The tobacco cutworm, Spodoptera litura, is among the most widespread and destructive agricultural pests, feeding on over 100 crops throughout tropical and subtropical Asia. By genome sequencing, physical mapping and transcriptome analysis, we found that the gene families encoding receptors for bitter or toxic substances and detoxification enzymes, such as cytochrome P450, carboxylesterase and glutathione-S-transferase, were massively expanded in this polyphagous species, enabling its extraordinary ability to detect and detoxify many plant secondary compounds. Larval exposure to insecticidal toxins induced expression of detoxification genes, and knockdown of representative genes using short interfering RNA (siRNA) reduced larval survival, consistent with their contribution to the insect’s natural pesticide tolerance. A population genetics study indicated that this species expanded throughout southeast Asia by migrating along a South India–South China–Japan axis, adapting to wide-ranging ecological conditions with diverse host plants and insecticides, surviving and adapting with the aid of its expanded detoxification systems. The findings of this study will enable the development of new pest management strategies for the control of major agricultural pests such as S. litura.
SummaryWe have constructed a linkage map of random amplified polymorphic DNAs (RAPDs) in Bombyx mori. We screened 320 10-mer primers, and found 243 clear polymorphic bands between C108 and p50 strains. In the F2 generation, segregation ratios of 168 bands were nearly 3:1 in a chi square test, showing Mendelian inheritance. The MAPMAKER program sorted 168 bands into 29 linkage groups and 10 unlinked loci at minimum LOD score 3·0, and determined orders of loci in each group, which contained 2–11 markers. It also detected typing errors in our data. We calculated map distances between pairs of neighbouring loci using recombination values in males and the Kosambi mapping function. Our RAPD map consists of 169 loci including the p locus, and the sum of map distances is approximately 900 cM. Linkage groups 1 and 2 of our map correspond to chromosomes 1 and 2 on the conventional linkage map because of linkage to sex and p, respectively.
α-Amylase is a common enzyme for hydrolyzing starch. In the silkworm, Bombyx mori L. (Lepidoptera: Bombycidae), α-amylase is found in both digestive fluid and hemolymph. Here, the complete genomic sequence of the Amy gene encoding α-amylase from a local Thai silkworm, the Nanglai strain, was obtained. This gene was 7981 bp long with 9 exons. The full length Amy cDNA sequence was 1749 bp containing a 1503 bp open reading frame. The ORF encoded 500 amino acid residues. The deduced protein showed 81–54% identity to other insect α-amylases and more than 50% identity to mammalian enzymes. Southern blot analysis revealed that in the Nanglai strain Amy is a single-copy gene. RT- PCR showed that Amy was transcribed only in the foregut. Transgenic B. mori also showed that the Amy promoter activates expression of the transgene only in the foregut.
Degumming is the process of removing the sericin or gum from silk yarn. Removing the gum improves the sheen, color, hand, and texture of the silk. Mai 1 silk yarn from Thai hybrid multivoltine Bombyx mori was degummed with commercial grade bromelain and with sodium carbonate. 96.58% of sericin content was removed from the silk yarn in small scale degumming procedure with 2 g/L bromelain and 91.84 % in large scale degumming with 5 g/L bromelain. Scanning electron micrographs of the silk yarn degummed with enzyme showed neither sign of destruction in its morphology nor surface damage. The surface of the yarn degummed with bromelain was smoother than that of the yarn degummed with sodium carbonate. According to the evaluation of its mechanical properties using Kawabata Evaluation System for Fabric, the silk fabric degummed with bromelain showed good tensile strength, better response to bending deformation, higher flexibility, smother feel during bending, and softer and better elastic properties during compression.
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