Related Experiment Video

Updated: Aug 21, 2026

Detection of Toxin Translocation into the Host Cytosol by Surface Plasmon Resonance
10:41

Detection of Toxin Translocation into the Host Cytosol by Surface Plasmon Resonance

Published on: January 3, 2012

Effects of dynamin inactivation on pathways of anthrax toxin uptake

Werner Boll1, Marcelo Ehrlich, R John Collier

  • 1Department of Cell Biology, The CBR Institute for Biomedical Research, Harvard Medical School, Boston, MA 02115, USA.

European Journal of Cell Biology
|October 30, 2004
PubMed

Insights

Anthrax toxin entry into cells involves dynamin, but blocking this protein only partially reduces toxicity, suggesting alternative pathways. Long-term dynamin disruption alters the endosome environment, further decreasing anthrax lethal factor toxicity.

Area of Science:

  • Cell Biology
  • Toxicology
  • Molecular Biology

Background:

  • Anthrax lethal factor (LF) and protective antigen (PA) entry into host cells is crucial for toxicity.
  • This process requires internalization via the anthrax toxin receptor (ATR) and trafficking to acidic endosomes.
  • Dynamin protein is essential for clathrin-mediated endocytosis, a key pathway for toxin uptake.

Purpose of the Study:

  • To investigate the role of dynamin in anthrax toxin internalization and toxicity.
  • To differentiate the effects of acute versus long-term dynamin function disruption.
  • To explore alternative endocytic pathways for anthrax toxins.

Main Methods:

  • Utilized LFn-DTA, a fusion protein mimicking LF's N-terminal domain and diphtheria toxin catalytic subunit.
  • Assessed LFn-DTA toxicity under conditions of acute and long-term dynamin function blockade.
  • Analyzed the impact of dynamin disruption on endosomal trafficking and cellular environment.

Main Results:

  • Both acute and long-term dynamin inhibition partially reduced LFn-DTA toxicity, indicating alternative internalization routes.
  • Long-term dynamin blockade caused a further decrease in LFn-DTA toxicity.
  • This enhanced toxicity reduction suggests an altered endosomal environment, potentially increased endosomal pH.

Conclusions:

  • Dynamin is important but not solely responsible for anthrax toxin internalization.
  • Alternative endocytic pathways contribute to toxin uptake.
  • Long-term dynamin inhibition impacts the endosomal environment, affecting anthrax toxin efficacy.

More Related Videos

Analyzing Dynamic Protein Complexes Assembled On and Released From Biolayer Interferometry Biosensor Using Mass Spectrometry and Electron Microscopy09:30

Analyzing Dynamic Protein Complexes Assembled On and Released From Biolayer Interferometry Biosensor Using Mass Spectrometry and Electron Microscopy

Published on: August 6, 2018

Related Concept Videos

Inhalation Anthrax01:25

Inhalation Anthrax

Anthrax is a zoonotic disease caused by Bacillus anthracis, a Gram-positive, spore-forming bacterium. It primarily affects herbivorous animals but can be transmitted to humans through skin contact, ingestion, or inhalation of spores.Cutaneous anthrax, the most common form, typically results from direct contact with bacterial spores through skin abrasions and is generally less severe. Gastrointestinal anthrax results from eating undercooked or contaminated meat. It affects the mouth, throat, or...
Receptor-mediated Endocytosis01:20

Receptor-mediated Endocytosis

Receptor-mediated endocytosis is when bulk amounts of specific molecules are imported into a cell after binding to cell surface receptors. The molecules bound to these receptors are taken into the cell through inward folding of the cell surface membrane, which is eventually pinched off into a vesicle within the cell. Structural proteins, such as clathrin, coat the budding vesicle.
Clathrin-Mediated Endocytosis of LDL
One well-characterized example of receptor-mediated endocytosis is the...
Receptor-mediated Endocytosis01:38

Receptor-mediated Endocytosis

Overview
Pinching-off of Coated Vesicles01:32

Pinching-off of Coated Vesicles

Vesicle budding is orchestrated by distinct cytosolic proteins such as adaptor proteins, coat proteins, and GTPases. To initiate vesicle budding, membrane-bending proteins containing crescent-shaped BAR domains bind to the lipid heads in the bilayer and distort the membrane to form a protein-coated vesicle bud. Adaptors proteins such as AP2 for clathrin-coated vesicles can nucleate on the deformed membrane. Finally, coat proteins such as clathrin or COPI and COPII assemble into a coat forming...
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...
Botulism01:22

Botulism

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...