Culex quinquefasciatus alpha-glucosidase serves as a putative receptor of the Cry48Aa toxin from Lysinibacillus sphaericus

Guo, Qianjin; Yuan, Gao; Xing, Chong; Niu, Yingchao; Ding, Lu; Dai, Xiaohua

doi:10.1016/j.ibmb.2022.103799

Cited by 4 publications

(3 citation statements)

References 45 publications

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“… Cry toxin Part of toxin (full-length/domain) Receptor/Mosquito source Dissociation constant ( K d , nM) Technique for binding analysis Reference Cry4Ba Full-length ALP/ A. aegypti 14 Quartz crystal microbalance [ 15 ] Cry4Ba Full-length ALP/ A. aegypti 80 ELISA [ 17 ] Cry4Ba Full-length Cadherin fragment CR11-MPED/ Anopheles gambiae 23 ELISA [ 27 ] Cry4Ba Domain II ALP/ A. aegypti 116 ELISA This study Cry4Ba Domain III ALP/ A. aegypti 110 ELISA [ 17 ] Cry11Ba Full-length Brush border membrane vesicles (BBMV)/ A. aegypti 8.2 ELISA [ 28 ] Cry11Ba Full-length APN/ An. gambiae 6.4 ELISA [ 29 ] Cry48Aa Full-length Alpha-glucosidase /Culex quinquefasciatus 48.7 ELISA [ 30 ...…”

Section: Discussionmentioning

confidence: 99%

Cry4Ba toxin of Bacillus thuringiensis subsp. israelensis uses both domains II and III to bind to its receptor—Aedes aegypti alkaline phosphatase

Thammasittirong,

Thammasittirong

2023

Heliyon

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Section: Discussionmentioning

confidence: 99%

Cry4Ba toxin of Bacillus thuringiensis subsp. israelensis uses both domains II and III to bind to its receptor—Aedes aegypti alkaline phosphatase

Thammasittirong,

Thammasittirong

2023

Heliyon

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“…The RIAB59 strain also displays a moderate resistance level (RR ~ 15-fold) to the Cry48Aa/Cry49Aa toxin. This is a second binary toxin produced by the IAB59 strain which binds to other receptors than the Cqm1 [ 24 – 26 ]. Most investigations on L. sphaericus resistance have concentrated efforts to characterize the mechanisms and genes that confer the Bin-resistance itself [ 3 ], while much less is known about other features that could be related to this phenotype.…”

Section: Introductionmentioning

confidence: 99%

A Culex quinquefasciatus strain resistant to the binary toxin from Lysinibacillus sphaericus displays altered enzyme activities and energy reserves

et al. 2023

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Background The resistance of a Culex quinquefasciatus strain to the binary (Bin) larvicidal toxin from Lysinibacillus sphaericus is due to the lack of expression of the toxin’s receptors, the membrane-bound Cqm1 α-glucosidases. A previous transcriptomic profile of the resistant larvae showed differentially expressed genes coding Cqm1, lipases, proteases and other genes involved in lipid and carbohydrate metabolism. This study aimed to investigate the metabolic features of Bin-resistant individuals by comparing the activity of some enzymes, energy reserves, fertility and fecundity to a susceptible strain. Methods The activity of specific enzymes was recorded in midgut samples from resistant and susceptible larvae. The amount of lipids and reducing sugars was determined for larvae and adults from both strains. Additionally, the fecundity and fertility parameters of these strains under control and stress conditions were examined. Results Enzyme assays showed that the esterase activities in the midgut of resistant larvae were significantly lower than susceptible ones using acetyl-, butyryl- and heptanoyl-methylumbelliferyl esthers as substrates. The α-glucosidase activity was also reduced in resistant larvae using sucrose and a synthetic substrate. No difference in protease activities as trypsins, chymotrypsins and aminopeptidases was detected between resistant and susceptible larvae. In larval and adult stages, the resistant strain showed an altered profile of energy reserves characterized by significantly reduced levels of lipids and a greater amount of reducing sugars. The fertility and fecundity of females were similar for both strains, indicating that those changes in energy reserves did not affect these reproductive parameters. Conclusions Our dataset showed that Bin-resistant insects display differential metabolic features co-selected with the phenotype of resistance that can potentially have effects on mosquito fitness, in particular, due to the reduced lipid accumulation. Graphical Abstract

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“…Several classes of Cry48Aa1/Tpp49Aa1 binding proteins have been identified, including maltases, aminopeptidases, alkaline phosphatases, and metalloproteases ( 12 ). In addition, an alpha-glucosidase (Glu71) from C. quinquefasciatus has been identified as a putative receptor of Cry48Aa1 ( 13 ). Following membrane interaction, subsequent cytopathological effects including cytoplasmic and mitochondrial vacuolation, endoplasmic reticulum breakdown, and microvillus disruption are seen ( 14 ), culminating in insect death.…”

mentioning

confidence: 99%

Structure of the Lysinibacillus sphaericus Tpp49Aa1 pesticidal protein elucidated from natural crystals using MHz-SFX

Williamson,

Galchenkova,

Best

et al. 2023

Proc. Natl. Acad. Sci. U.S.A.

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The Lysinibacillus sphaericus proteins Tpp49Aa1 and Cry48Aa1 can together act as a toxin toward the mosquito Culex quinquefasciatus and have potential use in biocontrol. Given that proteins with sequence homology to the individual proteins can have activity alone against other insect species, the structure of Tpp49Aa1 was solved in order to understand this protein more fully and inform the design of improved biopesticides. Tpp49Aa1 is naturally expressed as a crystalline inclusion within the host bacterium, and MHz serial femtosecond crystallography using the novel nanofocus option at an X-ray free electron laser allowed rapid and high-quality data collection to determine the structure of Tpp49Aa1 at 1.62 Å resolution. This revealed the packing of Tpp49Aa1 within these natural nanocrystals as a homodimer with a large intermolecular interface. Complementary experiments conducted at varied pH also enabled investigation of the early structural events leading up to the dissolution of natural Tpp49Aa1 crystals—a crucial step in its mechanism of action. To better understand the cooperation between the two proteins, assays were performed on a range of different mosquito cell lines using both individual proteins and mixtures of the two. Finally, bioassays demonstrated Tpp49Aa1/Cry48Aa1 susceptibility of Anopheles stephensi , Aedes albopictus, and Culex tarsalis larvae—substantially increasing the potential use of this binary toxin in mosquito control.

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Culex quinquefasciatus alpha-glucosidase serves as a putative receptor of the Cry48Aa toxin from Lysinibacillus sphaericus

Cited by 4 publications

References 45 publications

Cry4Ba toxin of Bacillus thuringiensis subsp. israelensis uses both domains II and III to bind to its receptor—Aedes aegypti alkaline phosphatase

Cry4Ba toxin of Bacillus thuringiensis subsp. israelensis uses both domains II and III to bind to its receptor—Aedes aegypti alkaline phosphatase

A Culex quinquefasciatus strain resistant to the binary toxin from Lysinibacillus sphaericus displays altered enzyme activities and energy reserves

Structure of the Lysinibacillus sphaericus Tpp49Aa1 pesticidal protein elucidated from natural crystals using MHz-SFX

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