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For a half-century, the commercial wild silkworm, Antheraea pernyi, has been protected by coumaphos, which is an internal organophosphorus insecticide used to kill the potential parasitic fly larvae inside. Knowledge about the detoxification genes of A. pernyi as well as the detoxification mechanism for this species remains severely limited. In this study, we identified 281 detoxification genes (32 GSTs, 48 ABCs, 104 CYPs, and 97 COEs) in the genome of this insect, which are unevenly distributed over 46 chromosomes. When compared to the domesticated silkworm, Bombyx mori, a lepidopteran model species, A. pernyi has a similar number of ABCs, but a greater number of GSTs, CYPs, and COEs. By transcriptome-based expression analysis, we found that coumaphos at a safe concentration level significantly changed the pathways related to ATPase complex function and the transporter complex in A. pernyi. KEGG functional enrichment analysis indicated that protein processing in the endoplasmic reticulum was the most affected pathway after coumaphos treatment. Finally, we identified four significantly up-regulated detoxification genes (ABCB1, ABCB3, ABCG11, and ae43) and one significantly down-regulated detoxification gene (CYP6AE9) in response to coumaphos treatment, suggesting that these five genes may contribute to detoxification of coumaphos in A. pernyi. Our study provides the first set of detoxification genes for wild silkworms from Saturniidae and highlights the importance of detoxification gene repertoire in insect pesticide tolerance. [ABSTRACT FROM AUTHOR]

Abstract: A gene encoding phosphoserine aminotransferase from Antheraea pernyi (ApPSAT) was isolated and characterized, and its value for phylogenetic inference was assessed. The resulting 1309 bp cDNA sequence contains an open reading frame of 1095 bp encoding a polypeptide of 364 amino acids, with 58% sequence identity to that from Homo sapiens. RT-PCR analysis showed that the ApPSAT gene was transcribed at four developmental stages, and in all examined tissues with the most abundance in malpighian tubules. Sequence alignment suggested that ApPSAT protein sequence exhibited 41–87% homology with the known PSATs from bacteria, fungi, plants, invertebrates and vertebrates. Phylogenetic analysis revealed that 37 representative PSAT protein sequences were well divided into five groups corresponding to the known fungi, bacteria, plants, invertebrates and vertebrates. The phylogenetic relationships obtained were consistent with the traditional classification and other molecular data, suggesting the potential value of the PSAT protein in phylogenetic inference. [Copyright &y& Elsevier]

Abstract: The complete A+T-rich region of mitochondrial DNA has been cloned and sequenced from Antheraea pernyi (Lepidoptera: Saturniidae). Nine haplotypes were obtained from 16 inbred strains of the domesticated type with the range from 550 to 554 bp in size, exhibiting a low degree of sequence divergence from 0.18 to 0.91%. Two haplotypes were observed from three individuals of the wild type with 516 or 517 bp, respectively, showing a length polymorphism and a relatively high degree of sequence divergence compared with those of the domesticated type. Phylogenetic analysis showed the presence of two clearly differentiated mitochondrial clades: the domesticated type and the wild type. The length polymorphism between the two types was caused by the presence of a variable number of tandemly repeated units. Several conserved structural elements previously described in other insects were also present in the A. pernyi A+T-rich region. Moreover, two tRNA-like structures were observed in this region. [Copyright &y& Elsevier]

Abstract: Myosin light chain 2 (MLC-2) gene was isolated and characterized from Antheraea pernyi, a well-known wild silkmoth. The isolated cDNA sequence is 905 bp in length with an open reading frame of 612 bp encoding a polypeptide of 203 amino acids. Semi-quantitative RT-PCR analysis showed that the MLC-2 gene was transcribed during four developmental stages (egg, larva, pupa, and moth), and present in all tissues tested. Alignment analysis revealed that the deduced protein sequence has over 95% identity to myosin light chain 2 of lepidopteran species, and 57–88% identity to other insect species, suggesting that insect MLC-2 proteins are highly conserved throughout evolution. The protein sequence was used to construct phylogenetic trees with other known vertebrate and invertebrate MLC-2 sequences, and the obtained trees demonstrated similar topology with the classical systematics, indicating the potential value of MLC-2 gene in phylogenetic study. [ABSTRACT FROM AUTHOR]