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<p>Dorsal switch protein 1 (DSP1) is a ubiquitously expressed immune protein in insects. A previous study reported that DSP1 activated Toll pathway via the spätzle processing enzyme (SPE) to induce immune responses. SPE is the downmost component of the proteolytic cascade in <i>T. molitor</i>. The current study aimed to analyse the association of the upstream protease, modular serine protease (MSP) in the DSP1-induced Toll pathway in <i>T. molitor</i>. <i>Tm-MSP</i> was expressed in all stages of development, and larval tissues. Bacterial infection with <i>E. mundtii</i> significantly increased the level of <i>Tm-MSP</i> expression. However, silencing of the <i>Tm-MSP</i> via RNA interference (RNAi) significantly decreased the expression. Haemolytic nodulation, antimicrobial peptide (AMP) synthesis, phenoloxidase (PO) and phospholipase A<sub>2</sub> (PLA<sub>2</sub>) activity were also induced upon immune challenge. Injection of recombinant DSP1 (rDSP1) also showed the same phenomenon of immune challenge. Loss of function with RNAi of <i>Tm-MSP</i> indicated its involvement in mediating immune responses induced by DSP1. Additionally, RNAi of <i>Tm-MSP</i> significantly increased the susceptibility of <i>T. molitor</i> larvae upon immune challenge with Gram-positive <i>E. mundtii</i> but not with Gram-negative <i>X. hominickii</i>. But injection of rDSP1 attenuated the increased mortality in double stranded RNA control (dsCON) treated larvae but not in dsMSP-treated larvae. These results justified the role of <i>Tm-MSP</i> in activating the DSP1-induced Toll pathway.</p>

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Dorsal switch protein 1 activates toll immune signaling pathway via modular serine protease in Tenebrio molitor

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  • 发表日期：

    2026年5月25日

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  • Md. Mahi Imam Mollah

摘要

Dorsal switch protein 1 (DSP1) is a ubiquitously expressed immune protein in insects. A previous study reported that DSP1 activated Toll pathway via the spätzle processing enzyme (SPE) to induce immune responses. SPE is the downmost component of the proteolytic cascade in T. molitor. The current study aimed to analyse the association of the upstream protease, modular serine protease (MSP) in the DSP1-induced Toll pathway in T. molitor. Tm-MSP was expressed in all stages of development, and larval tissues. Bacterial infection with E. mundtii significantly increased the level of Tm-MSP expression. However, silencing of the Tm-MSP via RNA interference (RNAi) significantly decreased the expression. Haemolytic nodulation, antimicrobial peptide (AMP) synthesis, phenoloxidase (PO) and phospholipase A2 (PLA2) activity were also induced upon immune challenge. Injection of recombinant DSP1 (rDSP1) also showed the same phenomenon of immune challenge. Loss of function with RNAi of Tm-MSP indicated its involvement in mediating immune responses induced by DSP1. Additionally, RNAi of Tm-MSP significantly increased the susceptibility of T. molitor larvae upon immune challenge with Gram-positive E. mundtii but not with Gram-negative X. hominickii. But injection of rDSP1 attenuated the increased mortality in double stranded RNA control (dsCON) treated larvae but not in dsMSP-treated larvae. These results justified the role of Tm-MSP in activating the DSP1-induced Toll pathway.