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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...
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Proteins and neurotransmitters in secretory vesicles can be released from a cell upon vesicle docking, priming, and fusion with the plasma membrane. Vesicles are docked and primed in preparation for the quick exocytosis of their contents in response to a stimulus. The fusion process is mainly carried out by a SNAP Receptor or SNARE complex, consisting of synaptobrevin, syntaxin-1, and SNAP-25.
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Mechanisms of Membrane Domain Formation00:59

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Different physical properties of lipids and proteins allow them to localize and form distinct islands or domains in the membrane. Some membrane domains are formed due to protein-protein interactions, whereas others are formed due to the presence of specific lipids such as sphingolipids and sterols—for example, large proteins, such as bacteriorhodopsin, aggregate and create distinct domains.
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α-Helix containing multi-pass transmembrane proteins
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Botulism01:22

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

Published on: August 25, 2013

Membrane interaction of Pasteurella multocida toxin involves sphingomyelin.

Michael C Brothers1, Mengfei Ho, Ram Maharjan

  • 1Department of Chemistry, University of Illinois, Urbana, IL 61801, USA.

The FEBS Journal
|September 29, 2011
PubMed
Summary
This summary is machine-generated.

Pasteurella multocida toxin (PMT) binds to host cell membranes via phospholipids like sphingomyelin, not gangliosides. This finding suggests a protein co-receptor may be involved in PMT entry.

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Area of Science:

  • Microbiology
  • Cell Biology
  • Biochemistry

Background:

  • Pasteurella multocida toxin (PMT) is an AB toxin inducing various host cell effects.
  • The N-terminus of PMT (PMT-N) is crucial for cellular entry and toxin delivery.
  • Gangliosides were previously suggested as host receptors for PMT.

Purpose of the Study:

  • To investigate the specific membrane components involved in PMT binding.
  • To clarify the role of gangliosides versus phospholipids in PMT-host cell interactions.
  • To elucidate the mechanism of PMT cellular entry.

Main Methods:

  • Thin-layer chromatography (TLC)-overlay binding assays with labeled PMT fragments.
  • Pull-down experiments using reconstituted membrane liposomes and full-length PMT.
  • Surface plasmon resonance (SPR) analysis of PMT-N binding to liposomes and cell membranes.

Main Results:

  • PMT and PMT-N did not bind to gangliosides (GM1, GM2, GM3) in experimental systems.
  • PMT and PMT-N demonstrated binding to membrane phospholipids, particularly sphingomyelin and phosphatidylcholine.
  • SPR analysis indicated PMT-N binding to HEK-293T cell membranes, suggesting a role for sphingomyelin.

Conclusions:

  • Sphingomyelin is critical for PMT binding to host cell membranes.
  • The findings challenge the role of gangliosides as primary PMT receptors.
  • A protein co-receptor is likely involved in PMT-membrane interactions.