Cloning, heterologous expression, and localization of a novel crystal protein gene fromBacillus thuringiensis serovarjaponensis strain Buibui toxic to scarabaeid insects

Satō, Ryōichi; Takeuchi, Katsuyoshi; Ogiwara, Katsutoshi; Minami, Masayosi; Kaji, Yasuko; Suzuki, Nobukazu; Hori, Hidetaka; Asano, Shoji; Ohba, Michio; Iwahana, Hidenori

doi:10.1007/bf01575980

Cited by 40 publications

(16 citation statements)

References 25 publications

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“…A pair of primers was designed for the coding region of cry8Ca sequence to allow amplification of the full-length cry8 gene (Sato et al 1994):…”

Section: Bacterial Strains and Growth Conditionsmentioning

confidence: 99%

“…Proteins of the Cry3, Cry6, Cry7, Cry8, Cry18, and Cry43 classes, as well as the binary toxins Cry34A-Cry35A are toxic for insects of the Coleoptera order, including beetles and weevils (Baum et al 2004;Shu et al 2009;Yu et al 2006;Lambert et al 1992). Among these classes, cry8, cry18 and cry43 genes are toxic for Scarabaeidae larvae (Shu et al 2009;Yu et al 2006;Sato et al 1994;Asano et al 2003;Yokoyama et al 2004;Zhang et al 1997).…”

Section: Introductionmentioning

confidence: 99%

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Characterization of one novel cry8 gene from Bacillus thuringiensis strain Q52-7

Liu

Shu

et al. 2014

World J Microbiol Biotechnol

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Bacillus thuringiensis (Bt) is the most widely used insecticidal microbe due to its specific toxicity and safe use with respect to animals and the environment. In this study, we isolated Bt strain Q52-7 from a soil sample collected in the Qian Shan District, Liao Ning Province, China. We observed that the Q52-7 strain produced spherical crystals. The Bt Q52-7 strain had high toxicity against Asian Cockchafer (Holotrichia parallela), exhibiting an LC50 of 3.80 × 10(9) cfu/g, but is not toxic for Anomala corpulenta Motschulsky and Holotrichia oblita. Using general cry8 primers, we amplified a 1.3 kb fragment with the polymerase chain reaction. Specific primers were designed for the amplified fragment to clone the full-length coding region. A novel gene, cry8Na1, had 69 % sequence similarity with cry8Ca1. cry8Na1 gene was successfully expressed in the HD-73(-) acrystalliferous mutant of Bt subsp. Kurstaki HD-73. Bioassays demonstrated that the Cry8Na1 protein is highly toxic for the H. parallela, with a 50 % lethal concentration of 8.18 × 10(10) colony forming units per gram.

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“…A pair of primers was designed for the coding region of cry8Ca sequence to allow amplification of the full-length cry8 gene (Sato et al 1994):…”

Section: Bacterial Strains and Growth Conditionsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Characterization of one novel cry8 gene from Bacillus thuringiensis strain Q52-7

Liu

Shu

et al. 2014

World J Microbiol Biotechnol

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“…Proteins of the Cry3 (12,17), Cry7 (14), and Cry8 (19) classes are active against insects of the order Coleoptera (beetles and weevils). Cry3Aa is the most active natural protein for the important potato pest Leptinotarsa decemlineata (Say) (Colorado potato beetle; CPB).…”

mentioning

confidence: 99%

Bacillus thuringiensis Delta-Endotoxin Cry1 Hybrid Proteins with Increased Activity against the Colorado Potato Beetle

Naimov

Weemen-Hendriks

Dukiandjiev

et al. 2001

Appl Environ Microbiol

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“…Recent studies have shown that Bacillus thuringiensis (Bt) toxin Cry8-type had specific activity against coleopteran larvae (Sato et al, 1994;Yamaguchi et al, 2008). Cry8like, Cry8Ab, Cry8Ea, Cry8Ga, and Cry8Na1 were proven to widely used for control of H. parallela (Shu et al, 2009a,b;Zhang et al, 2013;Li et al, 2014).…”

Section: Introductionmentioning

confidence: 99%

Characterization of a novel Cry8Ea3-binding V-ATPase Subunit A in Holotrichia parallela

et al. 2016

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ABSTRACT. Several receptor proteins of Cry toxin have been previously identified, including cadherin-like, aminopeptidase N, and alkaline phosphatase. In the present work, a novel binding protein, V-ATPase subunit A (HpVAA), was identified in Holotricia parallela larvae and characterized. We performed reverse transcriptionpolymerase chain reaction and rapid amplification of cDNA ends technology to obtain the cDNA of the full-length hpvaa. Sequencing analysis showed that the open reading frame of hpvaa (GenBank accession No. KU497557) is 1845 bp long, encoding 614 amino acid residues. The predicted molecular weight and isoelectric point of HpVAA were 67.85 kDa and 4.9, respectively. The HpVAA protein, which includes two putative conserved domains, ATP-synt_ab_N and ATP-synt_ab_C, and a Walker A (GAFGCGKT) motif and a Walker B (SMMAD) motif, possesses the same structural characteristics as V-ATPase subunit A from other insects. The protein was successfully 2 W. Wei et al. Genetics and Molecular Research 15 (3): gmr.15038994 expressed in Escherichia coli, and a ligand blot assay showed binding of the protein with Cry8Ea3 toxin. Transcriptional analysis of hpvaa in different tissues of H. parallela larvae was performed by qRT-PCR, which showed that the relative expression of hpvaa in the Malpighian tubules is higher than that in other tissues.

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Cloning, heterologous expression, and localization of a novel crystal protein gene fromBacillus thuringiensis serovarjaponensis strain Buibui toxic to scarabaeid insects

Cited by 40 publications

References 25 publications

Characterization of one novel cry8 gene from Bacillus thuringiensis strain Q52-7

Characterization of one novel cry8 gene from Bacillus thuringiensis strain Q52-7

Bacillus thuringiensis Delta-Endotoxin Cry1 Hybrid Proteins with Increased Activity against the Colorado Potato Beetle

Characterization of a novel Cry8Ea3-binding V-ATPase Subunit A in Holotrichia parallela

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