Article
Proteolytic cleavage of pertussis toxin S1 subunit is not essential for its activity in mammalian cells.
BMC microbiology - 3 Feb 2005
Carbonetti Nicholas H, Mays R Michael, Artamonova Galina V, Plaut Roger D, Worthington Zoë E V
Abstract excerpt
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...
Topics
- Amino Acid Sequence
- Animals
- Binding Sites
- CHO Cells
- Cricetinae
- Gene Expression Regulation
- Mutation
- Pertussis Toxin
- Protein Processing, Post-Translational
- Protein Transport