Bordetella Extracytoplasmic Adenylate Cyclase: Structural and Functional Analogies with Bacillus anthracis Edema Factor Adenylate Cyclase
Abstract
Despite enzymatic similarities, the adenylate cyclase (AC) toxins from Bordetella pertussis and Bacillus anthracis appear to be very different structurally and functionally. The two do not compete in intoxication of target cells and clearly enter by different mechanisms, with EF + PA employing a receptor-mediated endocytosis pathway and B. pertussis AC toxins entering by unknown route. The two AC toxins exhibit some major differences in target cell specificities, with EF + PA being less efficacious in affecting immune effector cells such as monocytes. Although there appears to be a very limited immunologic cross-reactivity, the toxins do not seem to have significant structural homology. Examination of the two toxins do not seem to have significant structural homology. Examination of the two toxins in parallel has proven to be a useful approach,superior to the isolated study of either alone. Keywords: Bordetella pertussis; Bacillus anthracis; Rabbits; Edema factor; Adenylate.
Document Details
- Document Type
- Technical Report
- Publication Date
- Mar 11, 1988
- Accession Number
- ADA211956
Entities
People
- Erik L. Hewlett
- Valery Gordon
Organizations
- University of Virginia