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    Toxins (Basel). 2011 Jul;3(7):884-99. Epub 2011 Jul 15.

    G(i/o) Protein-Dependent and -Independent Actions of Pertussis Toxin (PTX).

    Mangmool S, Kurose H.

    Source

    Department of Pharmacology, Faculty of Pharmacy, Mahidol University, 447 Sri-Ayudhaya, Rajathevi, Bangkok 10400, Thailand; Email: pysmm@mahidol.ac.th.

    Abstract

    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 α 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 Gα(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).

    PMID:
    22069745
    [PubMed]
    PMCID:
    PMC3202852
    Free PMC Article

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