Tribolium castaneum immune defense genes are differentially expressed in response to Bacillus thuringiensis toxins sharing common receptor molecules and exhibiting disparate toxicity

被引:25
作者
Contreras, Estefania [1 ]
Benito-Jardon, Maria [1 ]
Jose Lopez-Galiano, M. [1 ]
Dolores Real, M. [1 ]
Rausell, Carolina [1 ]
机构
[1] Univ Valencia, Fac Ciencias Biol, Dept Genet, Valencia, Spain
关键词
Tribolium castaneum; Bacillus thuringiensis; Defensin; Apolipophorin III; Innate immunity; Cry toxin receptors; BRUSH-BORDER MEMBRANE; ANTIMICROBIAL PEPTIDES; FUNCTIONAL-SIGNIFICANCE; DELTA-ENDOTOXIN; MANDUCA-SEXTA; SUSCEPTIBILITY; PROTEIN; IDENTIFICATION; CADHERIN; DOMAIN;
D O I
10.1016/j.dci.2015.02.005
中图分类号
S9 [水产、渔业];
学科分类号
0908 ;
摘要
In Tribolium castaneum larvae we have demonstrated by RNA interference knockdown that the Bacillus thuringiensis Cry3Ba toxin receptors Cadherin-like and Sodium solute symporter proteins are also functional receptors of the less active Cry3Aa toxin. Differences in susceptibility to B. thuringiensis infection might not only rely on toxin-receptor interaction but also on host defense mechanisms. We compared the expression of the immune related genes encoding Apolipophorin-Ill and two antimicrobial peptides, Defensin3 and Defensin2 after B. thuringiensis challenge. All three genes were up-regulated following Cry3Ba spore-crystal intoxication whereas only Defensins gene expression was induced upon Cry3Aa spore-crystal treatment, evidencing a possible association between host immune response and larval susceptibility to B. thuringiensis. We assessed the antimicrobial activity spectra of T. castaneum defensins peptide fragments and found that a peptide fragment of Defensin3 was effective against the human microbial pathogens, Escherichia coil, Staphylococcus aureus and Candida albicans, being S. aureus the most susceptible one. (C) 2015 Elsevier Ltd. All rights reserved.
引用
收藏
页码:139 / 145
页数:7
相关论文
共 44 条
[41]   Enhanced toxicity of Bacillus thuringiensis Cry3A δ-endotoxin in coleopterans by mutagenesis in a receptor binding loop [J].
Wu, SJ ;
Koller, CN ;
Miller, DL ;
Bauer, LS ;
Dean, DH .
FEBS LETTERS, 2000, 473 (02) :227-232
[42]   Functional significance of loops in the receptor binding domain of Bacillus thuringiensis CryIIIA delta-endotoxin [J].
Wu, SJ ;
Dean, DH .
JOURNAL OF MOLECULAR BIOLOGY, 1996, 255 (04) :628-640
[43]   A rapid and simple flour-disk bioassay for testing substances active against stored-product insects [J].
Xie, YS ;
Bodnaryk, RP ;
Fields, PG .
CANADIAN ENTOMOLOGIST, 1996, 128 (05) :865-875
[44]   Synergistic interactions between mammalian antimicrobial defense peptides [J].
Yan, H ;
Hancock, REW .
ANTIMICROBIAL AGENTS AND CHEMOTHERAPY, 2001, 45 (05) :1558-1560