Intracellular trafficking and membrane translocation of pertussis toxin into host cells

International Journal of Medical Microbiology

Volumn 290, Issue 4-5, 2000, Pages 409-413

  Veithen, A ^a   Raze, D ^a   Locht, C ^a  

^a INSTITUT PASTEUR DE LILLE   (France)

Author keywords

ADP; Endoplasmic reticulum; Pertussis toxin; Ribosylation; Translocation

Indexed keywords

EID: 0033752841     PISSN: 14384221     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1438-4221(00)80053-3     Document Type: Conference Paper

References (17)

1. Roles of the disulfide bond and the carboxy-terminal region of the S1 subunit in the assembly and biosynthesis of pertussis toxin
2. Intracellular delivery of a cytolytic T-lymphocyte epitope peptide by pertussis toxin to major histocompatibility complex class I without involvement of the cytosolic class I antigen processing pathway
3. Endocytosis and retrograde transport of pertussis toxin to the Golgi complex as a prerequisite for cellular intoxication
4. Importance of ADP-ribosylation in the morphological changes of PC-12 cells induced by cholera toxin
5. Interaction of pertussis toxin with cells and model membranes
6. Accumulating evidence suggests that several AB-toxins subvert the endoplasmic reticulum-associated protein degradation pathway to enter target cells
7. Surfing on a retrograde wave: How does Shiga toxin reach the endoplasmic reticulum?
8. Pertussis toxin and target eukaryotic cells: Binding, entry, and activation
9. Assignment of functional domains involved in ADP-ribosylation and B-oligomer binding within the carboxyl terminus of the S1 subunit of pertussis toxin
10. Retrograde transport: Going against the flow
11. Toxin entry: Retrograde transport through the secretory pathway
12. Protein toxins and membrane transport
13. Genetic exchange of the S2 and S3 subunits in pertussis toxin
14. Disruption of an internal membrane-spanning region in Shiga toxin 1 reduces cytotoxicity
15. Expression of bacterial cytotoxin genes in mammalian target cells
16. Pertussis toxin-mediated ADP-ribosylation of target proteins in Chinese Hamster Ovary cells involves a vesicle trafficking mechanism
17. Pertussis toxin-catalysed ADP-ribosylation of G(iα2) and G(iα3) in CHO cells is modulated by inhibitors of intracellular trafficking