Molecular characterization and expression profiles of nicotinic acetylcholine receptors in the rice striped stem borer, Chilo suppressalis （Lepidoptera： Crambidae）

Nicotinic acetylcholine receptors （nAChRs） are members of the cys-loop ligand- gated ion channel （cysLGIC） superfamily, mediating fast synaptic cholinergic transmission in the central nervous system in insects. Insect nAChRs are the molecular targets of economically important insecticides, such as neonicotinoids and spinosad. Identification and characterization of the nAChR gene family in the rice striped stem borer, Chilo suppressa[is, could provide beneficial information about this important receptor gene family and contribute to the investigation of the molecular modes of insecticide action and resistance for current and future chemical control strategies. We searched our C. suppressalis transcriptome database using Bombyx mori nAChR sequences in local BLAST searches and obtained the putative nAChR subunit complementary DNAs （cDNAs） via reverse transcription polymerase chain reaction （RT-PCR） and rapid amplification of cDNA ends methods. Similar to B. mori, C. suppressalis possesses 12 nAChR subunits, including nine c^-type and three/%type subunits. Quantitative RT-PCR analysis revealed the expression profiles of the nAChR subunits in various tissues, including the brain, subesophageal ganglion, thoracic ganglion, abdominal ganglion, hemocytes, fat body, foregut, midgut, hindgut and Malpighian tubules. Developmental expression analyses showed clear differential expression of nAChR subunits throughout the C. suppressalis life cycle. The identification of nAChR subunits in this study will provide a foundation for investigating the diverse roles played by nAChRs in C. suppressalis and for exploring specific target sites for chemicals that control agricultural pests while sparing beneficial species

An endoparasitoid uses its egg surface proteins to regulate its host immune response

With proteomic analysis,we identified 379 egg surface proteins from an endoparasitoid,Cotesia chilonis.Proteins containing conserved enzymatic domains constitute a large proportion of egg surface components.Some proteins,such as superoxidase dismutase,homolog of C.rubecula 32-kDa protein,and immunoevasive protein-2A,are classical parasitism factors that have known functions in host immunity regulation.Melanization assays revealed that a novel egg surface protein,C.chilonis egg surface serpin domain-containing protein had the same function as a C.chilonis venom serpin,as both suppressed host melanization in a dose-dependent manner.C.chilonis egg surface serpin domain-containing protein is mainly transcribed in C.chilonis oocytes with follicular cells,and it is located on both the anterior and posterior sides of the mature egg surface.Additionally,we used LC-MS/MS to identify 586 binding proteins sourced from C.suppressalis plasma located on the eggshell surface of C.chilonis,which included some immunity-related proteins.These results not only indicate that C.chilonis uses its egg surface proteins to reduce the immune response of its host but also imply that endoparasitoid egg surface proteins might be a new parasitism factor involved in host immune regulation.