Pseudomonas exotoxin: chimeric toxins.

I Pastan; D FitzGerald

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PubMed · 2504717

Pseudomonas exotoxin: chimeric toxins.

I Pastan·D FitzGerald

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Abstract

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.

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ADP Ribose Transferases Bacterial Toxins Chimera Exotoxins Genes Genes, Bacterial Mutation Pseudomonas aeruginosa Virulence Factors Pseudomonas aeruginosa Exotoxin A Journal Article Review

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I Pastan, D FitzGerald. 1989-09-15. Pseudomonas exotoxin: chimeric toxins.. https://pubmed.ncbi.nlm.nih.gov/2504717/

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