ArticleInfection and immunity1999
Localization of the intracellular activity domain of Pasteurella multocida toxin to the N terminus.
Article in Infection and immunity, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 27 citations in OpenAlex.
- CXCL8 Knockout: A Key to ResistingInternational journal of molecular sciences · 2024Article
- A protein-based subunit vaccine with biological adjuvants provides effective protection against Pasteurella multocida in pigs.Veterinary research · 2023Article
- Pasteurella multocida toxin activates various heterotrimeric G proteins by deamidation.Toxins · 2010Article
- Expression of 4 truncated fragments of Pasteurella multocida toxin and their immunogenicity.Canadian journal of veterinary research = Revue canadienne de recherche veterinaire · 2009Article
- The C3 domain of Pasteurella multocida toxin is the minimal domain responsible for activation of Gq-dependent calcium and mitogenic signaling.Protein science : a publication of the Protein Society · 2008Article
- Application of intact cell-based NFAT-beta-lactamase reporter assay for Pasteurella multocida toxin-mediated activation of calcium signaling pathway.Toxicon : official journal of the International Society on Toxinology · 2008Article
- Distinct signaling functions for Shc isoforms in the heart.The Journal of biological chemistry · 2006Article
- Localization of functional domains of the mitogenic toxin of Pasteurella multocida.Infection and immunity · 2001Article
- Biological activity of a C-terminal fragment of Pasteurella multocida toxin.Infection and immunity · 2001Article
- Physical and functional interactions of Galphaq with Rho and its exchange factors.The Journal of biological chemistry · 2001Article
- Epitope mapping of monoclonal antibodies capable of neutralizing cytotoxic necrotizing factor type 1 of uropathogenic Escherichia coli.Infection and immunity · 2001Article
- Differential modulation and subsequent blockade of mitogenic signaling and cell cycle progression by Pasteurella multocida toxin.Infection and immunity · 2000Article
- Identification of functional domains of Bordetella dermonecrotizing toxin.Infection and immunity · 1999Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
We have shown that Pasteurella multocida toxin (PMT) directly causes transient activation of Gqalpha protein that is coupled to phosphatidylinositol-specific phospholipase Cbeta1 in Xenopus oocytes (B. A. Wilson, X. Zhu, M. Ho, and L. Lu, J. Biol. Chem. 272:1268-1275, 1997). We found that antibodies directed against an N-terminal peptide of PMT inhibited the toxin-induced response in Xenopus oocytes, but antibodies against a C-terminal peptide did not. To test whether the intracellular activity domain of PMT is localized to the N terminus, we conducted a deletion mutational analysis of the PMT protein, using the Xenopus oocyte system as a means of screening for toxin activity. Using PCR and conventional cloning techniques, we cloned from a toxinogenic strain of P. multocida the entire toxA gene, encoding the 1,285-amino-acid PMT protein, and expressed the recombinant toxin as a His-tagged fusion protein in Escherichia coli. We subsequently generated a series of N-terminal and C-terminal deletion mutants and expressed the His-tagged PMT fragments in E. coli. These proteins were screened for cytotoxic activity on cultured Vero cells and for intracellular activity in the Xenopus oocyte system. Only the full-length protein without the His tag exhibited activity on Vero cells. The full-length PMT and N-terminal fragments containing the first 500 residues elicited responses in oocytes, but the C-terminal 780 amino acid fragment did not. Our results confirm that the intracellular activity domain of PMT is localized to the N-terminal 500 amino acids of the protein and that the C terminus is required for entry into cells.
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