Pseudomonas exotoxin: chimeric toxins.
Pseudomonas exotoxin binds to and enters cells by receptor-mediated endocytosis. Within the cell it requires exposure to low pH to enable it to translocate to the cell cytoplasm where it inhibits protein synthesis by ADP-ribosylating elongation factor 2. The toxin has three main structural domains whose functions are: Ia, cell binding; II, translocation; and III, ADP-ribosylation. Key amino acids have been identified within each domain that are required for the function of the toxin. Chimeric toxins were made originally by using chemical cross-linking reagents to couple Pseudomonas exotoxin (or other toxins) to cell-binding proteins. More recently, a variety of Pseudomonas exotoxin-related chimeric toxins have been made by gene fusion technology. These chimeric toxins may be useful clinically for treating various diseases and experimentally for understanding receptor function.
Pastan
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I
Laboratory of Molecular Biology, National Cancer Institute, Bethesda, Maryland 20892.
FitzGerald
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D
D036002:ADP Ribose Transferases; D001427:Bacterial Toxins; D002678:Chimera; D005098:Exotoxins / Q000235:genetics*; D005796:Genes; D005798:Genes, Bacterial; D009154:Mutation; D011550:Pseudomonas aeruginosa / Q000235:genetics*; D037521:Virulence Factors; D000097668:Pseudomonas aeruginosa Exotoxin A
D036002:ADP Ribose Transferases; D001427:Bacterial Toxins; D005098:Exotoxins; D037521:Virulence Factors; D000097668:Pseudomonas aeruginosa Exotoxin A