PMID: 9523712Apr 2, 1998Paper

Production and purification of active snowdrop lectin in Escherichia coli

European Journal of Biochemistry
M LongstaffW D Hamilton

Abstract

Recombinant snowdrop lectin was produced in Escherichia coli from a cDNA clone encoding mature Galanthus nivalis agglutinin. After induction with isopropylthio-beta-D-galactoside, inclusion bodies from E. coli were solubilised and the G. nivalis agglutinin purified by metal-affinity chromatography using a carboxy-terminal hexahistidine tag. The protein was refolded on the metal-affinity column prior to elution. After purification, the recombinant G. nivalis agglutinin agglutinated rabbit erythrocytes to a dilution similar to that determined for 'native' lectin purified from snowdrop, and showed similar specific binding to mannose. The toxicity of the recombinant G. nivalis agglutinin towards rice brown planthopper (Nilaparvata lugens) was shown to be similar to that of 'native' G. nivalis agglutinin when incorporated into an artificial diet. The recombinant G. nivalis agglutinin is thus functionally similar to 'native' snowdrop lectin.

Citations

Jul 26, 2003·Protein Expression and Purification·Patrick R StancombeJohn A Chaddock
Jul 8, 2009·Pakistan Journal of Biological Sciences : PJBS·Eduardo Armienta-AldanaSandra Viviana Laguna-Granados
Dec 26, 2007·Journal of Invertebrate Pathology·Qi GaofuZhao Xiuyun
Apr 26, 2012·Critical Reviews in Biotechnology·Carla OliveiraLucília Domingues
Jan 10, 2006·Journal of Plant Physiology·Xiuyun ZhaoKexuan Tang
Mar 29, 2018·Molecules : a Journal of Synthetic Chemistry and Natural Product Chemistry·Xiaoliang DuanRongqi Liang

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