Journal
TOXINS
Volume 3, Issue 7, Pages 884-899Publisher
MDPI AG
DOI: 10.3390/toxins3070884
Keywords
A-protomer; ADP-ribosylation; B-oligomer; G(i/o)-dependent; G(i/o)-independent; heterotrimeric G protein; G protein-coupled receptor; pertussis toxin; Toll-like receptor 4
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Pertussis toxin (PTX) is a typical A-B toxin. The A-protomer (S1 subunit) exhibits ADP-ribosyltransferase activity. The B-oligomer consists of four subunits (S2 to S5) and binds extracellular molecules that allow the toxin to enter the cells. The A-protomer ADP-ribosylates the alpha subunits of heterotrimeric G(i/o) proteins, resulting in the receptors being uncoupled from the G(i/o) proteins. The B-oligomer binds proteins expressed on the cell surface, such as Toll-like receptor 4, and activates an intracellular signal transduction cascade. Thus, PTX modifies cellular responses by at least two different signaling pathways; ADP-ribosylation of the G alpha(i/o) proteins by the A-protomer (G(i/o) protein-dependent action) and the interaction of the B-oligomer with cell surface proteins (G(i/o) protein-independent action).
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