Hetero-oligomerization of Bacillus thuringiensis Cry1A proteins enhance binding to the ABCC2 transporter of Spodoptera exigua
| العنوان: | Hetero-oligomerization of Bacillus thuringiensis Cry1A proteins enhance binding to the ABCC2 transporter of Spodoptera exigua |
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| المؤلفون: | Noelia Joya, Daniel Pinos, Juan Ferré, Patricia Hernández-Martínez, Salvador Herrero |
| المصدر: | Biochemical Journal. 478:2589-2600 |
| بيانات النشر: | Portland Press Ltd., 2021. |
| سنة النشر: | 2021 |
| مصطلحات موضوعية: | 0301 basic medicine, Cell Survival, Bacillus thuringiensis, ATP-binding cassette transporter, Spodoptera, Biochemistry, Hemolysin Proteins, 03 medical and health sciences, 0302 clinical medicine, Bacterial Proteins, Protein Domains, Sf9 Cells, Animals, Binding site, Receptor, Molecular Biology, Binding Sites, Bacillus thuringiensis Toxins, biology, Chemistry, fungi, food and beverages, Transporter, Cell Biology, biology.organism_classification, Multidrug Resistance-Associated Protein 2, Endotoxins, 030104 developmental biology, Membrane protein, Cry1Ac, Mutation, Insect Proteins, Multidrug Resistance-Associated Proteins, Protein Multimerization, 030217 neurology & neurosurgery, Protein Binding |
| الوصف: | The ATP binding cassette (ABC) transporters are membrane proteins that can act as putative receptors for Cry proteins from Bacillus thuringiensis (Bt) in the midgut of different insects. For the beet armyworm, Spodoptera exigua, ABCC2 and ABCC3 have been found to interact with Cry1A proteins, the main insecticidal proteins used in Bt crops, as well as Bt-based pesticides. The ABCC2 has shown to have specific binding towards Cry1Ac and is involved in the toxic process of Cry1A proteins, but the role of this transporter and how it relates with the Cry1A proteins is still unknown. Here, we have characterized the interactions between the SeABCC2 and the main proteins that bind to the receptor. By labeling the Cry1Aa protein, we have found that virtually all of the binding is in an oligomeric state, a conformation that allowed higher levels of specific binding that could not be achieved by the monomeric protein on its own. Furthermore, we have observed that Cry1A proteins can hetero-oligomerize in the presence of the transporter, which is reflected in an increase in binding and toxicity to SeABCC2-expressing cells. This synergism can be one of the reasons why B. thuringiensis co-expresses different Cry1 proteins that can apparently have similar binding preferences. The results from in vitro competition and ex vivo competition showed that Cry1Aa, Cry1Ab and Cry1Ac share functional binding sites. By using Cry1Ab–Cry1Ac chimeras, the presence of domain I from Cry1A proteins was revealed to be critical for oligomer formation. |
| تدمد: | 1470-8728 0264-6021 |
| الوصول الحر: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bdff454f2a02f6e45b5d05e6430040f5Test https://doi.org/10.1042/bcj20210137Test |
| حقوق: | OPEN |
| رقم الانضمام: | edsair.doi.dedup.....bdff454f2a02f6e45b5d05e6430040f5 |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 14708728 02646021 |
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