Parasitoid wasps depend on a variety of maternal virulence factors to ensure successful parasitism. Encapsulation response carried out by host hemocytes is one of the major host immune responses toward limiting endoparasitoid wasp offspring production. We found that VRF1, a metalloprotease homolog venom protein identified from the endoparasitoid wasp, Microplitis mediator, could modulate egg encapsulation in its host, the cotton bollworm, Helicoverpa armigera. Here, we show that the VRF1 proenzyme is cleaved after parasitism, and that the C-terminal fragment containing the catalytic domain enters host hemocytes 6 h post-parasitism. Furthermore, using yeast two-hybrid and pull-down assays, VRF1 is shown to interact with the H. armigera NF-κB factor, Dorsal. We also show that overexpressed of VRF1 in an H. armigera cell line cleaved Dorsal in vivo. Taken together, our results have revealed a novel mechanism by which a component of endoparasitoid wasp venom interferes with the Toll signaling pathway in the host hemocytes.
Recently, parasitoid wasp species Microplitis mediator has evoked increasing research attention due to its possible use in the control of Lepidoptera insects. Because insect development involves changes in cuticle composition, identification and expression analysis of M. mediator cuticular proteins may clarify the mechanisms involved in parasite development processes. We found 70 cuticular proteins from the M. mediator transcriptome and divided them into seven distinct families. Expression profiling indicated that most of these cuticular protein genes have expression peaks specific for one particular developmental stage of M. mediator. Eggs and pupae have the highest number of transcriptionally active cuticular protein genes (47 and 52 respectively). Only 12 of these genes maintained high expression activity during late larval development. Functional analysis of two larval proteins, MmCPR3 and MmCPR14, suggested their important role in the proper organization of the cuticle layers of larvae. During M. mediator larval development, normal cuticle formation can be supported by a limited number of cuticular proteins.
White L. vannamei have become the most widely cultivated shrimp species worldwide. Cultivation of L. vannamei is one of the predominant sectors in China’s aquaculture industry. This study focused on the physiological and biochemical responses, differential protein expression, and expression characteristics of the related crucial functional protein genes under low oxygen conditions among different strains of L. vannamei. It was found that 6 h of hypoxic stress caused a significant reduction in the total hemocyte number in both strains, while the hypoxia-sensitive strain showed a stronger reduction. In contrast, the hemocyanin concentration showed only an overall upward trend. Proteomic analysis of L. vannamei muscle tissue revealed 3,417 differential proteins after 12 h of hypoxic stress. Among them, 29 differentially expressed proteins were downregulated and 244 were upregulated in the hypoxia-sensitive strain. In contrast, there were only 10 differentially expressed proteins with a downregulation pattern and 25 with an upregulation pattern in the hypoxia-tolerant strain. Five protein genes that responded significantly to hypoxic stress were selected for quantitative real-time PCR analysis, namely, hemocyanin, chitinase, heat shock protein 90 (HSP 90), programmed death protein, and glycogen phosphorylase. The results showed that the gene expression patterns were consistent with proteomic experimental data except for death protein and glycogen phosphorylase. These results can enrich the general knowledge of hypoxic stress in L. vannamei and the information provided differentially expressed proteins which may be used to assist breeding programs of L. vannamei of new strains with tolerance to hypoxia.
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