期刊
DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY
卷 116, 期 -, 页码 -出版社
ELSEVIER SCI LTD
DOI: 10.1016/j.dci.2020.103927
关键词
Cathepsin L; Innate immune response; Autophagy; Bombyx mori
资金
- Youth Project of Anhui Natural Science Foundation [1908085QC94]
- General Project of Anhui Natural Science Foundation [1908085MC86]
- General Program of Anhui Higher Education Natural Science Foundation [KJ2020B22]
Cathepsin L-like protease in silkworm plays a significant role in innate immune response and anti-microbial autophagy. It is highly expressed in the fat body and its expression is induced by 20-hydroxyecdysone. Suppression of cathepsin L-like alters the expression of immune-related genes and autophagy-related genes, indicating its regulatory function in innate immunity and autophagy in silkworm. Fluorescence microscopic analysis reveals the localization of cathepsin L-like in the cytoplasm and its activation and dispersion upon induction of anti-microbial autophagy.
Cathepsins belongs to the cysteine protease family, which are activated by an acidic environment. They play essential biological roles in the innate immunity and development of animals. Here, we identified a 62 kDa cathepsin L-like protease from the silkworm Bombyx mori. It contained putative conserved domains, including an 129 inhibitor domain and a peptidase C1A domain. The expression analysis revealed that cathepsin L-like was highly produced in the fat body, and 20-hydroxyecdysone (20 E) induced its expression. After challenge with three different types of heat-killed pathogens (Escherichia coli, Beauveria bassiana, and Bacillus cereus), the mRNA levels of cathepsin L-like significantly increased and displayed variable expression patterns in the immune tissues, suggesting its potential role in the innate immune response. The suppression of cathepsin L-like altered the expression of immune-related genes associated with the Toll and IMD pathway. Besides, autophagy-related genes such as Atg6, Atg8, VAMP2, Vps4, and syntaxin expression were also altered, indicating that cathepsin L-like regulates innate immunity and autophagy. Fluorescence microscopic analysis exhibited that cathepsin L-like was localized in the cytoplasm, and it was activated and dispersed throughout the cytoplasm and nucleus following the induction of anti-microbial autophagy. Altogether, our data suggest that cathepsin L-like may regulate the innate immune response and anti-microbial autophagy in the silkworm, B. mori.
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