistically from adult forms. In infants, botulism commonly...
Lysosomes01:31

Lysosomes

Lysosomes are membrane-enclosed spherical sacs derived from the Golgi apparatus. The most important function of the lysosome is degrading macromolecules and biological polymers that are released during membrane trafficking events such as the secretory, endocytic, autophagic, and phagocytic pathways. The degradation is carried out by several hydrolytic enzymes active in an acidic environment of the lysosomal lumen. These acid hydrolases are involved in cellular processes such as cell signaling,...
Lysosomes01:31

Lysosomes

Lysosomes are membrane-enclosed spherical sacs derived from the Golgi apparatus. The most important function of the lysosome is degrading macromolecules and biological polymers that are released during membrane trafficking events such as the secretory, endocytic, autophagic, and phagocytic pathways. The degradation is carried out by several hydrolytic enzymes active in an acidic environment of the lysosomal lumen. These acid hydrolases are involved in cellular processes such as cell signaling,...
Formation of Lipopolysaccharides01:19

Formation of Lipopolysaccharides

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Related Experiment Video

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Live Imaging Assay for Assessing the Roles of Ca2+ and Sphingomyelinase in the Repair of Pore-forming Toxin Wounds
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Published on: August 25, 2013

Lysenin: a sphingomyelin specific pore-forming toxin.

Hidehiko Shogomori1, Toshihide Kobayashi

  • 1Supra-Biomolecular System Research Group, RIKEN (Institute of Physical and Chemical Research) Frontier Research System, 2-1, Hirosawa, Wako-shi, Saitama 351-0198, Japan.

Biochimica Et Biophysica Acta
|November 6, 2007
PubMed
Summary

Sphingomyelin, a key cell lipid, acts as a reservoir for signaling molecules. A modified toxin revealed that sphingomyelin-rich membrane domains are diverse in function and spatial organization.

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Published on: January 7, 2019

Area of Science:

  • Cell Biology
  • Biochemistry
  • Lipid Metabolism

Background:

  • Sphingomyelin is a crucial sphingolipid in mammalian cells.
  • It serves as a reservoir for bioactive lipid mediators like ceramide and sphingosine-1-phosphate.
  • Sphingomyelin is a key component of lipid rafts, specialized membrane microdomains rich in cholesterol and other lipids.

Purpose of the Study:

  • To investigate the role of sphingomyelin in cellular signaling.
  • To explore the structural organization and functional heterogeneity of sphingolipid-rich membrane domains.
  • To utilize lysenin, a sphingomyelin-binding toxin, as a tool to probe these membrane domains.

Main Methods:

  • Utilizing lysenin, a known sphingomyelin-binding toxin.
  • Developing a non-toxic mutant of lysenin.
  • Analyzing the binding specificity of lysenin to sphingomyelin based on its membrane distribution.
  • Investigating the spatial and functional characteristics of sphingolipid-rich membrane domains using the lysenin mutant.

Main Results:

  • Lysenin selectively binds to clustered sphingomyelin within cell membranes.
  • The binding is dependent on the specific distribution and organization of sphingomyelin.
  • A non-toxic lysenin mutant demonstrated that sphingolipid-rich membrane domains exhibit spatial and functional heterogeneity.
  • This heterogeneity is linked to the organization of sphingomyelin.

Conclusions:

  • Sphingomyelin's membrane organization dictates its accessibility to binding partners like lysenin.
  • Lysenin, particularly its non-toxic mutant, is a valuable tool for dissecting the complexity of sphingolipid-rich membrane domains.
  • These findings highlight the functional and spatial diversity within sphingolipid microdomains, impacting cellular processes.