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Expression and purification of Zantedeschia aethiopica agglutinin in Escherichia  coli

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Abstract

Recombinant Zantedeschia aethiopica agglutinin (ZAA) was expressed in Escherichia coli as N-terminal His-tagged fusion. After induction with isopropylthio-β-d-galactoside (IPTG), the recombinant ZAA was purified by metal-affinity chromatography. The purified ZAA protein was applied in anti-fungal assay and the result showed that recombinant ZAA had anti-fungal activity towards leaf mold (Fulvia fulva), one of the most serious phytopathogenic fungi causing significant yield loss of crops. This study suggests that ZAA could be an effective candidate in genetic engineering of plants for the control of leaf mold.

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Acknowledgements

This work was supported by China National Transgenic Plant Research and Commercialization Project, China National High-Tech ‘863’ Program and Shanghai Science and Technology Committee.

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Authors and Affiliations

  1. State Key Laboratory of Genetic Engineering, School of Life Sciences, Fudan-SJTU-Nottingham Plant Biotechnology R&D Center, Morgan-Tan International Center for Life Sciences, Fudan University, Shanghai, 200433, People′s Republic of China

    Ling Lin, Ling-Chuan Hu, Yin Zhou, Xiao-Fen Sun & Ke-Xuan Tang

  2. School of Agriculture and Food System, University of Melbourne, Parkville, VIC, 3010, Australia

    Xue-Fen Liu

  3. Plant Biotechnology Research Center, School of Agriculture and Biology, Fudan-SJTU-Nottingham Plant Biotechnology R&D Center, School of Life Sciences and Technology, Shanghai Jiao Tong University, Shanghai, 200030, China

    Ke-Xuan Tang

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  1. Ling Lin
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  2. Xue-Fen Liu
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  3. Ling-Chuan Hu
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  4. Yin Zhou
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  5. Xiao-Fen Sun
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Correspondence to Ke-Xuan Tang.

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Lin, L., Liu, XF., Hu, LC. et al. Expression and purification of Zantedeschia aethiopica agglutinin in Escherichia  coli . Mol Biol Rep 36, 437–441 (2009). https://doi.org/10.1007/s11033-007-9198-8

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  • DOI: https://doi.org/10.1007/s11033-007-9198-8

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