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Functions of Bombyx mori cathepsin L-like in innate immune response and anti-microbial autophagy.

Abstract：

: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 I29 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.

journal_name

Dev Comp Immunol

journal_title

Developmental and comparative immunology

authors

Sun YX,Chen C,Xu WJ,Abbas MN,Mu FF,Ding WJ,Zhang HJ,Li J

doi

10.1016/j.dci.2020.103927

subject

Has Abstract

pub_date

2021-03-01 00:00:00

pages

103927

eissn

0145-305X

issn

1879-0089

pii

S0145-305X(20)30482-1

journal_volume

116

pub_type

杂志文章

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