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Biochemical properties of pertussis toxin
D L Burns1, S Z Hausman, M H Witvliet
1Center for Biologics Evaluation and Research, Food and Drug Administration, Bethesda, MD 20892.
Abstract:
Pertussis toxin is an exotoxin produced by the organism Bordetella pertussis. The toxin binds to receptors on the eukaryotic cell surface. After introduction into the eukaryotic cell, the toxin is activated by ATP and subsequently ADP-ribosylates a family of GTP-binding regulatory proteins interrupting signal transduction within the cell. We have examined the location of several critical sites on the toxin molecule. These sites include the receptor binding site and the ATP binding site. The B oligomer of the toxin was found to contain at least two sites capable of binding glycoproteins suggesting that the B oligomer may have more than one eukaryotic cell receptor binding site. ATP was also shown to bind to a site on the B oligomer. These results indicate that the B oligomer contains several sites necessary for toxin action.
Insights
Pertussis toxin from Bordetella pertussis targets eukaryotic cells by binding receptors and interrupting cell signaling. Research shows the toxin's B oligomer contains key binding sites for cellular receptors and ATP, crucial for its action.
Area of Science:
- Microbiology
- Molecular Biology
- Cell Biology
Background:
- Pertussis toxin is a critical virulence factor produced by Bordetella pertussis.
- The toxin disrupts eukaryotic cell signal transduction via ADP-ribosylation of GTP-binding proteins.
Purpose of the Study:
- To investigate the specific locations of functional sites on pertussis toxin.
- To identify the receptor binding site and ATP binding site on the toxin molecule.
Main Methods:
- Biochemical analysis of pertussis toxin structure and function.
- Characterization of binding interactions between the toxin's B oligomer and cellular components.
Main Results:
- The B oligomer of pertussis toxin possesses at least two glycoprotein binding sites, suggesting multiple eukaryotic cell receptors.
- A specific ATP binding site was identified on the B oligomer of the toxin.
Conclusions:
- The B oligomer of pertussis toxin contains essential sites for receptor binding and ATP interaction.
- These findings elucidate critical domains within the B oligomer necessary for pertussis toxin's cellular activity.