Bacillus sphaericus as a mosquito pathogen: properties of the organism and its toxins.

Baumann, Paul; Clark, Marta A.; Baumann, Linda C.; Broadwell, Andrew H.

doi:10.1128/mmbr.55.3.425-436.1991

Cited by 140 publications

(86 citation statements)

References 53 publications

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“…Mosquitocidal strains of B. sphaericus can be divided into two groups on the basis of their toxicity to mosquito larvae. Highly toxic strains synthesize a parasporal crystal containing two proteins (BinA and BinB) of 51 and 42 kDa that appear to act in a synergistic manner as a binary toxin (Baumann et al, 1991). These protein crystals are solubilized in the midgut of mosquito larvae following ingestion.…”

Section: The Mtx From B Sphaericus Ssii-1mentioning

confidence: 99%

Bacillus sphaericus mosquitocidal toxin (MTX) and pierisin: the enigmatic offspring from the family of ADP‐ribosyltransferases

Carpusca

Jank

Aktories³

2006

Molecular Microbiology

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SummaryThe mosquitocidal toxin (MTX) from Bacillus sphaericus and the apoptosis-inducing pierisin-1 from the cabbage butterfly Pieris rapae are two of the most intriguing members of the family of ADPribosyltransferases. They are both~100 kDa proteins, composed of an N-terminal ADP-ribosyltransferase (~27 kDa) and a C-terminal putative binding and translocation domain (~70 kDa) consisting of four ricin-Blike domains. While they both share structural homologies, with an overall amino acid sequence identity of~30% that becomes~50% at the level of the catalytic core, and functional similarities, notably in terms of enzyme regulation, they seem to largely differ with regard to their targets or cell internalization mechanisms. MTX ADP-ribosylates numerous proteins in lysates of target insect cells at arginine residues, whereas pierisin-1 modifies DNA of insect and mammalian cells by ADP-ribosylation at 2Ј-deoxyguanosine residues resulting in DNA adducts, mutations and eventually apoptosis. This target specificity differentiates pierisin-1 from all other ADP-ribosyltransferases described so far, and implies that the enzyme must reach the nucleus of target cells. The recently solved crystal structure of MTX catalytic domain is helpful to reveal new insights into structural organization, catalytic mechanisms, proteolytic activation and autoinhibition of both enzymes. The uptake and processing of the ADPribosyltransferases is discussed.

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Section: The Mtx From B Sphaericus Ssii-1mentioning

confidence: 99%

Bacillus sphaericus mosquitocidal toxin (MTX) and pierisin: the enigmatic offspring from the family of ADP‐ribosyltransferases

Carpusca

Jank

Aktories³

2006

Molecular Microbiology

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“…israelensis (Bti) and Bacillus sphaericus (Bs) which selectively kill mosquito larvae with negligible effect to the non-target organisms (Walker & Lynch, 2007). Susceptible mosquito larvae have alkaline gut conditions, enzymes and specific receptors for processing and binding of the Bti or Bs toxins (Baumann, Clark, Baumann, & Broadwell, 1991;Dadd, 1975;Nicolas, Lecroisey, & Charles, 1990;Soberón, Fernández, Pérez, Gill, & Bravo, 2007). Thus, the toxins responsible for the pathogenic effect in mosquito larvae have no effect to vertebrates and some invertebrates, and hence they are suitable for application even in peri-domestic mosquito breeding habitats (Lacey, 2007;Lacey & Merritt, 2003;Saik, Lacey, & Lacey, 1990).…”

Section: Introductionmentioning

confidence: 99%

Microbial larvicides for mosquito control: Impact of long lasting formulations ofBacillus thuringiensisvar.israelensisandBacillus sphaericuson non‐target organisms in western Kenya highlands

Derua

Kahindi

Mosha

et al. 2018

Ecology and Evolution

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The microbial larvicides Bacillus thuringiensis var. israelensis and Bacillus sphaericus have been used extensively for mosquito control and have been found to be effective and safe to non‐target organisms cohabiting with mosquito larvae. Recently developed long lasting microbial larvicides (LLML), although evading the previous challenge of short duration of activity, increase the risk of persistence of toxins in the treated larval habitats. This study monitored the impact of LLML FourStar® and LL3 on non‐target organisms cohabiting with mosquito larvae in an operational study to control malaria vectors in western Kenya highlands. A total of 300 larval habitats were selected in three highland villages. The habitats were first monitored for 5 weeks to collect baseline data on non‐target organisms cohabiting with mosquito larvae and then randomized into two treatment arms (respective FourStar® and LL3) and one control arm. Non‐target organisms were sampled weekly for 5 months after treatment to assess the impact of LLML intervention. Before treatment, the mean density of all non‐target organisms combined in the control, LL3 and FourStar® treated habitats was 1.42, 1.39 and 1.49 individuals per habitat per sampling occasion, respectively. Following treatment, this density remained fairly unchanged for 21 weeks at which time it was 1.82, 2.11, and 2.05 for the respective control, LL3 and FourStar® treated habitats. Statistical analysis revealed that LL3 and FourStar® did not significantly alter abundance, richness or diversity of the 11 taxa studied, when comparing the intervention and control larval habitats. However, both FourStar® and LL3 significantly reduced the density of malaria vectors. In conclusion, one round of label rate application of FourStar® or LL3 in natural larval habitats did not alter richness, abundance or diversity of the monitored aquatic non‐target organisms cohabiting with mosquito larvae to an ecologically significant level.

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“…Lysinibacillus sphaericus has been used successfully as a microbial larvicide for mosquito control worldwide (Hu et al, 2008). High-toxicity strains exhibit toxicity against Culex and Anopheles species but are almost inactive against Aedes species (Baumann et al, 1991;Charles et al, 1996). The mosquitocidal activity predominantly relies on binary (Bin) toxins (BinA/BinB proteins), which form crystal inclusions during sporulation (Priest et al, 1997).…”

Section: Introductionmentioning

confidence: 99%

Interaction of Lysinibacillus sphaericus Cry48Aa/Cry49Aa toxin with midgut brush‐border membrane fractions from Culex quinquefasciatus larvae

Guo

Cai

et al. 2016

Insect Molecular Biology

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The Cry48Aa/Cry49Aa mosquitocidal toxin from Lysinibacillus sphaericus was uniquely composed of a three-domain (Cry) toxin and binary (Bin) toxin-like protein, with high toxicity against Culex spp. However, its mode of action against the target mosquitoes is still unknown. In this study, Cry48Aa, Cry49Aa and its N- and C-terminal truncated proteins were expressed and purified, and the binding affinities of the purified proteins with midgut brush-border membrane fractions (BBMFs) from Culex quin-quefasciatus larvae were performed. The results showed that both Cry48Aa and Cry49Aa have specific and high binding affinity to BBMFs, with dissociation constants of 9.5 ± 1.8 and 25.4 ± 3.8 nM, respectively. Competition assays demonstrated that Cry49Aa C-terminal derivatives were able to bind to the BBMFs, whereas Far-Western dot blot analysis revealed that its N-terminal constructs interacted with Cry48Aa. Nevertheless, larvicidal activity was almost lost when Cry49Aa truncated proteins, either individually or in pairs, combined with Cry48Aa. It is concluded that Cry49Aa is responsible for receptor binding and interaction with Cry48Aa and plays an important role in the mechanism of action of these two-component toxins.

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Bacillus sphaericus as a mosquito pathogen: properties of the organism and its toxins.

Cited by 140 publications

References 53 publications

Bacillus sphaericus mosquitocidal toxin (MTX) and pierisin: the enigmatic offspring from the family of ADP‐ribosyltransferases

Bacillus sphaericus mosquitocidal toxin (MTX) and pierisin: the enigmatic offspring from the family of ADP‐ribosyltransferases

Microbial larvicides for mosquito control: Impact of long lasting formulations ofBacillus thuringiensisvar.israelensisandBacillus sphaericuson non‐target organisms in western Kenya highlands

Interaction of Lysinibacillus sphaericus Cry48Aa/Cry49Aa toxin with midgut brush‐border membrane fractions from Culex quinquefasciatus larvae

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