ArticleInfection and immunity1995
Pertussis toxin-mediated ADP-ribosylation of target proteins in Chinese hamster ovary cells involves a vesicle trafficking mechanism.
Article in Infection and immunity, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 52 citations in OpenAlex.
- Salmonella enterica serovar typhi limits the potency of typhoid toxin and ADP-ribosylating toxin AB to establish a persistent infection.FEBS open bio · 2026Article
- Article
- Pharmacological targeting of host chaperones protects from pertussis toxin in vitro and in vivo.Scientific reports · 2021Article
- Application of xCELLigence real-time cell analysis to the microplate assay for pertussis toxin induced clustering in CHO cells.PloS one · 2021Article
- A binding motif for Hsp90 in the A chains of ADP-ribosylating toxins that move from the endoplasmic reticulum to the cytosol.Cellular microbiology · 2019Article
- Review
- Humanised monoclonal antibodies neutralise pertussis toxin by receptor blockade and reduced retrograde trafficking.Cellular microbiology · 2018Article
- Article
- Thermal Unfolding of the Pertussis Toxin S1 Subunit Facilitates Toxin Translocation to the Cytosol by the Mechanism of Endoplasmic Reticulum-Associated Degradation.Infection and immunity · 2016Article
- The NarE protein of Neisseria gonorrhoeae catalyzes ADP-ribosylation of several ADP-ribose acceptors despite an N-terminal deletion.FEMS microbiology letters · 2016Article
- Intracellular disassembly and activity of pertussis toxin require interaction with ATP.Pathogens and disease · 2016Article
- In vitro assays to monitor the activity of Pseudomonas aeruginosa Type III secreted proteins.Methods in molecular biology (Clifton, N.J.) · 2014Article
- Detection of toxin translocation into the host cytosol by surface plasmon resonance.Journal of visualized experiments : JoVE · 2012Article
- Review
- The decoupling of Smoothened from Galphai proteins has little effect on Gli3 protein processing and Hedgehog-regulated chick neural tube patterning.Developmental biology · 2008Article
- Evading the proteasome: absence of lysine residues contributes to pertussis toxin activity by evasion of proteasome degradation.Infection and immunity · 2007Article
- The pertussis toxin S1 subunit is a thermally unstable protein susceptible to degradation by the 20S proteasome.Biochemistry · 2006Article
- ADP-ribosylating and vacuolating cytotoxin of Mycoplasma pneumoniae represents unique virulence determinant among bacterial pathogens.Proceedings of the National Academy of Sciences of the United States of America · 2006Article
- Molecular pathogenesis, epidemiology, and clinical manifestations of respiratory infections due to Bordetella pertussis and other Bordetella subspecies.Clinical microbiology reviews · 2005Review
- Proteolytic cleavage of pertussis toxin S1 subunit is not essential for its activity in mammalian cells.BMC microbiology · 2005Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Pertussis toxin (PT)-catalyzed ADP-ribosylation of target proteins in intact Chinese hamster ovary (CHO) cells was evaluated with an in vitro ADP-ribosylation assay. In this assay, a postnuclear supernatant was prepared from CHO cells and used as a source of PT-sensitive target proteins for in vitro [32P[ADP-ribosylation. The postnuclear supernatant contained three proteins that were ADP-ribosylated in vitro, with apparent molecular masses of 50, 45, and 42 kDa. The 42- and 45-kDa proteins were membrane associated, while the 50-kDa protein was soluble. Following PT treatment of CHO cells, the 42- and 45-kDa proteins were not available for in vitro ADP-ribosylation, while the soluble 50-kDa protein remained available for in vitro ADP-ribosylation. The decrease in the availability of the 42- and 45-kDa proteins to in vitro ADP-ribosylation was proportional to the PT concentration and time of incubation with CHO cells. Western immunoblot analysis showed that extracts from PT-treated CHO cells and control CHO cells possessed equivalent amounts of two proteins that were recognized by anti-Gi protein antiserum. The two proteins recognized by anti-Gi protein antiserum from PT-treated cells migrated with higher apparent molecular weights than the two proteins from control cells. This was consistent with the in vivo ADP-ribosylation of the two proteins by PT.(ABSTRACT TRUNCATED AT 250 WORDS)
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