Characterization and expression profiling of serine protease inhibitors in the yellow mealworm Tenebrio molitor.

Autor: Li GY; Key Laboratory of Forest Disaster Warning and Control of Yunnan Province, Southwest Forestry University, Kunming, China., Yang L; Key Laboratory of Forest Disaster Warning and Control of Yunnan Province, Southwest Forestry University, Kunming, China., Xiao KR; Key Laboratory of Forest Disaster Warning and Control of Yunnan Province, Southwest Forestry University, Kunming, China., Song QS; Division of Plant Science and Technology, University of Missouri, Columbia, Missouri, USA., Stanley D; USDA/ARS Biological Control of Insects Research Laboratory, Columbia, Missouri, USA., Wei SJ; Key Laboratory of Forest Disaster Warning and Control of Yunnan Province, Southwest Forestry University, Kunming, China.; Institute of Plant Protection, Beijing Academy of Agriculture and Forestry Sciences, Beijing, China., Zhu JY; Key Laboratory of Forest Disaster Warning and Control of Yunnan Province, Southwest Forestry University, Kunming, China.; Key Laboratory for Forest Resources Conservation and Utilization in the Southwest Mountains of China, Ministry of Education, Southwest Forestry University, Kunming, China.
Jazyk: angličtina
Zdroj: Archives of insect biochemistry and physiology [Arch Insect Biochem Physiol] 2022 Nov; Vol. 111 (3), pp. e21948. Date of Electronic Publication: 2022 Jun 24.
DOI: 10.1002/arch.21948
Abstrakt: 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.
(© 2022 Wiley Periodicals LLC.)
Databáze: MEDLINE
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