Toxicity and cytotoxicity of nigrin b, a two-chain ribosome-inactivating protein from Sambucus nigra : comparison with ricin |
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Authors: | Maria Giulia Battelli Lucía Citores Laura Buonamici J. Miguel Ferreras F. M. de Benito Fiorenzo Stirpe Thomás Girbés |
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Affiliation: | (1) Dipartimento di Patologia Sperimentale, Via S. Giacomo 14, I-40126 Bologna, Italy, IT;(2) Departemento de Bioquímica, Biología Molecular y Fisiologia, Facultad de Ciencias, Universidad de Valladolid, 47005 Valladolid, Spain, ES |
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Abstract: | Nigrin b, a lectin isolated from the bark of elderberry (Sambucus nigra L.), has structure and enzymatic activity similar to that of ricin and other type 2 ribosome-inactivating proteins (RIPs), and yet is much less toxic to cells and animals. In an attempt to explain this difference, we studied (1) the cytotoxicity of both lectins at 18 and 37 °C, and in the presence of substances interfering with intracellular routing, and (2) the binding of nigrin b to, and its uptake and degradation by HeLa cells, in parallel with ricin. As compared with the latter, (1) less nigrin b was bound and more was degraded by cells, with a resulting lower concentration remaining inside the cells, and (2) there is evidence for a different intracellular routing followed by the two lectins. These results may explain at least partly the different cytotoxicity and consequently the lower toxicity to mice of nigrin b compared with ricin. Received: 5 September 1996 / Accepted: 30 October 1996 |
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Keywords: | Nigrin b Ribosome-inactivating proteins Lectins HeLa cells Toxicity to mice |
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