AI Article Synopsis
- Saporin is a ribosome-inactivating protein commonly used to create immunotoxins.
- A mutated version, Cys255sap-3, was developed by adding a cysteine residue and showed similar toxicity levels as the original saporin and its isomer in protein synthesis assays.
- This single cysteine allows for consistent and effective antibody conjugation while maintaining the protein's activity.
Article Abstract
Saporin, a ribosome inactivating protein is widely used for immunotoxin construction. Here we describe a mutation of saporin (sap)-3 DNA by introducing a cysteine residue, followed by protein expression and purification by ion exchange chromatography. The purified Cys255sap-3, sap-3 isomer and commercially purchased saporin, were tested for toxicity using assays measuring inhibition for protein synthesis. The IC(50) values showed that the toxicity of the Cys255sap-3 is equivalent to the sap-3 isomer and commercial saporin. Reactivity of Cys255sap-3 was confirmed by labeling with a thio-specific fluorescent probe as well as conjugation with a nonspecific mouse IgG. We have found that a single cysteine within saporin provides a method for antibody conjugation that ensures a uniform and reproducible modification of a saporin variant retaining high activity.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2719709 | PMC |
| http://dx.doi.org/10.1016/j.pep.2007.11.005 | DOI Listing |
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