(1) Department of Microbiology and Immunology, University of Maryland School of Medicine, 21201 Baltimore, MD, USA
Abstract:
Background
Pertussis toxin (PT) is an exotoxin virulence factor produced by Bordetella pertussis, the causative agent of whooping cough. PT consists of an active subunit (S1) that ADP-ribosylates the alpha subunit of several
mammalian G proteins, and a B oligomer (S2–S5) that binds glycoconjugate receptors on cells. PT appears to enter cells by
endocytosis, and retrograde transport through the Golgi apparatus may be important for its cytotoxicity. A previous study
demonstrated that proteolytic processing of S1 occurs after PT enters mammalian cells. We sought to determine whether this
proteolytic processing of S1 is necessary for PT cytotoxicity.