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Isolation and molecular cloning of a novel type 2 ribosome-inactivating protein with an inactive B chain from elderberry (Sambucus nigra) bark



Isolation and molecular cloning of a novel type 2 ribosome-inactivating protein with an inactive B chain from elderberry (Sambucus nigra) bark



Journal of Biological Chemistry 272(13): 8353-8360



One of the predominant proteins in the bark of elderberry (Sambucus nigra) has been identified as a novel type 2 ribosome-inactivating protein that exhibits a normal RNA N-glycosidase activity, but is devoid of carbohydrate binding activity. Sequence analysis of the corresponding cDNA clones revealed a striking homology to the previously cloned bark lectins from elderberry, suggesting that the new protein is a lectin-related protein. Molecular modeling of the protein confirmed that its A chain is fully active, whereas its B chain contains two functionally inactive carbohydrate-binding sites. These findings not only demonstrate for the first time the occurrence of a type 2 ribosome-inactivating protein with an inactive B chain, but also offer interesting perspectives for the synthesis of immunotoxins with an improved selectivity.

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Accession: 002880746

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PMID: 9079659

DOI: 10.1074/jbc.272.13.8353


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