Sip1Ab gene from a native Bacillus thuringiensis strain QZL38 and its insecticidal activity against Colaphellus bowringi Baly

Sha, Junxue; Zhang, Jinbo; Chi, Baoyan; Liu, Rongmei; Li, Haitao; Gao, Jiguo

doi:10.1080/09583157.2018.1460313

Cited by 17 publications

(19 citation statements)

References 23 publications

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“…Currently, two Sip proteins have been described, both active against several coleopteran pests. The fact that strains harboring sip1Aa and sip1Ab genes also contain cry3 and cry8 genes, respectively, suggests that Sip1 proteins may have a role in the insecticidal mechanism against coleopteran insects [ 184 ].…”

Section: The Secretable Coleopteran-active Proteinsmentioning

confidence: 99%

“…As occurs with other related “B” compounds, Vip1 is formed by four domains involved in docking to enzymatic components, binding to specific cell surface receptors, oligomerization, and channel formation in lipid membranes [ 188 ]. Coleopteran active Sip1Aa protein contains a predicted Gram-positive consensus secretion signal [ 4 ] and exhibits 46% similarity with Mtx3 mosquitocidal toxin of Lysinibacillus sphaericus [ 184 ]. This homology may indicate that Sip1Aa toxicity should be caused by pore formation.…”

Section: The Secretable Coleopteran-active Proteinsmentioning

confidence: 99%

“…Sip1Aa caused lethal toxicity for L. decemlineata larvae and stunting in D. virgifera and D. undecimpunctata larvae [ 181 ]. Sip1Ab was also toxic to Colaphellus bowringi Baly (Coleoptera: Chrysomelidae) but it did not harm Hloltrichia diomphalia (Coleoptera: Scarabaeidae) larvae [ 184 ], suggesting specific chrysomelid activity, although further studies are needed to determine its host range.…”

Section: The Secretable Coleopteran-active Proteinsmentioning

confidence: 99%

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Insecticidal Activity of Bacillus thuringiensis Proteins against Coleopteran Pests

Domínguez-Arrizabalaga

Villanueva

Escriche

et al. 2020

Toxins

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Bacillus thuringiensis is the most successful microbial insecticide agent and its proteins have been studied for many years due to its toxicity against insects mainly belonging to the orders Lepidoptera, Diptera and Coleoptera, which are pests of agro-forestry and medical-veterinary interest. However, studies on the interactions between this bacterium and the insect species classified in the order Coleoptera are more limited when compared to other insect orders. To date, 45 Cry proteins, 2 Cyt proteins, 11 Vip proteins, and 2 Sip proteins have been reported with activity against coleopteran species. A number of these proteins have been successfully used in some insecticidal formulations and in the construction of transgenic crops to provide protection against main beetle pests. In this review, we provide an update on the activity of Bt toxins against coleopteran insects, as well as specific information about the structure and mode of action of coleopteran Bt proteins.

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Section: The Secretable Coleopteran-active Proteinsmentioning

confidence: 99%

Section: The Secretable Coleopteran-active Proteinsmentioning

confidence: 99%

Section: The Secretable Coleopteran-active Proteinsmentioning

confidence: 99%

See 1 more Smart Citation

Insecticidal Activity of Bacillus thuringiensis Proteins against Coleopteran Pests

Domínguez-Arrizabalaga

Villanueva

Escriche

et al. 2020

Toxins

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“…In order to test the broad-use potential of the created database, a selection of arbitrarily chosen manuscripts were additionally added to the dataset. These works investigate biocidal activity of agents other than B. thuringiensis Cry/Cyt/Vip proteins, including: chitinolytic enzymes [38][39][40][41][42] , synthetic and biochemical insecticides [43][44][45] , insect midgut proteins [46][47][48] Bacillus thuringiensis Mpp5A (formerly Sip1 proteins) 49,50 , scorpion toxins 51 and fungal spores 52,53 .…”

Section: Experiments Source Selection Research Papers Investigating Imentioning

confidence: 99%

TOXiTAXi: a web resource for toxicity of Bacillus thuringiensis protein compositions towards species of various taxonomic groups

Baranek

Pogodziński

Szipluk

et al. 2020

Sci Rep

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Bioinsecticides consisting of different sets of Bacillus thuringiensis (Bt) Cry, Cyt and Vip toxins are broadly used in pest control. Possible interactions (synergistic, additive or antagonistic) between these proteins can not only influence the overall efficacy of certain Bt-based bioinsecticide, but also raise questions regarding environmental safety. Here, we assemble, summarize and analyze the outcomes of experiments published over 30 years, investigating combinatorial effects among Bt Cry, Cyt and Vip toxins. We collected the results on 118 various two-to-five-component combinations that have been bioassayed against 38 invertebrate species. Synergism, additive effect and antagonism was indicated in 54%, 32% and 14% of experiments, respectively. Synergism was noted most frequently for Cry/Cyt combinations, followed by Cyt/Vip and Cry/Cry. In Cry/Vip combinations, antagonism is more frequent and higher in magnitude compared to other categories. Despite a significant number of tested Bt toxin combinations, most of them have been bioassayed only against one pest species. To aid the research on Bt pesticidal protein activity, we present TOXiTAXi (https://www.combio.pl/toxitaxi/), a universal database and a dedicated web tool to conveniently gather and analyze the existing and future bioassay results on biocidal activity of toxins against various taxonomic groups.

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“…Then, she constructed a truncated mutant, amplified and expressed the sip1Ab coding sequence that contained 1005 bp after the first 90 bp signal peptide was removed, and encoded 334 amino acids, and she renamed it as Sip1Aa, whose size was 37.6 kDa. The assay results of the insecticidal activity showed that the Lethal Concentration 50 (LC 50 ) of the C. bowringi Baly was 1.051 µg/mL (Sha et al, 2018).…”

Section: Introductionmentioning

confidence: 99%

In silico Structure–Based Investigation of Key Residues of Insecticidal Activity of Sip1Aa Protein

et al. 2020

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Colaphellus bowringi Baly mainly damages cruciferous vegetables, leading to huge economic losses. The secretory insecticidal protein (Sip) of Bacillus thuringiensis (Bt) has high insecticidal activity against C. bowringi Baly. The tertiary structure of Sip1Aa protein was analyzed by homologous modeling and other bioinformatics methods to predict the conserved domain of Sip1Aa protein. Acidic and basic amino acids in the conserved domain were selected, and alanine was used to replace these amino acids by site-directed mutation. The difference between the insecticidal activities of mutant protein and Sip1Aa protein was analyzed. The insecticidal activities of H99A, K109A, K128A, and E130A against C. bowringi Baly were significantly increased, among which that of K128A was the most obviously changed, and the LC 50 value was decreased by about 10 times compared with that of Sip1Aa protein. The LC 50 value of mutant E130A was 0.286 µg/mL, which was about six times less than that of Sip1Aa. K128 and E130 were both in the β9-β10 loop. The toxicity of D290A, H242A, and H303A to C. bowringi Baly was significantly reduced, and their LC 50 value increased by about six, eight, and three times compared with that of Sip1Aa protein, respectively. This study showed that acidic and basic amino acid residues played a certain role in the toxicity of Sip1Aa protein, and the loss of side chains in key residues had a significant impact on the insecticidal activity of the protein. This study provides the theoretical basis for revealing the relationship between the structure and function of Sip1Aa protein and also provides a new method for the subsequent study of sip gene.

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Sip1Ab gene from a native Bacillus thuringiensis strain QZL38 and its insecticidal activity against Colaphellus bowringi Baly

Cited by 17 publications

References 23 publications

Insecticidal Activity of Bacillus thuringiensis Proteins against Coleopteran Pests

Insecticidal Activity of Bacillus thuringiensis Proteins against Coleopteran Pests

TOXiTAXi: a web resource for toxicity of Bacillus thuringiensis protein compositions towards species of various taxonomic groups

In silico Structure–Based Investigation of Key Residues of Insecticidal Activity of Sip1Aa Protein

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