Pathways & interactions
Aerolysin/Pertussis toxin domain (IPR005138)
Short name: APT_dom
Overlapping homologous superfamilies
- C-type lectin fold (IPR016187)
- Aerolysin/Pertussis toxin (APT), N-terminal domain superfamily (IPR037015)
This is the N-terminal domain of aerolysin and pertussis toxin which contains a type-C lectin like fold.
Aerolysin causes the pathogenicity of Aeromonas hydrophila, a bacterium associated with diarrhoeal diseases and deep wound infections. Like many other microbial toxins, the protein changes in a multistep process from a completely water-soluble form to produce a transmembrane channel that breaks the permeability barrier of cells [PMID: 7510043].
Pertussis toxin is a major virulence factor of Bordetella pertussis, which causes whooping cough. The protein is a hexamer containing a catalytic subunit (S1) that is tightly associated with a pentameric cell-binding component (B-oligomer). ATP, detergents and phospholipids assist in activating the holotoxin by destabilising the interaction between S1 and the B-oligomer [PMID: 8637000]. Pertussis toxin is an exotoxin and is an essential component of acellular vaccines [PMID: 8075982, PMID: 7634099]. The catalytic A-subunit (S1) shares structural homology with other ADP-ribosylating bacterial toxins, although differences in the carboxy-terminal portion explain its unique activation mechanism [PMID: 8075982]. The diverse biological activities of the toxin depend on its ability to recognise carbohydrate-containing receptors on a wide variety of eukaryotic cells.
- PF03440 (APT)