Characterization and expression profiling of serine protease inhibitors in the yellow mealworm Tenebrio molitor. Issue 3 (24th June 2022)

• Record Type: Journal Article
• Authors: Li, Guang‐Ya; Yang, Lin; Xiao, Kai‐Ran; Song, Qi‐Sheng; Stanley, David; Wei, Shu‐Jun; Zhu, Jia‐Ying
• Other Names: Zhu Jia‐Ying guestEditor.; Song Qisheng guestEditor.; Stanley David guestEditor.
• Is Part Of: Archives of insect biochemistry and physiology. Volume 111:Issue 3(2022)
• Page Start: n/a
• Page End: n/a
• Publication Date: 2022-06-24
• Subjects: expression profile -- serine protease inhibitor -- serpin -- Tenebrio molitor; Insects -- Physiology -- Periodicals; Insect biochemistry -- Periodicals; 595.701572
• DOI: 10.1002/arch.21948
• Languages: English
• ISSNs: 0739-4462

Abstract

Abstract: Serine protease inhibitors (SPIs) act in diverse biological processes in insects such as immunity, development, and digestion by preventing the unwanted proteolysis. So far, the repertoire of genes encoding SPIs has been identified from few insect species. In this study, 62 SPI genes were identified from the genome of the yellow mealworm, Tenebrio molitor . According to their modes of action, they were classified into three families, serpin (26), canonical SPI (31), and α‐macroglobulins (A2M) (5). These SPIs feature eight domains including serpin, Kazal, TIL, Kunitz, WAP, Antistasin, pacifastin, and A2M. In total, 39 SPIs contain a single SPI domain, while the others encode at least two inhibitor units. Based on the amino acids in the cleaved reactive sites, the abilities of these SPIs to inhibit trypsin, chymotrypsin, or elastase‐like enzymes are predicted. The expression profiling based on the RNA‐seq data showed that these genes displayed stage‐specific expression patterns during development, suggesting to us their significance in development. Some of the SPI genes were exclusively expressed in particular tissues such as hemocyte, fat body, gut, ovary, and testis, which may be involved in biological processes specific to the indicated tissues. These findings provide necessary information for further investigation of insect SPIs. Abstract : Serine protease inhibitor genes were identified in the Tenebrio molitor genome. Multiple domains were detected in the sequences of their encoded proteins. Their mRNA levels were highly or specifically expressed in various tissues. Research Highlights: Sixty‐two serine protease inhibitors (SPIs) were identified in the genome of the yellow mealworm. Domains encoded by SPIs and their inhibitory ability to trypsin, chymotrypsin, or elastase‐like enzymes were predicted. Profiling of SPI gene expression at different life stages and in various tissues illuminated their functions.