TIL-type protease inhibitors may be used as targeted resistance factors to enhance silkworm defenses against invasive fungi

Li, Youshan; Zhao, Ping; Liu, Huawei; Guo, Xiaomeng; He, Huawei; Zhu, Rui; Zhang, Xiang; Xia, Qingyou

doi:10.1016/j.ibmb.2014.11.006

Cited by 46 publications

(47 citation statements)

References 43 publications

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“…In the immersion experiment, a larger number of SPI genes such as BmSPI38 (BGIBMGA009094), protease inhibitor 4 (BGIBMGA008711) and kazal-type proteinase inhibitor (BGIBMGA011573) were up-regulated in K8 strain. BmSPI38 and BmSPI39 could inhibit the germination of B. bassiana conidia and markedly improve the survival rate of silkworm hosts [28,29]. The up-regulated SPIs in the K8 strain may help to inhibit the germination of B. bassiana conidia and thus delay or prevent invasion.…”

Section: Discussionmentioning

confidence: 99%

RNA-Seq Analyses for Two Silkworm Strains Reveals Insight into Their Susceptibility and Resistance to Beauveria bassiana Infection

Xing

Yang

Jiang

et al. 2017

IJMS

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The silkworm Bombyx mori is an economically important species. White muscardine caused by Beauveria bassiana is the main fungal disease in sericulture, and understanding the silkworm responses to B. bassiana infection is of particular interest. Herein, we investigated the molecular mechanisms underlying these responses in two silkworm strains Haoyue (HY, sensitive to B. bassiana) and Kang 8 (K8, resistant to B. bassiana) using an RNA-seq approach. For each strain, three biological replicates for immersion treatment, two replicates for injection treatment and three untreated controls were collected to generate 16 libraries for sequencing. Differentially expressed genes (DEGs) between treated samples and untreated controls, and between the two silkworm strains, were identified. DEGs and the enriched Kyoto Encyclopedia of Genes and Genomes (KEGG) pathways of the two strains exhibited an obvious difference. Several genes encoding cuticle proteins, serine proteinase inhibitors (SPI) and antimicrobial peptides (AMP) and the drug metabolism pathway involved in toxin detoxification were considered to be related to the resistance of K8 to B. bassiana. These results revealed insight into the resistance and susceptibility of two silkworm strains against B. bassiana infection and provided a roadmap for silkworm molecular breeding to enhance its resistance to B. bassiana.

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Section: Discussionmentioning

confidence: 99%

RNA-Seq Analyses for Two Silkworm Strains Reveals Insight into Their Susceptibility and Resistance to Beauveria bassiana Infection

Xing

Yang

Jiang

et al. 2017

IJMS

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“…Comparative proteomics of B. mori silk revealed the presence of abundant cysteinerich protease inhibitors, particularly TIL-type protease inhibitors (Dong et al, 2013). Their inhibitory activities against microbial proteases and conidial germination have been demonstrated in our previous studies (Li et al, 2012;Li et al, 2015). Their inhibitory activities against microbial proteases and conidial germination have been demonstrated in our previous studies (Li et al, 2012;Li et al, 2015).…”

Section: Discussionmentioning

confidence: 68%

“…Activity staining (Li et al, 2012;Li et al, 2015) of protease inhibitors was performed as previously described.…”

Section: Activity Stainingmentioning

confidence: 99%

“…Two similar serine proteinase inhibitors, BmSPI1 and BmSPI2, have been identified from the silk gland of B. mori, which suggests the protection of the silk cocoon from microbial proteases (Nirmala et al, 2001b). Furthermore, two B. mori TIL-type protease inhibitors, BmSPI38 and BmSPI39, can suppress conidial germination and integument penetration by inhibiting cuticle-degrading proteases that are secreted by entomopathogenic fungi, and could be targeted as fungal-resistance factors in the silkworm (Li et al, 2012;Li et al, 2015). Furthermore, two B. mori TIL-type protease inhibitors, BmSPI38 and BmSPI39, can suppress conidial germination and integument penetration by inhibiting cuticle-degrading proteases that are secreted by entomopathogenic fungi, and could be targeted as fungal-resistance factors in the silkworm (Li et al, 2012;Li et al, 2015).…”

Section: Introductionmentioning

confidence: 99%

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Protease inhibitors in Bombyx mori silk might participate in protecting the pupating larva from microbial infection

Liu

Zhu

et al. 2015

Insect Science

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Pupae inside cocoons rarely suffer from disease. It is apparent that some factors in the cocoon exert antimicrobial effects whereby the pupae inside can be protected from microbial infection. In the present study, we investigated the expression of cocoon protease inhibitors using immunoblotting and activity staining. Enzymatic hydrolysis of cocoon proteins in vitro was performed to characterize their roles in protecting the cocoon from microbial proteases. We found that some protease inhibitors, particularly trypsin inhibitor-like (TIL)-type protease inhibitors, can be secreted into the cocoon layer during the spinning process, thereby providing effective protection to the cocoon and pupa by inhibiting the extracellular proteases that can be secreted by pathogens.

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“…In addition to antimicrobial peptides, a large number of protein components involved in this defence system have been characterized, including Toll receptors, phenoloxidases, complement factors, protease inhibitors and other humoral factors (Iwanaga & Lee, ). As many pathogens have been shown to synthesize and secrete abundant extracellular proteases during invasion (St. Leger, ; Travis et al, ), the host must, in turn, produce large amounts of protease inhibitors in response (Clermont et al, ; Armstrong, ; Donpudsa et al, ; Li et al, ). Unfortunately, the current understanding of these protease inhibitors is limited, particularly in the silkworm.…”

Section: Introductionmentioning

confidence: 99%

The fungal‐resistance factors BmSPI38 and BmSPI39 predominantly exist as tetramers, not monomers, in Bombyx mori

Dong

Liu

et al. 2018

Insect Molecular Biology

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Previous studies have indicated that trypsin inhibitor-like cysteine-rich domain (TIL)-type protease inhibitors, BmSPI38 and BmSPI39, suppress conidial germination and integument penetration of entomopathogenic fungi by inhibiting their cuticle-degrading proteases and might functions as fungal-resistance factors in the silkworm. To date, the physiological forms and functional significance of multimerization of BmSPI38 and BmSPI39 remain unknown. In this study, we investigated the physiological forms of BmSPI38 and BmSPI39 in Bombyx mori silkworms using multiple complementary methods, including activity staining, reducing and nonreducing sodium dodecyl sulfate polyacrylamide gel electrophoresis, matrix-assisted laser desorption ionization time-of-flight mass spectrometry, western blotting and immunofluorescence. We found that recombinant BmSPI38 and BmSPI39 tend to form homologous multimers, and their dimers, trimers and tetramers possessed intense inhibitory activity against subtilisin A from Bacillus licheniformis. In contrast, their monomers showed no detectable inhibitory activity. Both BmSPI38 and BmSPI39 also exist mainly as stable tetramers in silkworm tissues, and they also predominantly function as a tetramer in these tissues. This study is the first to demonstrate this preferred quaternary form of a TIL-type protease inhibitor and will likely help to elucidate the mechanisms of BmSPI38 and BmSPI39 in the innate immune response of the silkworm.

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TIL-type protease inhibitors may be used as targeted resistance factors to enhance silkworm defenses against invasive fungi

Cited by 46 publications

References 43 publications

RNA-Seq Analyses for Two Silkworm Strains Reveals Insight into Their Susceptibility and Resistance to Beauveria bassiana Infection

RNA-Seq Analyses for Two Silkworm Strains Reveals Insight into Their Susceptibility and Resistance to Beauveria bassiana Infection

Protease inhibitors in Bombyx mori silk might participate in protecting the pupating larva from microbial infection

The fungal‐resistance factors BmSPI38 and BmSPI39 predominantly exist as tetramers, not monomers, in Bombyx mori

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