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Serpin-15 from Bombyx mori inhibits prophenoloxidase activation and expression of antimicrobial peptides
Dongran Liu1, Lei Wang1, Liu Yang1
1College of Life Science, Anhui Agricultural University, Hefei 230036, China.
Abstract:
Serine protease inhibitors (SPIs) play a key role in physiological responses by controlling protease activities. In this study, we studied the biochemical functions of serpin-15, an SPI, from Bombyx mori (Bmserpin-15). Recombinant Bmserpin-15 was expressed in Escherichia coli cells and used to raise rabbit anti-Bmserpin-15 polyclonal antibodies. Bmserpin-15 mRNA and protein expression was detected in all tested tissues, particularly in the fat body and silk gland. After challenge with four different microorganisms (Escherichia coli, Beauveria bassiana, Micrococcus luteus and B. mori nuclear polyhedrosis virus), the expressions of Bmserpin-15 mRNA and protein were induced significantly, particularly by B. bassiana and M. luteus. Recombinant Bmserpin-15 inhibited prophenoloxidase activation, but did not affect phenoloxidase activity, in B. mori hemolymph. Injection of recombinant Bmserpin-15 into B. mori larvae reduced significantly the transcript levels of antimicrobial peptides in fat body. Our results suggested that Bmserpin-15 plays an important role in the innate immunity of B. mori.
Insights
Serine protease inhibitors regulate physiological functions. This study shows Bombyx mori serpin-15 (Bmserpin-15) is crucial for innate immunity, particularly against fungal and bacterial infections.
Area of Science:
- Insect immunology
- Biochemistry
- Molecular biology
Background:
- Serine protease inhibitors (SPIs) are vital regulators of protease activity in physiological processes.
- Understanding the specific roles of SPIs in insects like Bombyx mori is essential for comprehending their immune defense mechanisms.
Purpose of the Study:
- To investigate the biochemical functions and immune role of serpin-15 (Bmserpin-15) from the silkworm, Bombyx mori.
- To characterize the expression patterns and immune-induced regulation of Bmserpin-15.
Main Methods:
- Recombinant Bmserpin-15 was produced in Escherichia coli.
- Bmserpin-15 expression was analyzed in various tissues and after microbial challenge.
- Functional assays were performed on prophenoloxidase activation and antimicrobial peptide expression.
Main Results:
- Bmserpin-15 mRNA and protein were expressed in multiple tissues, with high levels in the fat body and silk gland.
- Expression of Bmserpin-15 was significantly induced by Beauveria bassiana and Micrococcus luteus.
- Recombinant Bmserpin-15 inhibited prophenoloxidase activation and reduced antimicrobial peptide transcript levels in Bombyx mori.
Conclusions:
- Bmserpin-15 plays a significant role in the innate immune response of Bombyx mori.
- Bmserpin-15 contributes to immune defense by modulating prophenoloxidase activation and antimicrobial peptide production.
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