Individual transmembrane domains of SfABCC2 from Spodoptera frugiperda do not serve as functional Cry1F receptors
文献类型： 外文期刊
作者： Zhong, Jianfeng 1 ; Dos Santos, Rafael Ferreira 2 ; Abdelgaffar, Heba 2 ; de Bortoli, Caroline Placidi 2 ; Raza, Ahmad 2 ; Jurat-Fuentes, Juan Luis 2 ;
作者机构： 1.Inst Food Safety & Nutr, Jiangsu Acad Agr Sci, Minist Agr & Rural Affairs, Jiangsu Key Lab Food Qual & Safety,State Key Lab C, Nanjing 210014, Peoples R China
2.Univ Tennessee, Dept Entomol & Plant Pathol, Knoxville, TN 37996 USA
关键词： Spodoptera frugiperda; ABC transporter; Cytotoxicity; Domains; Cry toxins; Receptors
期刊名称：PESTICIDE BIOCHEMISTRY AND PHYSIOLOGY （ 影响因子：4.7； 五年影响因子：4.7 ）
ISSN： 0048-3575
年卷期： 2024 年 199 卷
页码：
收录情况： SCI
摘要： The fall armyworm (Spodoptera frugiperda) is a major global pest causing severe damage to various crops, especially corn. Transgenic corn producing the Cry1F pesticidal protein from the bacterium Bacillus thuringiensis (Cry1F corn) showed effectiveness in controlling this pest until S. frugiperda populations at locations in North and South America evolved practical resistance. The mechanism for practical resistance involved disruptive mutations in an ATP binding cassette transporter subfamily C2 gene (SfABCC2), which serves as a functional Cry1F receptor in the midgut cells of susceptible S. frugiperda. The SfABCC2 protein contains two transmembrane domains (TMD1 and TMD2), each with a cytosolic nucleotide (ATP) binding domain (NBD1 and NBD2, respectively). Previous reports have demonstrated that disruptive mutations in TMD2 were linked with resistance to Cry1F, yet whether the complete SfABCC2 structure is needed for receptor functionality or if a single TMD-NBD protein can serve as functional Cry1F receptor remains unknown. In the present study, we separately expressed TMD1 and TMD2 with their corresponding NBDs in cultured insect cells and tested their Cry1F receptor functionality. Our results show that the complete SfABCC2 structure is required for Cry1F receptor functionality. Moreover, binding competition assays revealed that Cry1F specifically bound to SfABCC2, whereas neither SfTMD1-NBD1 nor SfTMD2-NBD2 exhibited any significant binding. These results provide insights into the molecular mechanism of Cry1F recognition by SfABCC2 in S. frugiperda, which could facilitate the development of more effective insecticidal proteins
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