Tumor protease-activated, pore-forming toxins from a combinatorial library.

Journal article

We describe a library of two-chain molecular complementation mutants of staphylococcal alpha-hemolysin that features a combinatorial cassette encoding thousands of protease recognition sites in the central pore-forming domain. The cassette is flanked by a peptide extension that inactivates the protein. We screened the library to identify alpha-hemolysins that are highly susceptible to activation by cathepsin B, a protease that is secreted by certain metastatic tumor cells. Toxins obtained by ...

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Authors: Panchal, R; Cusack, E; Cheley, S; Bayley, J

• Publication status: Published
• Journal: Nature biotechnology
• Volume: 14
• Issue: 7
• Pages: 852-856
• Publication date: 1996-07-01
• DOI: 10.1038/nbt0796-852
• EISSN: 1546-1696
• ISSN: 1087-0156
• Language: English
• Keywords: Amino Acid Sequence; Mutagenesis; Humans; Hemolysin Proteins; Exotoxins; Neoplasms; Bacterial Toxins; Base Sequence; DNA Primers; Peptide Library; Cysteine Endopeptidases; Cathepsin B