ArticleInfection and immunity1998
Activity of the mitogenic Pasteurella multocida toxin requires an essential C-terminal residue.
Article in Infection and immunity, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 49 citations in OpenAlex.
- CXCL8 Knockout: A Key to ResistingInternational journal of molecular sciences · 2024Article
- In Vivo Targets ofInternational journal of molecular sciences · 2020Article
- Selective Membrane Redistribution and Depletion of Gαq-Protein by Pasteurella multocida Toxin.Toxins · 2016Article
- The actions of Pasteurella multocida toxin on neuronal cells.Neuropharmacology · 2014Article
- What a difference a Dalton makes: bacterial virulence factors modulate eukaryotic host cell signaling systems via deamidation.Microbiology and molecular biology reviews : MMBR · 2013Review
- Pasteurella multocida toxin as a transporter of non-cell-permeating proteins.Infection and immunity · 2013Article
- Substrate specificity of Pasteurella multocida toxin for α subunits of heterotrimeric G proteins.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2013Article
- Modification of heterotrimeric G-proteins in Swiss 3T3 cells stimulated with Pasteurella multocida toxin.PloS one · 2012Article
- Pasteurella multocida toxin-stimulated osteoclast differentiation is B cell dependent.Infection and immunity · 2011Article
- Characterization of the membrane-targeting C1 domain in Pasteurella multocida toxin.The Journal of biological chemistry · 2010Article
- Expression of 4 truncated fragments of Pasteurella multocida toxin and their immunogenicity.Canadian journal of veterinary research = Revue canadienne de recherche veterinaire · 2009Article
- Pasteurella multocida toxin activation of heterotrimeric G proteins by deamidation.Proceedings of the National Academy of Sciences of the United States of America · 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
- Crystal structures reveal a thiol protease-like catalytic triad in the C-terminal region of Pasteurella multocida toxin.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- Histidine Residues at the Active Site of the Pasteurella multocida Toxin.The open biochemistry journal · 2007Article
- Crystallization and preliminary crystallographic studies of the Pasteurella multocida toxin catalytic domain.Acta crystallographica. Section F, Structural biology and crystallization communications · 2006Article
- Localization of functional domains of the mitogenic toxin of Pasteurella multocida.Infection and immunity · 2001Article
- Escherichia coli cytotoxic necrotizing factor and Pasteurella multocida toxin induce focal adhesion kinase autophosphorylation and Src association.Infection and immunity · 2001Article
- Biological activity of a C-terminal fragment of Pasteurella multocida toxin.Infection and immunity · 2001Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Pasteurella multocida toxin (PMT) is a potent mitogen that also affects bone resorption. PMT acts intracellularly and is therefore postulated to have several domains involved in different aspects of its function. The toxin contains eight cysteine residues. Mutants with individual substitutions for each of these residues were constructed, and the effects of these on the biological activity of the toxin were determined by cultured-cell assays. Only the most C-terminal of the eight cysteines (C1165) was essential for full activity, although mutation of the cysteine residue at position 1159 caused a slight but reproducible loss of potency. In animal challenge experiments, mutant toxin (C1165S) was not toxic to piglets, even at doses exceeding a lethal dose of active PMT 1, 000-fold. The mutant and wild-type toxins displayed identical purification characteristics, similar susceptibility to proteolytic digestion, and circular dichroism profiles, which indicated that no gross structural changes had taken place. The function of the essential C1165 residue is not yet known, although its most likely role is an enzymatic one at or near the catalytic center of the toxin.
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