Expression and purification of Zantedeschia aethiopica agglutinin in Escherichia coli.
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.
Lin
Ling
L
State Key Laboratory of Genetic Engineering, School of Life Sciences, Fudan University, Shanghai, People's Republic of China. beconfidante@gmail.com
Liu
Xue-Fen
XF
Hu
Ling-Chuan
LC
Zhou
Yin
Y
Sun
Xiao-Fen
XF
Tang
Ke-Xuan
KX
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*
D000373:Agglutinins; D000900:Anti-Bacterial Agents