Expression of various biotin-binding proteins in transgenic tobacco confers resistance to potato tuber moth, Phthorimaea operculella (Zeller) (fam. Gelechiidae)

被引:3
|
作者
Murray, Colleen [1 ]
Markwick, Ngaire P. [2 ]
Kaji, Ryohei [1 ]
Poulton, Joanne [2 ]
Martin, Harry [1 ]
Christeller, John T. [1 ]
机构
[1] New Zealand Inst Plant & Food Res Ltd, Manawatu Mail Ctr, Palmerston North 4442, New Zealand
[2] New Zealand Inst Plant & Food Res Ltd, Auckland, New Zealand
关键词
Avidin; Biotin; Insecticidal protein; Bioassay; Transgenic tobacco; CIRCULARLY PERMUTED AVIDINS; CHICKEN AVIDIN; BRADYRHIZOBIUM-JAPONICUM; INSECTICIDAL ACTIVITY; DEPENDENT ENZYMES; STREPTAVIDIN; PLANTS; PESTS; LEPIDOPTERA; SEQUENCES;
D O I
10.1007/s11248-010-9380-y
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
The high affinity biotin-binding proteins (BBPs) avidin and streptavidin are established insecticidal agents, effective against a range of insect pests. Earlier work showed that, when expressed in planta, full length avidin and a truncated form of streptavidin are highly insecticidal. More recently, a wide range of BBPs, found in diverse organisms or engineered for various biotechnological applications have been reported. However, their effectiveness as plant-based insecticides has not been established. Here we report in planta expression of three different genes, designed to produce BBP variant proteins in the vacuole. The first was mature full length chicken avidin, the second a circularly permuted dual chain chicken avidin, and the third was an avidin homologue, a native bradavidin from Bradyrhyzobium japonicum. All three proteins were expressed in Nicotiana tabacum (tobacco). The transgenic tobacco lines were healthy, phenotypically normal and, when subjected to bioassay, resistant to the important cosmopolitan pest, potato tuber moth (Phthorimaea operculella) larvae at concentrations of similar to 50 ppm.
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页码:1041 / 1051
页数:11
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