Aspergillus Restrictus Restrictocin Dimer (DAG4643)

Aspergillus Restrictus Restrictocin Dimer, natural protein from Aspergillus

Product Overview
Aspergillus restrictus Restrictocin Dimer
Nature
Native
Tag/Conjugate
Unconjugated
Procedure
None
Format
freeze dried
Concentration
Trace amount of protein contaminants
Preservative
None
Storage
2-8°C short term, -20°C long term
Introduction
Restrictocin is a 149 amino acid ribonucleolytic toxin produced by the fungus Aspergillus. specifically cleaves. It is a member of a group of fungal ribosome inactivating proteins that cleave a single phosphodiester bond within 28S rRNA, which results in a potent inhibition of protein synthesis in eukaryotic cells. Fusion proteins between Restrictocin and monoclonal antibodies have been used as an immunotoxin directed against human carcinoma cells.
Keywords
Restrictocin; Aspergillus restrictus Restrictocin; Aspergillus restrictus; Aspergillus

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References


Construction, expression and characterization of chimaeric toxins containing the ribonucleolytic toxin restrictocin: Intracellular mechanism of action

BIOCHEMICAL JOURNAL

Authors: Rathore, D; Batra, JK

Restrictocin is a ribonucleolytic toxin produced by the fungus Aspergillus restrictus. Two chimaeric toxins containing restrictocin directed at the human transferrin receptor have been constructed. Anti-TFR(scFv)-restrictocin is encoded by a gene produced by fusing the DNA encoding a single-chain antigen-combining region (scFv) of a monoclonal antibody, directed at the human transferrin receptor, at the 5' end of that encoding restrictocin. The other chimaeric toxin, restrictocin-anti-TFR(scFv),is encoded by a gene fusion containing the DNA encoding the single-chain antigen-combining region of antibody to human transferrin receptor at the 3' end of the DNA encoding restrictocin. These gene fusions were expressed in Escherichia coli, and fusion proteins purified from the inclusion bodies by simple chromatography techniques to near-homogeneity. The two chimaeric toxins were found to be equally active in inhibiting protein synthesis in a cell-free in vitro translation assay system. The chimaeric toxins were selectively toxic to the target cells in culture with potent cytotoxic activities. However, restrictocin-anti-TFR(scFv) was more active than anti-TFR(scFv)-restrictocin on all cell lines studied. By using protease and metabolic inhibitors, it can be shown that, to manifest their cytotoxic activity, the restrictocin-containing chimaeric toxins need to be proteolytically processed intracellularly and the free toxin or a fragment thereof thus generated is translocated to the target via a route involving the Golgi apparatus.

Ribotoxins are a more widespread group of proteins within the filamentous fungi than previously believed

TOXICON

Authors: Martinez-Ruiz, A; Kao, R; Davies, J; del Pozo, AM

alpha-Sarcin, restrictocin and mitogillin are the best known members of the family of fungal ribotoxins. In recent years, new members of this family have been discovered and characterised. In this work, we study the occurrence of ribotoxins among different species of fungi. The presence of ribotoxins has been identified in some new species by means of genetic studies, as well as expression and activity assays. The ribotoxin genes have been partially sequenced, and demonstrate a high degree of similarity. These studies demonstrate that these toxins are more widespread than previously considered. This is surprising, considering the ribotoxins are such specific and potent toxins, of unknown biological function. These studies confirm the hypothesis that these proteins are naturally engineered toxins derived from ribonucleases of broad substrate specificity. (C) 1999 Elsevier Science Ltd. All rights reserved.

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