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Molecular Characterization of Heat-Induced HSP11.0 and Master-Regulator HSF from Cotesia chilonis and Their Consistent Response to Heat Stress.

ABSTRACT: Small heat shock proteins (sHSPs) are members of the heat shock protein (HSP) family that play an important role in temperature stress, and heat shock factors (HSFs) are transcriptional activators that regulate HSP expression. Cotesia chilonis, the major endoparasitoid of Chilo suppressalis, modulates the C. suppressalis population in the field. In this study, we cloned and characterized two genes from C.chilonis: the heat-induced HSP11.0 gene (Cchsp11.0) that consisted of a 306-bp ORF, and the master regulator HSF (Cchsf) containing an 1875-bp ORF. CcHSP11.0 contained a chaperonin cpn10 signature motif that is conserved in other hymenopteran insects. CcHSF is a typical HSF and contains a DNA-binding domain, two hydrophobic heptad repeat domains, and a C-terminal trans-activation domain. Neither Cchsp11.0 or Cchsf contain introns. Real-time quantitative PCR revealed that Cchsp11.0 and Cchsf were highly induced at 36 °C and 6 °C after a 2-h exposure. Overall, the induction of Cchsf was lower than Cchsp11.0 at low temperatures, whereas the opposite was true at high temperatures. In conclusion, both Cchsp11.0 and Cchsf are sensitive to high and low temperature stress, and the expression pattern of the two genes were positively correlated during temperature stress.

SUBMITTER: He FJ

PROVIDER: S-EPMC8066536 | biostudies-literature |

REPOSITORIES: biostudies-literature

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Project description:BackgroundDuring oviposition many parasitoid wasps inject various factors, such as polydnaviruses (PDVs), along with eggs that manipulate the physiology and development of their hosts. These manipulations are thought to benefit the parasites. However, the detailed mechanisms of insect host-parasitoid interactions are not fully understood at the molecular level. Based on recent findings that some parasitoids influence gene expression in their hosts, we posed the hypothesis that parasitization by a braconid wasp, Cotesia chilonis, influences the expression of genes responsible for development, metabolism and immune functions in the fatbody and hemocytes of its host, Chilo suppressalis.Methodology/principal findingsWe obtained 39,344,452 reads, which were assembled into 146,770 scaffolds, and 76,016 unigenes. Parasitization impacted gene expression in fatbody and hemocytes. Of these, 8096 fatbody or 5743 hemocyte unigenes were down-regulated, and 2572 fatbody or 1452 hemocyte unigenes were up-regulated. Gene ontology data showed that the majority of the differentially expressed genes are involved in enzyme-regulated activity, binding, transcription regulator activity and catalytic activity. qPCR results show that most anti-microbial peptide transcription levels were up-regulated after parasitization. Expression of bracovirus genes was detected in parasitized larvae with 19 unique sequences identified from six PDV gene families including ankyrin, CrV1 protein, cystatin, early-expressed (EP) proteins, lectin, and protein tyrosine phosphatase.ConclusionsThe current study supports our hypothesis that parasitization influences the expression of fatbody and hemocyte genes in the host, C. suppressalis. The general view is that manipulation of host metabolism and immunity benefits the development and emergence of the parasitoid offsprings. The accepted beneficial mechanisms include the direct impact of parasitoid-associated virulence factors such as venom and polydnavirus on host tissues (such as cell damage) and, more deeply, the ability of these factors to influence gene expression. We infer that insect parasitoids generally manipulate their environments, the internal milieu of their hosts.

Project description:BackgroundA fundamental feature of parasitism is the nutritional exploitation of host organisms by their parasites. Parasitoid wasps lay eggs on arthropod hosts, exploiting them for nutrition to support larval development by using diverse effectors aimed at regulating host metabolism. However, the genetic components and molecular mechanisms at the basis of such exploitation, especially the utilization of host amino acid resources, remain largely unknown. To address this question, here, we present a chromosome-level genome assembly of the parasitoid wasp Cotesia chilonis and reconstruct its amino acid biosynthetic pathway.ResultsAnalyses of the amino acid synthetic pathway indicate that C. chilonis lost the ability to synthesize ten amino acids, which was confirmed by feeding experiments with amino acid-depleted media. Of the ten pathways, nine are known to have been lost in the common ancestor of animals. We find that the ability to synthesize arginine was also lost in C. chilonis because of the absence of two key genes in the arginine synthesis pathway. Further analyses of the genomes of 72 arthropods species show that the loss of arginine synthesis is common in arthropods. Metabolomic analyses by UPLC-MS/MS reveal that the temporal concentrations of arginine, serine, tyrosine, and alanine are significantly higher in host (Chilo suppressalis) hemolymph at 3 days after parasitism, whereas the temporal levels of 5-hydroxylysine, glutamic acid, methionine, and lysine are significantly lower. We sequence the transcriptomes of a parasitized host and non-parasitized control. Differential gene expression analyses using these transcriptomes indicate that parasitoid wasps inhibit amino acid utilization and activate protein degradation in the host, likely resulting in the increase of amino acid content in host hemolymph.ConclusionsWe sequenced the genome of a parasitoid wasp, C. chilonis, and revealed the features of trait loss in amino acid biosynthesis. Our work provides new insights into amino acid exploitation by parasitoid wasps, and this knowledge can specifically be used to design parasitoid artificial diets that potentially benefit mass rearing of parasitoids for pest control.

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Molecular Characterization of Heat-Induced HSP11.0 and Master-Regulator HSF from Cotesia chilonis and Their Consistent Response to Heat Stress.

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