Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Anthrax toxin: receptor binding, internalization, pore formation, and translocation.

John A T Young1, R John Collier

  • 1Infectious Disease Laboratory, The Salk Institute for Biological Studies, La Jolla, California 92037, USA. jyoung@salk.edu

Annual Review of Biochemistry
|March 6, 2007
PubMed
Summary

Anthrax toxin uses Protective Antigen (PA) to deliver Lethal Factor (LF) and Edema Factor (EF) into cells. PA forms a pore in the endosome, enabling enzyme entry and cellular toxicity.

Related Concept Videos

You might also read

Related Articles

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

Sort by
Same author

Antiviral target compound profile for pandemic preparedness.

Nature reviews. Drug discovery·2024
Same author

Author Correction: A novel antibiotic class targeting the lipopolysaccharide transporter.

Nature·2024
Same author

A novel antibiotic class targeting the lipopolysaccharide transporter.

Nature·2024
Same author

Discovery of 4,5,6,7-Tetrahydropyrazolo[1.5-a]pyrizine Derivatives as Core Protein Allosteric Modulators (CpAMs) for the Inhibition of Hepatitis B Virus.

Journal of medicinal chemistry·2023
Same author

Discovery of Linvencorvir (RG7907), a Hepatitis B Virus Core Protein Allosteric Modulator, for the Treatment of Chronic HBV Infection.

Journal of medicinal chemistry·2023
Same author

Discovery of a first-in-class orally available HBV cccDNA inhibitor.

Journal of hepatology·2023

Area of Science:

  • Biochemistry
  • Cell Biology
  • Toxicology

Background:

  • Anthrax toxin is a tripartite complex comprising Protective Antigen (PA), Lethal Factor (LF), and Edema Factor (EF).
  • LF and EF are enzymatic components, while PA facilitates cellular entry and complex assembly.
  • Understanding the molecular mechanisms of toxin translocation is crucial for developing countermeasures.

Purpose of the Study:

  • To elucidate the molecular mechanisms by which anthrax toxin components enter mammalian cells.
  • To investigate the role of Protective Antigen (PA) in receptor binding, complex assembly, and endosomal translocation.
  • To gain insights into the function of the PA pore in delivering enzymatic factors to the cytosol.

Main Methods:

  • Analysis of PA-receptor and PA-ligand interactions.

Related Experiment Videos

  • Investigation of pH-dependent pore formation by PA.
  • Studies on the translocation of LF and EF across the endosomal membrane mediated by PA.

    • Main Results:

    • PA recognizes specific cellular receptors and binds LF and EF to form toxic complexes.
    • PA-receptor interactions modulate the pH-dependent pore formation critical for endosomal escape.
    • The PA pore facilitates the translocation of LF and EF into the host cell cytosol.

    Conclusions:

    • Protective Antigen (PA) is central to anthrax toxin's cellular entry mechanism.
    • PA's ability to form a pH-sensitive pore in endosomal membranes is key to delivering toxic enzymes.
    • This research deepens the understanding of anthrax toxin pathogenesis and informs therapeutic strategies.