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Identification of the cellular receptor for anthrax toxin
K A Bradley1, J Mogridge, M Mourez
1McArdle Laboratory for Cancer Research, University of Wisconsin-Madison, 1400 University Avenue, Madison, Wisconsin 53706, USA.
Nature
|November 9, 2001
Summary
Researchers identified the human anthrax toxin receptor (ATR). This protein binds protective antigen (PA) and mediates toxin entry into cells, offering a potential target for anthrax treatments.
Area of Science:
- Microbiology
- Immunology
- Molecular Biology
Background:
- Bacillus anthracis secretes a tripartite toxin to evade host immunity and cause systemic infection.
- The toxin components, oedema factor (OF) and lethal factor (LF), impair host defenses by modifying intracellular substrates.
- Protective antigen (PA) facilitates toxin entry into mammalian cells by binding to a cellular receptor.
Purpose of the Study:
- To identify and clone the human receptor for Bacillus anthracis protective antigen (PA).
Main Methods:
- Cloning of the human PA receptor using a genetic complementation approach.
Main Results:
- The human PA receptor, named ATR (anthrax toxin receptor), was cloned.
- ATR is a type I membrane protein featuring an extracellular von Willebrand factor A domain.
- This domain directly binds to PA, and a soluble version can neutralize the toxin's effects.
Conclusions:
- The identification of ATR provides a key molecular target for understanding and potentially neutralizing anthrax toxin.
- ATR's PA-binding domain is crucial for toxin entry and represents a promising therapeutic target.
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