title: Expression and purification of Zantedeschia aethiopica agglutinin in Escherichia coli.
abstract: Recombinant Zantedeschia aethiopica agglutinin (ZAA) was expressed in Escherichia coli as N-terminal His-tagged fusion. After induction with isopropylthio-beta-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.
authors: State Key Laboratory of Genetic Engineering, School of Life Sciences, Fudan University, Shanghai, People's Republic of China. beconfidante@gmail.com
authors: Ling
authors: L
authors: Lin
authors: Xue-Fen
authors: XF
authors: Liu
authors: Ling-Chuan
authors: LC
authors: Hu
authors: Yin
authors: Y
authors: Zhou
authors: Xiao-Fen
authors: XF
authors: Sun
authors: Ke-Xuan
authors: KX
authors: Tang
mesh_terms: D000373:Agglutinins / Q000235:genetics / Q000302:isolation & purification* / Q000378:metabolism* / Q000494:pharmacology; D000900:Anti-Bacterial Agents / Q000302:isolation & purification / Q000378:metabolism / Q000494:pharmacology; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism*; D015870:Gene Expression; D005822:Genetic Vectors / Q000235:genetics; D050296:Microbial Viability / Q000187:drug effects; D031064:Zantedeschia / Q000235:genetics / Q000378:metabolism*
chemical_list: D000373:Agglutinins; D000900:Anti-Bacterial Agents