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- W2140293166 abstract "Abstract Chimeric protein toxins that act selectively on cells expressing a designated receptor may serve as investigational probes and/or antitumor agents. Here, we report use of the enzyme sortase A (SrtA) to create four chimeric toxins designed to selectively kill cells bearing the tumor marker HER2. We first expressed and purified: (i) a receptor recognition-deficient form of diphtheria toxin that lacks its receptor-binding domain and (ii) a mutated, receptor-binding–deficient form of anthrax-protective antigen. Both proteins carried at the C terminus the sortase recognition sequence LPETGG and a H6 affinity tag. Each toxin protein was mixed with SrtA plus either of two HER2-recognition proteins—a single-chain antibody fragment or an Affibody—both carrying an N-terminal G5 tag. With wild-type SrtA, the fusion reaction between the toxin and receptor-recognition proteins approached completion only after several hours, whereas with an evolved form of the enzyme, SrtA*, the reaction was virtually complete within 5 minutes. The four fusion toxins were purified and shown to kill HER2-positive cells in culture with high specificity. Sortase-mediated ligation of binary combinations of diverse natively folded proteins offers a facile way to produce large sets of chimeric proteins for research and medicine. Mol Cancer Ther; 12(10); 2273–81. ©2013 AACR." @default.
- W2140293166 created "2016-06-24" @default.
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- W2140293166 date "2013-10-01" @default.
- W2140293166 modified "2023-09-29" @default.
- W2140293166 title "Receptor-Directed Chimeric Toxins Created by Sortase-Mediated Protein Fusion" @default.
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- W2140293166 doi "https://doi.org/10.1158/1535-7163.mct-13-0358" @default.
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