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Updated: Feb 7, 2026
08:14
Determining Membrane Protein Topology Using Fluorescence Protease Protection FPP
Published on: April 20, 2015
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Anthrax protective antigen is a calcium-dependent serine protease
Lisanne Storm1, Floris J Bikker2, Kamran Nazmi2
1a Department of Medical Microbiology and Infectious Diseases , Erasmus University Medical Centre , Rotterdam , The Netherlands.
Virulence
|July 28, 2018
Summary
Protective antigen (PA) from Bacillus anthracis is a calcium-dependent serine protease. Targeting this proteolytic activity offers a novel therapeutic strategy against anthrax infections.
Area of Science:
- Microbiology
- Biochemistry
- Pathogenesis
Background:
- Bacillus anthracis produces a three-component exotoxin complex crucial for anthrax pathogenesis.
- Exotoxin complex formation initiates with the binding of protective antigen (PA) to its cellular receptor.
Purpose of the Study:
- To investigate the enzymatic activity of protective antigen (PA).
- To explore the role of PA's proteolytic activity in receptor binding and anthrax pathogenesis.
Main Methods:
- Biochemical assays to determine PA's enzymatic properties.
- Analysis of PA's interaction with cellular receptors.
Main Results:
- Protective antigen (PA) functions as a calcium-dependent serine protease.
- PA's proteolytic activity is potentially involved in its binding to cellular receptors.
Conclusions:
- Protective antigen (PA) possesses intrinsic serine protease activity.
- Inhibiting PA's proteolytic function presents a potential novel therapeutic approach for B. anthracis infections.
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