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  • Title: Cloning and expression of mistletoe lectin III B-subunit.
    Author: Pevzner IB, Agapov II, Pfueller U, Pfueller K, Maluchenko NV, Moisenovich MM, Tonevitsky AG, Kirpichnikov MP.
    Journal: Biochemistry (Mosc); 2005 Mar; 70(3):306-15. PubMed ID: 15823085.
    Abstract:
    Aqueous extracts of mistletoe (Viscum album L.) contain toxic proteins (lectins) MLI (viscumin), MLII, and MLIII. We previously cloned the gene encoding MLIII precursor. In the present study, a gene fragment encoding the carbohydrate-binding subunit of mistletoe toxic lectin MLIII was cloned and expressed in Escherichia coli cells. The structure and immunochemical properties of recombinant MLIII B-subunit were investigated using a panel of monoclonal antibodies against ML-toxins. Sugar-binding activity of recombinant MLIII B-subunit was determined by ELISA. Amino acid sequence analysis of the cloned MLIII compared with known mistletoe toxins and other ribosome-inactivating type II proteins (ricin, abrin a, and nigrin b B-subunits) revealed essential features of the recombinant MLIIIB primary structure that could determine sugar specificity of the lectin as well as immunomodulating and anti-tumor properties of mistletoe extracts.
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