The Cry48Aa N-terminal Domain is Responsible for Cry48Aa–Cry49Aa Interaction in Lysinibacillus sphaericus Toxin

Guo, Qianjin; Yuan, Gao; Xing, Chong; Ding, Lu; Dai, Xiaohua; Xie, Qiangqiang; Tan, Xiao

doi:10.1007/s00284-020-01907-6

Cited by 7 publications

(7 citation statements)

References 23 publications

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“…These results demonstrated that Cys70, Cys91, Cys183, and Cys258 may not participate in the intra-or intermolecular disul de bonds formation in Cry49Aa molecules. Amino acid sequence analysis showed there are 2 cysteine residues (Cys479, Cys562) in N-terminal domain of active Cry48Aa toxin is responsible for Cry48Aa-Cry49Aa interaction (Guo et al, 2016(Guo et al, , 2020. Thus, it is supposed that one or more cysteine residues in Cry48Aa could result in disul de bond formation with Cys70, Cys91, Cys183, and Cys258 in Cry49Aa.…”

Section: Resultsmentioning

confidence: 99%

“…Cry49Aa-C258A inactive Effect of cysteine substitutions on Cry48Aa-Cry49Aa interaction Cry49Aa subunit plays a crucial role in the action mechanism of Cry48Aa/ Cry49Aa two-component toxins, while Cry48Aa-Cry49Aa interaction is one of the key steps in achieving their toxic activity against larvae (Jones et al, 2007;Guo et al, 2016Guo et al, , 2020. In our study, the far-Western dot blot analysis was used to explore the possible role of Cry49Aa cysteine in the intermolecular Cry49Aa-Cry48Aa interaction.…”

Section: Cry49aa-c183a Inactivementioning

confidence: 99%

“…These cysteine residues may not participate in disul de bond formation in Cry49Aa, but may affect crystal 3D structures, and then play an important role on Cry48Aa-Cry49Aa complex formation and toxin-receptor interaction. The Cry49Aa, as accessory protein, only combined with Cry48Aa could achieved the insecticidal activity (Jones et al, 2007(Jones et al, , 2008Guo et al, 2016Guo et al, , 2020. However, it is uncertain that mutations at these positions lead to weaken interaction between Cry49Aa mutants and Cry48Aa or BBMFs could account for the loss of virulence.…”

Section: Effect Of Cysteine Mutations On Binding To C Quinquefasciatus Bbmfsmentioning

confidence: 99%

“…The activated Cry49Aa fragment of approximately 47-kDa is produced through chymotrypsin-like cleavage by C. quinquefasciatus gut extract between F48 and N49 (Jones et al, 2008). Previous studies have indicated the Cry48Aa/Cry49Aa complex can be formed in synergy through the N-terminal portion of both Cry48Aa and Cry49Aa subunit (Guo et al, 2016(Guo et al, , 2020. Individual Cry48Aa and Cry49Aa subunit was able to interact with receptors located on the midgut of Culex larvae (Guo et al, 2016), and then these speci c receptors are being studied and putative candidates have been recently preliminarily identi ed (Rezende et al, 2017).…”

Section: Introductionmentioning

confidence: 99%

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Cys183 and Cys258 in Cry49Aa toxin from Lysinibacillus sphaericus are essential for toxicity to Culex quinquefasciatus larvae

et al. 2021

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The two-component Cry48Aa/Cry49Aa toxin produced by Lysinibacillus sphaericus shows speci cally toxic to Culex quinquefasciatus mosquito larvae. Cry49Aa C-terminal domain is responsible for speci c binding to the larval gut cell membrane, while its N-terminal domain is required for interaction with Cry48Aa. To investigate functional role of cysteine in Cry49Aa, four cysteine residues at positions 70, 91, 183, and 258 were substituted by alanine. All mutants showed similar crystalline morphology and comparable yield to that of the wild type except that the yield of the C91A mutant was low. These cysteine residues did not involve in disul de bond formation within or between Cry49Aa molecules. Cys91, Cys183 and Cys258 are essential for toxicity against C. quinquefasciatus larvae, while Cys70 is not. Substitution at C91, C183 and C258 caused weak Cry48Aa-Cry49Aa interaction, while mutations at C183 and C258 reduced the binding capacities to the larval gut cell membrane. Thus, Cysteine residues at position 91, 183 and 258 in Cry49Aa are required for full toxicity of Cry48Aa/Cry49Aa toxin.

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Section: Resultsmentioning

confidence: 99%

Section: Cry49aa-c183a Inactivementioning

confidence: 99%

Section: Effect Of Cysteine Mutations On Binding To C Quinquefasciatus Bbmfsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Cys183 and Cys258 in Cry49Aa toxin from Lysinibacillus sphaericus are essential for toxicity to Culex quinquefasciatus larvae

et al. 2021

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“…Effect of cysteine substitutions on Cry48Aa-Cry49Aa interaction Cry49Aa subunit plays a crucial role in the action mechanism of Cry48Aa/ Cry49Aa two-component toxins, while Cry48Aa-Cry49Aa interaction is one of the key steps in achieving their toxic activity against larvae (Jones et al, 2007;Guo et al, 2016Guo et al, , 2020. In our study, the far-Western dot blot analysis was used to explore the possible role of Cry49Aa cysteine in the intermolecular Cry49Aa-Cry48Aa interaction.…”

Section: Cry49aa-c258a Inactivementioning

confidence: 99%

Cys183, and Cys258 in Cry49Aa Toxin From Lysinibacillus Sphaericus Are Essential for Toxicity to Culex Quinquefasciatus Larvae

Guo

Ding

Yuan

et al. 2021

Preprint

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The two-component Cry48Aa/Cry49Aa toxin produced by Lysinibacillus sphaericus shows specifically toxic to Culex quinquefasciatus mosquito larvae. Cry49Aa C-terminal domain is responsible for specific binding to the larval gut cell membrane, while its N-terminal domain is required for interaction with Cry48Aa. To investigate functional role of cysteine in Cry49Aa, four cysteine residues at positions 70, 91, 183, and 258 were substituted by alanine. All mutants showed similar crystalline morphology and comparable yield to that of the wild type except that the yield of the C91A mutant was low. These cysteine residues did not involve in disulfide bond formation within or between Cry49Aa molecules. Cys91, Cys183 and Cys258 are essential for toxicity against C. quinquefasciatus larvae, while Cys70 is not. Substitution at C91, C183 and C258 caused weak Cry48Aa- Cry49Aa interaction, while mutations at C183 and C258 reduced the binding capacities to the larval gut cell membrane. Thus, Cysteine residues at position 91, 183 and 258 in Cry49Aa are required for full toxicity of Cry48Aa/Cry49Aa toxin.

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

Guo

Yuan

Xing

et al. 2022

Insect Biochemistry and Molecular Biology

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The Cry48Aa N-terminal Domain is Responsible for Cry48Aa–Cry49Aa Interaction in Lysinibacillus sphaericus Toxin

Cited by 7 publications

References 23 publications

Cys183 and Cys258 in Cry49Aa toxin from Lysinibacillus sphaericus are essential for toxicity to Culex quinquefasciatus larvae

Cys183 and Cys258 in Cry49Aa toxin from Lysinibacillus sphaericus are essential for toxicity to Culex quinquefasciatus larvae

Cys183, and Cys258 in Cry49Aa Toxin From Lysinibacillus Sphaericus Are Essential for Toxicity to Culex Quinquefasciatus Larvae

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

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