The wolf spider Pardosa pseudoannulata is a dominant predator in paddy ecosystem and an important biological control agent of rice pests. Temperature represents a primary factor influencing its biology and behavior, although the underlying molecular mechanisms remain unknown. To understand the response of P. pseudoannulata to temperature stress, we performed comparative transcriptome analyses of spider adults exposed to 10°C and 40°C for 12 h. We obtained 67,725 assembled unigenes, 21,765 of which were annotated in P. pseudoannulata transcriptome libraries, and identified 905 and 834 genes significantly up‐ or down‐regulated by temperature stress. Functional categorization revealed the differential regulation of transcription, signal transduction, and metabolism processes. Calcium signaling pathway and metabolic pathway involving respiratory chain components played important roles in adapting to low temperature, whereas at high temperature, oxidative phosphorylation and amino acid metabolism were critical. Differentially expressed ribosomal protein genes contributed to temperature stress adaptation, and heat shock genes were significantly up‐regulated. This study represents the first report of transcriptome identification related to the Araneae species in response to temperature stress. These results will greatly facilitate our understanding of the physiological and biochemical mechanisms of spiders in response to temperature stress.
Vitellogenin (Vg) and vitellogenin receptor (VgR) play important roles in the vitellogenesis of insects. In this study, we cloned and characterized the two corresponding genes (TpVg and TpVgR) in an economically important insect, Thitarodes pui (Lepidoptera: Hepialidae), from the Tibetan plateau. The full length of TpVg is 5566 bp with a 5373 bp open reading frame (ORF) encoding 1,790 amino acids. Sequence alignment revealed that TpVg has three conserved domains: a Vitellogenin_N domain, a DUF1943 domain, and a von Willebrand factor type D domain (VWD). The full length of TpVgR is 5732 bp, with a 5397 bp ORF encoding 1798 amino acids. BLASTP showed that TpVgR belongs to the low-density lipoprotein receptor (LDLR) gene superfamily. Structural analysis revealed that TpVgR has a group of four structural domains: a ligand-binding domain (LBD), an epidermal growth factor (EGF)–precursor homology domain, a transmembrane (TM) domain, and a cytoplasmic domain. In addition, TpVgR has four cysteine-rich LDL repeats in the first ligand-binding site and seven in the second. Quantitative real-time polymerase chain reaction analysis revealed that the expression levels of TpVg and TpVgR are much higher in later pupa than in either the larval or adult stage, implying that the synthesis and uptake of Vg in T. pui occurs in the later pupal stage. These results will help us to understand the molecular mechanism of the reproductive capacity and will provide new insight into the mass rearing and utilization of T. pui.
The wolf spider Pardosa pseudoannulata (Araneae: Lycosidae) is an important biological control agent against rice pests in the paddy ecosystem. Vitellogenin (Vg) is the precursor of the yolk protein and is crucial for reproduction in P. pseudoannulata. We have identified three full‐length cDNAs encoding vitellogenins. The PpVg1 transcript is 5598 bp long, with an open reading frame (ORF) of 5379 bp encoding a 1792 amino acid protein. The PpVg2 transcript is 5394 bp long, with an ORF of 5205 bp encoding a 1734 amino acid protein. The PpVg3 transcript is 5229 bp long, with an ORF of a 5019 bp encoding a 1672 amino acid protein. Typical domains are found in all PpVgs sequences, including an N‐terminal lipoprotein domain, a DUF1943 domain and the von Willebrand factor type D domain. Phylogenetic analysis indicates that PpVg1, PpVg2 and PpVg3 are grouped with other arachnid Vgs. PpVg1 and PpVg2 are more closely related to Parasteatoda tepidariorum vitellogenin, whereas PpVg3 is segregated into a single clade in the arachnid group. Expression analysis by a quantitative reverse transcriptase‐polymerase chain reaction shows that PpVg1, PpVg2 and PpVg3 are mainly expressed in adult females. Mating elicite an increase in the transcription levels of PpVg1 and PpVg2, and the expression level of PpVg3 is up‐regulated after first oviposition. The present study represents the first report with respect to the molecular characterization and expression patterns for the spider vitellogenin and will greatly facilitate our understanding of the molecular mechanisms of P. pseudoannulata reproduction.
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