ArticleToxicon : official journal of the International Society on Toxinology2008
Application of intact cell-based NFAT-beta-lactamase reporter assay for Pasteurella multocida toxin-mediated activation of calcium signaling pathway.
Article in Toxicon : official journal of the International Society on Toxinology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 10 citations in OpenAlex.
- The T-type voltage-gated CaVirulence · 2025Article
- From GFP to β-lactamase: advancing intact cell imaging for toxins and effectors.Pathogens and disease · 2015Review
- Identification and characterization of monoclonal antibodies against the ORFV059 protein encoded by Orf virus.Virus genes · 2012Article
- Pasteurella multocida toxin interaction with host cells: entry and cellular effects.Current topics in microbiology and immunology · 2012Review
- Cellular and molecular action of the mitogenic protein-deamidating toxin from Pasteurella multocida.The FEBS journal · 2011Review
- Recent insights into Pasteurella multocida toxin and other G-protein-modulating bacterial toxins.Future microbiology · 2010Review
- 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
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Pasteurella multocida toxin (PMT) stimulates and subsequently uncouples phospholipase C beta1 (PLCbeta1) signal transduction through its selective action on the alpha subunit of the Gq-protein. Here, we describe the application of an NFAT-beta-lactamase reporter assay as a functional readout for PMT-induced activation of the Gq-protein-coupled PLCbeta1-IP(3)-Ca(2+) signaling pathway. Use of the NFAT-beta-lactamase reporter assay with a cell-permeable fluorogenic substrate provides high sensitivity due to the absence of endogenous beta-lactamase activity in mammalian cells. This assay system was optimized for cell density, dose and time exposure of PMT stimulation. It is suited for quantitative characterization of PMT activity in mammalian cells and for use as a high-throughput screening method for PMT deletion and point mutants suitable for vaccine development. This method has application's for diagnostic screening of clinical isolates of toxinogenic P. multocida.
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