Transcriptome profiling and in silico docking analysis of phosphine resistance in rice weevil, Sitophilus oryzae (Coleoptera: Curculionidae)

Author:

Selvapandian Upasna1,Nallusamy Saranya2,Singh Sonu Kumar1,Mannu Jayakanthan2,Shanmugam Varanavasiappan1,Ravikumar Caroline2,Subbarayalu Mohankumar1ORCID

Affiliation:

1. Department of Plant Biotechnology, Centre for Plant Molecular Biology & Biotechnology, Tamil Nadu Agricultural University , Coimbatore , India

2. Department of Plant Molecular Biology and Bioinformatics, Centre for Plant Molecular Biology & Biotechnology, Tamil Nadu Agricultural University , Coimbatore , India

Abstract

Abstract The rice weevil, Sitophilus oryzae (Linnaeus, Coleoptera: Curculionidae), is a serious cosmopolitan pest that affects grain in storage and has developed high levels of resistance toward phosphine. In this study, RNA-seq data was used to study the phosphine resistance mechanisms in S. oryzae. Resistant and susceptible populations of S. oryzae were identified based on phosphine bioassays conducted in 32 populations collected across Tamil Nadu, India. Differential expression of mitochondrial (COX1, COX2, COX3, ND2, ND3, ATP6, and ATP8) and detoxification genes (Cyps, Gsts, and Cbe) were observed in the resistant and susceptible populations of S. oryzae. The previously characterized phosphine resistant gene, dld (dihydrolipoamide dehydrogenase) linked to the rph2 locus, was found to be up-regulated in resistant S. oryzae population (ISO-TNAU-RT) treated with phosphine. Also, the genes involved in Tricarboxylic acid (TCA) cycle were significantly down-regulated. In addition, a significant up-regulation in the expression of the antioxidant enzymes superoxide dismutase (2.5×) and catalase (2.1×) in ISO-TNAU-RT populations was recorded. Furthermore, a distinct amino acid substitution, Lysine > Glutamic acid (K141E) was identified in resistant phenotypes. In silico docking studies of both resistant and susceptible DLD protein with phosphine molecule revealed that the amino acid residues involved in the interaction were different. This suggested that the amino acid substitution might lead to structural modifications which reduces the affinity of the target (phosphine). This study provides insight on the various genes, pathways, and functional mechanisms having a significant role in phosphine resistance in S. oryzae.

Funder

GOI

Publisher

Oxford University Press (OUP)

Subject

Insect Science,General Medicine

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