Essential role of tryptophan residues in toxicity of binary toxin from Bacillus sphaericus

Kunthic, Thittaya; Promdonkoy, Boonhiang; Srikhirin, Toemsak; Boonserm, Panadda

doi:10.5483/bmbrep.2011.44.10.674

Cited by 10 publications

(8 citation statements)

References 23 publications

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“…Pore formation by the Bin components has been demonstrated by patch clamp experiments on Culex quinquefasciatus cells . Similarly, previous studies have shown that both BinA and BinB components were able to permeabilize planar lipid bilayer and receptor‐free large unilamellar phospholipid vesicles . Both BinA and BinB components could insert into lipid monolayers, and conformational changes of both BinA and BinB were observed upon membrane association .…”

Section: Introductionsupporting

confidence: 56%

Crystal structure of BinB: A receptor binding component of the binary toxin from Lysinibacillus sphaericus

et al. 2014

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The binary toxin (Bin), produced by Lysinibacillus sphaericus, is composed of BinA (42 kDa) and BinB (51 kDa) proteins, which are both required for full toxicity against Culex and Anopheles mosquito larvae. Specificity of Bin toxin is determined by the binding of BinB component to a receptor present on the midgut epithelial membranes, while BinA is proposed to be a toxic component. Here, we determined the first crystal structure of the active form of BinB at a resolution of 1.75 Å. BinB possesses two distinct structural domains in its N- and C-termini. The globular N-terminal domain has a β-trefoil scaffold which is a highly conserved architecture of some sugar binding proteins or lectins, suggesting a role of this domain in receptor-binding. The BinB β-rich C-terminal domain shares similar three-dimensional folding with aerolysin type β-pore forming toxins, despite a low sequence identity. The BinB structure, therefore, is a new member of the aerolysin-like toxin family, with probably similarities in the cytolytic mechanism that takes place via pore formation.

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Section: Introductionsupporting

confidence: 56%

Crystal structure of BinB: A receptor binding component of the binary toxin from Lysinibacillus sphaericus

et al. 2014

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“…Given that L. sphaericus presents a tryptophan operon, this bacterium has the ability to synthesize tryptophan amino acid [11,23,38], which is one of the precursors to indole acetic acid [39,40]. In this sense, results showed that indole acetic acid could be determined directly from soil samples without the addition of tryptophan.…”

Section: Indole Acetic Acid Productionmentioning

confidence: 99%

Lysinibacillus sphaericusas a Nutrient Enhancer during Fire-Impacted Soil Replantation

Aguirre-Monroy

Santana-Martínez

Dussán

2019

Applied and Environmental Soil Science

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Over the past ten years, more than twenty fires have affected the El Noviciado estate located in Cerro Majuy, Colombia, leading to a loss of soil nutrients and infertility. Lysinibacillus sphaericus, a Gram-positive, mesophilic, and spore-forming bacterium, can be used in soil amendment in the replantation processes, given its ability to fix nitrogen, and nitrify, and solubilize phosphorus, increasing soil nutrients used for plant growth. In this study, we evaluated the soil-amendment potential of L. sphaericus by monitoring the nutrient content of a selected fragment of soil in the El Noviciado estate. For this purpose, we added a mixture of L. sphaericus OT4b.31, OT4b.49, CBAM5, III(3)7, and 2362 strains and determined the ammonium, nitrites, nitrates, phosphorus, and indole acetic acid concentrations in soil. Alnus acuminata sbsp. acuminata, a native model plant known for its restoration effect, was used for replantation. Results indicated that soils with added L. sphaericus presented significant differences in ammonium, nitrites, nitrates, phosphorus, and indole acetic acid concentrations when compared to control soils. Further, results showed no significant differences between soil that had been pre-inoculated in greenhouse and soil directly inoculated in field. We propose that L. sphaericus could be a good nutrient enhancer and plant growth promoter that can be used for the amendment of fire-impacted soils and replantation treatments.

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“…BinA, BinB and Cry49Aa1 do contain an occurrence of the QxW motif in the β-sheet core of the C-terminal domain as does Cry35Ab1 although this occurrence of the motif is absent from the much more closely-related Cry35Aa1 sequence. In BinA, substitution of Trp222 in this feature, equivalent to Trp211 of Cry35Ab1, results in loss of activity although the protein is still able to permeabilize liposomes [63]. Ricin-B-like lectin repeats were also noted in the 41.9 kDa B. thuringiensis protein [51] although there are no QxW motifs in this protein.…”

Section: Resultsmentioning

confidence: 99%

Structural and Biophysical Characterization of Bacillus thuringiensis Insecticidal Proteins Cry34Ab1 and Cry35Ab1

Kelker¹,

Berry

Evans³

et al. 2014

PLoS ONE

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Bacillus thuringiensis strains are well known for the production of insecticidal proteins upon sporulation and these proteins are deposited in parasporal crystalline inclusions. The majority of these insect-specific toxins exhibit three domains in the mature toxin sequence. However, other Cry toxins are structurally and evolutionarily unrelated to this three-domain family and little is known of their three dimensional structures, limiting our understanding of their mechanisms of action and our ability to engineer the proteins to enhance their function. Among the non-three domain Cry toxins, the Cry34Ab1 and Cry35Ab1 proteins from B. thuringiensis strain PS149B1 are required to act together to produce toxicity to the western corn rootworm (WCR) Diabrotica virgifera virgifera Le Conte via a pore forming mechanism of action. Cry34Ab1 is a protein of ∼14 kDa with features of the aegerolysin family (Pfam06355) of proteins that have known membrane disrupting activity, while Cry35Ab1 is a ∼44 kDa member of the toxin_10 family (Pfam05431) that includes other insecticidal proteins such as the binary toxin BinA/BinB. The Cry34Ab1/Cry35Ab1 proteins represent an important seed trait technology having been developed as insect resistance traits in commercialized corn hybrids for control of WCR. The structures of Cry34Ab1 and Cry35Ab1 have been elucidated to 2.15 Å and 1.80 Å resolution, respectively. The solution structures of the toxins were further studied by small angle X-ray scattering and native electrospray ion mobility mass spectrometry. We present here the first published structure from the aegerolysin protein domain family and the structural comparisons of Cry34Ab1 and Cry35Ab1 with other pore forming toxins.

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Essential role of tryptophan residues in toxicity of binary toxin from Bacillus sphaericus

Cited by 10 publications

References 23 publications

Crystal structure of BinB: A receptor binding component of the binary toxin from Lysinibacillus sphaericus

Crystal structure of BinB: A receptor binding component of the binary toxin from Lysinibacillus sphaericus

Lysinibacillus sphaericusas a Nutrient Enhancer during Fire-Impacted Soil Replantation

Structural and Biophysical Characterization of Bacillus thuringiensis Insecticidal Proteins Cry34Ab1 and Cry35Ab1

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