Expression and purification of Arisaema heterophyllum agglutinin in Escherichia coli.
Recombinant Arisaema heterophyllum agglutinin (AHA) was expressed in Escherichia coli as N-terminal His-tagged fusions. After induction with isopropylthio-beta-D-galactoside, the recombinant AHA was purified by metal-affinity chromatography. The purified AHA protein was incorporated into artificial diet at 0.1% (w/v) concentration in insect bioassay trial and the result showed that artificial diet containing AHA could significantly inhibit the growth of the third-instar nymphs of peach potato aphid (Myzus persicae). This study suggested that AHA could be an effective candidate for the control of peach potato aphid, one of the most serious sap-sucking insect pests causing significant yield loss of crops.
Zhao
Xiuyun
X
State Key Laboratory of Genetic Engineering, School of Life Sciences, Morgan-Tan International Center for Life Sciences, Fudan University, Shanghai 200433, People's Republic of China.
Chen
Zhonghai
Z
Lin
Juan
J
Kong
Weiwen
W
Sun
Xiaofen
X
Tang
Kexuan
K
D000373:Agglutinins / Q000096:biosynthesis* / Q000302:isolation & purification / Q000494:pharmacology; D000818:Animals; D001042:Aphids / Q000187:drug effects; D031057:Arisaema / Q000737:chemistry*; D018556:Crops, Agricultural / Q000469:parasitology; D004926:Escherichia coli / Q000235:genetics* / Q000378:metabolism; D005822:Genetic Vectors; D009758:Nymph / Q000187:drug effects; D011993:Recombinant Fusion Proteins / Q000096:biosynthesis*; D036401:Toxicity Tests, Chronic
D000373:Agglutinins; D011993:Recombinant Fusion Proteins