Isolation, cDNA cloning, biological properties, and carbohydrate binding specificity of sieboldin-b, a type II ribosome-inactivating protein from the bark of Japanese elderberry (Sambucus sieboldiana).

A type II ribosome-inactivating protein (RIP) was isolated from the bark tissue of Japanese elderberry (Sambucus sieboldiana) and named sieboldin-b. Sieboldin-b is a heterodimeric protein consisting of 27- and 33-kDa subunits and showed strong ribosome-inactivating activity in vitro but did not show in vivo toxicity. The amino acid sequence of sieboldin-b deduced from the structure of the cDNA showed that both subunits of sieboldin-b are encoded on a single precursor polypeptide. Sieboldin-b has a structure homologous with the Neu5Ac(alpha 2-6)Gal/GalNAc-specific bark lectin from S. sieboldiana (SSA) and also typical type II RIPs such as ricin and abrin. Detailed analyses of carbohydrate binding properties of sieboldin-b revealed that sieboldin-b binds to Gal/GalNAc, similar to ricin/abrin, in spite of its highly homologous structure with SSA. The biological properties of these toxins/lectins are compared, and the possible explanation for such diversity is discussed.