Cloning and expression of mistletoe lectin III B-subunit |
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Authors: | I?B?Pevzner I?I?Agapov U?Pfueller K?Pfueller N?V?Maluchenko M?M?Moisenovich Email author" target="_blank">A?G?TonevitskyEmail author M?P?Kirpichnikov |
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Institution: | (1) Faculty of Biology, Lomonosov Moscow State University, 119899 Moscow, Russia;(2) Institute of Phytochemistry, University of Witten/Herdecke, Stockumer Str. 10, D-58448 Witten, Germany |
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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.Translated from Biokhimiya, Vol. 70, No. 3, 2005, pp. 378–389.Original Russian Text Copyright © 2005 by Pevzner, Agapov, Pfueller, Pfueller, Maluchenko, Moisenovich, Tonevitsky, Kirpichnikov. |
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Keywords: | mistletoe toxic lectin recombinant MLIII B-subunit monoclonal antibody |
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