The Proteolytic Activation, Toxic Effects, and Midgut Histopathology of the Cry1Ia Protoxin in (Coleoptera: Curculionidae).
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| Formato: | Artículo científico |
| Lenguaje: | en |
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Toxins
2025
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| _version_ | 1868266239809290242 |
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| author | Ayra-Pardo, Camilo Ramaré, Victor Couto, Ana Almeida, Mariana Martins, Ricardo Sousa, José Américo Santos, Maria João |
| author_facet | Ayra-Pardo, Camilo Ramaré, Victor Couto, Ana Almeida, Mariana Martins, Ricardo Sousa, José Américo Santos, Maria João Ayra-Pardo, Camilo Ramaré, Victor Couto, Ana Almeida, Mariana Martins, Ricardo Sousa, José Américo Santos, Maria João |
| collection | PubMed - marine biology |
| contents | The Proteolytic Activation, Toxic Effects, and Midgut Histopathology of the Cry1Ia Protoxin in (Coleoptera: Curculionidae). Ayra-Pardo, Camilo Ramaré, Victor Couto, Ana Almeida, Mariana Martins, Ricardo Sousa, José Américo Santos, Maria João Animals Larva Weevils Bacillus thuringiensis Toxins Bacterial Proteins Hemolysin Proteins Bacterial Toxins Proteolysis Insecticides Bacillus thuringiensis Endotoxins Gastrointestinal Tract Pest Control, Biological Protein Precursors The red palm weevil (RPW; Coleoptera: Curculionidae) is a destructive pest affecting palms worldwide, capable of causing significant economic losses and ecological damage in managed palm ecosystems. Current management heavily relies on synthetic insecticides, but their overuse fosters resistance. (Bt) offers a promising alternative, producing toxins selective against various insect orders, including Coleoptera. However, no specific Bt toxin has yet been identified for RPW. This study investigates the toxicity against RPW larvae of the Bt Cry1Ia protoxin, known for its dual activity against Lepidoptera and Coleoptera. A laboratory RPW colony was reared for two generations, ensuring a reliable insect source for bioassays. Cry1Ia was expressed as a 6xHis-tagged fusion protein in and purified using nickel affinity. Incubation with RPW larval gut proteases for 24 h produced a stable core of ~65 kDa. Diet-incorporation bioassays revealed high Cry1Ia toxicity in neonate larvae. In contrast, the lepidopteran-active Cry1Ac protoxin, used as a robust negative control, was completely degraded after 24 h of in vitro proteolysis and showed no toxicity in bioassays. Cry1Ia-fed larvae exhibited significant midgut cell damage, characteristic of Bt intoxication. These findings highlight Cry1Ia's strong potential for integration into RPW management programs. |
| format | Artículo científico |
| id | pubmed_39998101 |
| institution | PubMed |
| language | en |
| publishDate | 2025 |
| publisher | Toxins |
| record_format | pubmed |
| spellingShingle | The Proteolytic Activation, Toxic Effects, and Midgut Histopathology of the Cry1Ia Protoxin in (Coleoptera: Curculionidae). Ayra-Pardo, Camilo Ramaré, Victor Couto, Ana Almeida, Mariana Martins, Ricardo Sousa, José Américo Santos, Maria João Animals Larva Weevils Bacillus thuringiensis Toxins Bacterial Proteins Hemolysin Proteins Bacterial Toxins Proteolysis Insecticides Bacillus thuringiensis Endotoxins Gastrointestinal Tract Pest Control, Biological Protein Precursors The Proteolytic Activation, Toxic Effects, and Midgut Histopathology of the Cry1Ia Protoxin in (Coleoptera: Curculionidae). Ayra-Pardo, Camilo Ramaré, Victor Couto, Ana Almeida, Mariana Martins, Ricardo Sousa, José Américo Santos, Maria João Animals Larva Weevils Bacillus thuringiensis Toxins Bacterial Proteins Hemolysin Proteins Bacterial Toxins Proteolysis Insecticides Bacillus thuringiensis Endotoxins Gastrointestinal Tract Pest Control, Biological Protein Precursors The red palm weevil (RPW; Coleoptera: Curculionidae) is a destructive pest affecting palms worldwide, capable of causing significant economic losses and ecological damage in managed palm ecosystems. Current management heavily relies on synthetic insecticides, but their overuse fosters resistance. (Bt) offers a promising alternative, producing toxins selective against various insect orders, including Coleoptera. However, no specific Bt toxin has yet been identified for RPW. This study investigates the toxicity against RPW larvae of the Bt Cry1Ia protoxin, known for its dual activity against Lepidoptera and Coleoptera. A laboratory RPW colony was reared for two generations, ensuring a reliable insect source for bioassays. Cry1Ia was expressed as a 6xHis-tagged fusion protein in and purified using nickel affinity. Incubation with RPW larval gut proteases for 24 h produced a stable core of ~65 kDa. Diet-incorporation bioassays revealed high Cry1Ia toxicity in neonate larvae. In contrast, the lepidopteran-active Cry1Ac protoxin, used as a robust negative control, was completely degraded after 24 h of in vitro proteolysis and showed no toxicity in bioassays. Cry1Ia-fed larvae exhibited significant midgut cell damage, characteristic of Bt intoxication. These findings highlight Cry1Ia's strong potential for integration into RPW management programs. |
| title | The Proteolytic Activation, Toxic Effects, and Midgut Histopathology of the Cry1Ia Protoxin in (Coleoptera: Curculionidae). |
| topic | Animals Larva Weevils Bacillus thuringiensis Toxins Bacterial Proteins Hemolysin Proteins Bacterial Toxins Proteolysis Insecticides Bacillus thuringiensis Endotoxins Gastrointestinal Tract Pest Control, Biological Protein Precursors |
| url | https://pubmed.ncbi.nlm.nih.gov/39998101/ |