Identification and expression profiling of serine protease-related genes in Tenebrio molitor

In insects, serine proteases and serine protease homologs (SPs/SPHs) are involved in a variety of physiological processes including digestion, development, and immunity. Here, we identified 112 SP and 88 SPH genes in the genome of the yellow mealworm, Tenebrio molitor. Based on the features of domain structure, they were divided into S group containing single Tryp-SPc or Tryp-SPHc domain, C group containing 1-4 CLIP domain (CLIPA-D) and M group containing the CBD, CUB, EGF, Fz, Gd, LDLa, PAN, SEA, SR, Sushi, and TSP domains, and have 115, 48, and 37 gene members, respectively. According to the active sites in the catalytic triad, the putative trypsin, chymotrypsin, or elastase-like enzyme specificity of the identified SPs/SPHs were predicted. Phylogenetic and genomic location analyses revealed that gene duplication exists in the large amount of SPs/SPHs. Gene expression profiling using RNA-seq data along with real time reverse transcription-polymerase chain reaction analysis showed that most SP/SPH genes display life stage specific expression patterns, indicating their important roles in development. Many SP/SPH genes are specifically or highly expressed in the gut, salivary gland, fat body, hemocyte, ovary, and testis, suggesting that they participate in digestion, immunity, and reproduction. The findings lay the foundation for further functional characterization of SPs/SPHs in T. molitor.

Automated summary

Serine proteases and serine protease homologs (SPs/SPHs) play important roles in various physiological processes in insects. In this study, a total of 112 SP and 88 SPH genes were identified in the genome of the yellow mealworm. These genes were classified into different groups based on their domain structure and showed stage-specific expression patterns. The findings provide a foundation for further understanding the functions of SPs/SPHs in T. molitor.