ArticleInfection and immunity2001
Biological activity of a C-terminal fragment of Pasteurella multocida toxin.
Article in Infection and immunity, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
27 citing papers in PubMed, 58 citations in OpenAlex.
- Genome wide CRISPR screen for Pasteurella multocida toxin (PMT) binding proteins reveals LDL Receptor Related Protein 1 (LRP1) as crucial cellular receptor.PLoS pathogens · 2022Article
- Salmonella Typhimurium effector SseI inhibits chemotaxis and increases host cell survival by deamidation of heterotrimeric Gi proteins.PLoS pathogens · 2018Article
- The two-pore channel TPC1 is required for efficient protein processing through early and recycling endosomes.Scientific reports · 2017Article
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- Cytotoxicity of the Vibrio vulnificus MARTX toxin effector DUF5 is linked to the C2A subdomain.Proteins · 2014Article
- 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
- Pasteurella multocida toxin prevents osteoblast differentiation by transactivation of the MAP-kinase cascade via the Gα(q/11)--p63RhoGEF--RhoA axis.PLoS pathogens · 2013Article
- Protective immunity conferred by the C-terminal fragment of recombinant Pasteurella multocida toxin.Clinical and vaccine immunology : CVI · 2012Article
- Pasteurella multocida toxin interaction with host cells: entry and cellular effects.Current topics in microbiology and immunology · 2012Review
- Characterization of the membrane-targeting C1 domain in Pasteurella multocida toxin.The Journal of biological chemistry · 2010Article
- Recent insights into Pasteurella multocida toxin and other G-protein-modulating bacterial toxins.Future microbiology · 2010Review
- Pasteurella multocida toxin activates various heterotrimeric G proteins by deamidation.Toxins · 2010Article
- The Salmonella SPI2 effector SseI mediates long-term systemic infection by modulating host cell migration.PLoS pathogens · 2009Article
- 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
- Lgt: a family of cytotoxic glucosyltransferases produced by Legionella pneumophila.Journal of bacteriology · 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
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The protein toxin of Pasteurella multocida PMT is a potent mitogen and activator of phospholipase Cbeta. In this study different toxin fragments were investigated. A C-terminal fragment encompassing amino acids 581 through 1285 (PMT581C) was constructed, which was inactive toward intact embryonic bovine lung (EBL) cells after addition to culture medium but caused reorganization of the actin cytoskeleton and rounding up of cells when introduced into the cells by electroporation. As the holotoxin, the toxin fragment PMT581C induced an increase in total inositol phosphate levels after introduction into the cell by electroporation. A C-terminal fragment shorter than PMT581C as well as N-terminal fragments were inactive. Exchange of cysteine-1165 for serine in the holotoxin resulted in a complete loss of the ability to increase inositol phosphate levels. Correspondingly, the mutated toxin fragment PMT581C.C1165S was inactive after cell introduction by electroporation, suggesting an essential role of Cys-1165 in the biological activity of the toxin.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.