Characterization of a new cry2Ab gene of Bacillus thuringiensis with high insecticidal activity against Plutella xylostella L.

2014 ◽  
Vol 30 (10) ◽  
pp. 2655-2662 ◽  
Author(s):  
Zhizhen Pan ◽  
Lian Xu ◽  
Yujing Zhu ◽  
Huai Shi ◽  
Zheng Chen ◽  
...  
Toxins ◽  
2020 ◽  
Vol 12 (10) ◽  
pp. 642
Author(s):  
Changlong Shu ◽  
Guixin Yan ◽  
Shizhi Huang ◽  
Yongxin Geng ◽  
Mario Soberón ◽  
...  

Scarabaeoidea and Chrysomeloidea insects are agriculture-destructive coleopteran pests. Few effective Bacillus thuringiensis (Bt) insecticidal proteins against these species have been described. Bt isolate BtSU4 was found to be active against coleopteran insects. Genome sequencing revealed two new cry8 genes in BtSU4, designated as cry8Ha1 and cry8Ia1. Both genes expressed a 135 kDa protoxin forming irregular shape crystals. Bioassays performed with Cry8Ha1 protoxin showed that it was toxic to both larvae and adult stages of Holotrichia parallela, also to Holotrichia oblita adults and to Anoplophora glabripennis larvae, but was not toxic to larval stages of H. oblita or Colaphellus bowringi. The Cry8Ia1 protoxin only showed toxicity against H. parallela larvae. After activation with chymotrypsin, the Cry8Ha1 activated toxin lost its insecticidal activity against H. oblita adults and reduced its activity on H. parallela adults, but gained toxicity against C. bowringi larvae, a Chrysomeloidea insect pest that feeds on crucifer crops. The chymotrypsin activated Cry8Ia1 toxin did not show toxicity to any one of these insects. These data show that Cry8Ha1 and Cry8Ia1 protoxin and activated toxin proteins have differential toxicity to diverse coleopteran species, and that protoxin is a more robust protein for the control of coleopteran insects.


BioControl ◽  
2018 ◽  
Vol 63 (6) ◽  
pp. 807-818 ◽  
Author(s):  
Ayda Khorramnejad ◽  
Reza Talaei-Hassanloui ◽  
Vahid Hosseininaveh ◽  
Yolanda Bel ◽  
Baltasar Escriche

PLoS ONE ◽  
2018 ◽  
Vol 13 (11) ◽  
pp. e0206813 ◽  
Author(s):  
Burcu Şahin ◽  
Joaquín Gomis-Cebolla ◽  
Hatice Güneş ◽  
Juan Ferré

2008 ◽  
Vol 47 (2) ◽  
pp. 222-227 ◽  
Author(s):  
Yang-Su Kim ◽  
Jong Yul Roh ◽  
Joong Nam Kang ◽  
Yong Wang ◽  
Hee Jin Shim ◽  
...  

2010 ◽  
Vol 104 (2) ◽  
pp. 90-96 ◽  
Author(s):  
Youjing Gong ◽  
Chongli Wang ◽  
Yihua Yang ◽  
Shuwen Wu ◽  
Yidong Wu

PeerJ ◽  
2019 ◽  
Vol 7 ◽  
pp. e7535
Author(s):  
Rashini Yasara Baragamaarachchi ◽  
Jayanetti Koralage Ramani Radhika Samarasekera ◽  
Ovitigala Vithanage Don Sisira Jagathpriya Weerasena ◽  
Kurt Lamour ◽  
Juan Luis Jurat-Fuentes

Background Biopesticides based on strains of the bacterium Bacillus thuringiensis (Bt) are used globally for effective and environmentally friendly pest control. The most serious threat to the sustainable use of these microbial pesticides is the development of resistance on targeted pests. Populations of Plutella xylostella (diamondback moth) have evolved field resistance to Bt pesticides at diverse locations worldwide. Discovery of novel Bt strains with varied toxin profiles that overcome resistance is one of the strategies to increase sustainability of Bt pesticides against P. xylostella. In this study, we report isolation and characterization of a Bt strain named AB1 from Sri Lanka displaying toxicity towards larvae of P. xylostella resistant to the commercial Bt pesticide Dipel. Methods Strains of Bt from diverse environments in Sri Lanka were evaluated for protein crystal production through Differential Interference Contrast (DIC) microscopic examination, and for insecticidal activity against P. xylostella in bioassays. The genome of the AB1 strain was sequenced by Hiseq Illumina sequencing to identify the insecticidal genes present in the genome and nano liquid chromatography followed by tandem mass spectrometry (nanoLC/MS/MS) of purified crystal proteins of AB1 was performed to identify the expressed insecticidal proteins. Multilocus sequence typing and Gyrase B gene sequence analyses were performed to identify the phylogenetic origin of the AB1 strain. Results The AB1 strain was identified as producing high levels of bipyramidal crystals and displaying insecticidal activity against susceptible and Dipel-resistant strains of P. xylostella. Multilocus sequence typing and phylogenetic analysis of the Gyrase B gene identified that AB1 belongs to the B. thuringiensis subsp. aizawai serotype. Comparative analysis of genomic and proteomic data showed that among the insecticidal protein coding genes annotated from the AB1 genome (cry1Aa, cry1Ca, cry1Da, cry1Ia, cry2Ab and cry9), Cry1Ca and Cry1Da toxins represented most of the toxin fraction in parasporal crystals from AB1. Overall findings warrant further development of B. thuringiensis subsp. aizawai AB1 strain as a pesticide to control P. xylostella.


2005 ◽  
Vol 51 (11) ◽  
pp. 988-995 ◽  
Author(s):  
Naoya Wasano ◽  
Hiroyuki Saitoh ◽  
Minoru Maeda ◽  
Akira Ohgushi ◽  
Eiichi Mizuki ◽  
...  

A novel δ-endotoxin gene from a lepidopteran-specific Bacillus thuringiensis serovar galleriae strain was cloned, and the full sequence of the cry gene was determined. The cloned 6.5-kb DNA fragment included the full sequence of the cry gene and three open reading frames located upstream of the cry gene. The gene, designated cry9Ec1, encodes a polypeptide of 1154 amino acid residues with a predicted molecular weight of 130 237. The deduced amino acid sequence of the Cry9Ec1 protein had the highest homology (77.7%) with the Cry9Ea1 protein when compared with existing Cry proteins. The expression, in an acrystalliferous B. thuringiensis strain, of the cry9Ec1 gene was high when controlled by the cyt1A2 promoter, leading to the formation of large spherical inclusions. The purified crystals from the recombinant strain were toxic when tested against two lepidopteran species, Bombyx mori and Plutella xylostella. However, the Cry9Ec1 protein gave no toxicity against Spodoptera litura, Spodoptera exigua, Plodia interpunctella, Helicoverpa zea, and Culex pipiens molestus.Key words: Bacillus thuringiensis serovar galleriae, Cry9Ec1 protein, lepidopteran-specific δ-endotoxin, Plutella xylostella.


Sign in / Sign up

Export Citation Format

Share Document