• Proceedings of the Korean Society of Sericultural Science Conference
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• 2002.10a
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• pp.76-76
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• 2002

No Abstract, See Full Text

• Proceedings of the Korean Society of Applied Entomolohy Conference
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• 2001.11a
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• pp.143-143
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• 2001

• International Journal of Industrial Entomology and Biomaterials
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• v.45 no.2
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• pp.43-48
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• 2022

Bombyx mori is a representative industrial insect and is used in silk production. Additionally, it serves as an insect model in molecular studies. To date, various molecular studies on its physiological characteristics, including the innate immune response and cuticular melanization, have been conducted. The melanization, including cuticular melanization, in insects is controlled by the prophenoloxidase-activating system, which is also involved in their innate immune response. In this review, to better understand the molecular mechanisms underlying the prophenoloxidase-activating system in the silkworm, the roles of five biomolecules, namely tyrosine hydroxylase, prophenoloxidase-activating enzyme, phenoloxidase, serine protease homolog, and immulectin, are discussed.

• International Journal of Industrial Entomology and Biomaterials
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• v.8 no.1
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• pp.95-99
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• 2004

Synthetic oligodeoxynucleotides (ODNs) containing unmethylated CpG dinucleotides in particular base contexts are known to induce immunity in vertebrate cells. In insect, however, it was recent to find out that ODNs induces insect immunity as other immune inducer such as lipopolysaccharide. However, the finding was solely based on one lepidopteran insect, Bombyx mori, and the expression of insect immunity was neither dependent on numbers of CpG repeats nor methylation of CpG repeats within ODNs. Instead, foreignness of DNA has been suggested to be a key factor governing induction of antibacterial peptide. In this study, we expanded our previous understanding to the potentiality of ODNs as an immune inducer for antifungal peptide in Galleria mellonella and B. mori. To do this, a defensin-type antifungal peptide gene, reported from G. mellonella was cloned and partially sequenced from G. mellonella and B. mori successfully and utilized as a probe in the Northern blot analysis. We found out that ODNs also work as an immune inducer for antifungal peptide in the fat body and midgut of G. mellonella and B. mori larvae. Also, induction pattern of antifungal peptide was irrelevant to the numbers of CpG repeats within ODNs as previously reported on the induction pattern of antibacterial peptides.

• International Journal of Industrial Entomology and Biomaterials
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• v.21 no.1
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• pp.127-132
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• 2010

We have characterized full-length cDNA encoding Gall-6-tox protein, which was cloned from the fat body of the immunized Galleria mellonella larvae. The cloned cDNA of Gall-6-tox consists of 1301 nucleotides and contained an open reading frame of 891 nucleotides corresponding to a protein of 296 residues that includes a putative 16-residue signal sequence and a 280-residue mature peptide with a calculated mass of 30,707.73 Da. The deduced mature peptide contains conserved tandem repeats of six cysteine-stabilized alpha beta ($Cs{\alpha}{\beta}$) motifs, which was detected in scorpion toxins and insect defensins. In the sequence homology search, mature Gall-6-tox showed 34% and 28% amino acid sequence homology with Bomb-6-tox from Bombyx mori and Spod-11-tox from Spodoptera frugiperda, respectively. Gall-6-tox orthologs were only found in Lepidopteran species, indicating that this new immune-related gene family is specific to this insect order. RT-PCR analysis revealed that Gall-6-tox was expressed primarily in the larval fat bodies, hemocytes, and midgut against invading bacteria into hemocoel. Moreover, the expression time course of Gall-6-tox was examined up to 24 h in the fat bodies and midgut after injection of E. coli. Altogether, these results suggest that Gall-6-tox is derived from defensins and Gall-6-tox may play a critical role in Lepidoptera immune system.

• International Journal of Industrial Entomology and Biomaterials
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• v.45 no.2
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• pp.108-114
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• 2022

Protaetia brevitarsis seulensis larva is well-known as an edible insect. The present study aimed to explore the immune-enhancing effect of 30% ethanol extract of Protaetia brevitarsis seulensis larvae (PBE) in RAW264.7 macrophage cells. PBE were not cytotoxic to RAW264.7 cells and nitric oxide production increased on PBE treatment in a dose-dependent manner. Furthermore, PBE significantly promoted the expression of immune-related mediators (Inos and COX-2) and cytokines (TNF-α, IL-6, and IL-1β) and the phosphorylation of MAPKs (ERK, p38, and JNK). Taken together, the immune-enhancing effects of 30% ethanol extract of PBE in vitro were identified. These findings can be used as data for the development of edible insect-based functional foods that improve immune function.

• Journal of Life Science
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• v.26 no.6
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• pp.737-748
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• 2016

By this time, insect antimicrobial peptides (AMPs) have been characterized more than 150 peptides since purification of cecropin in the hemolymph of pupae from Hyalophora cecropia in 1980. Therefore, it is considered that insects are good sources of AMP selection. Insect AMPs are small (low molecular weight) and cationic, and amphipathic with variable length, sequence, and structure. They perform a pivotal role on humoral immunity in the insect innate immune system against invading pathogens such as bacteria, fungi, parasites, and viruses. Most of the insect AMPs are induced rapidly in the fat bodies and other specific tissues of insects after septic injury or immune challenge. Then the AMPs subsequently released into the hemolymph to act against microorganisms. These peptides have a broad antimicrobial spectrum against various microbes including anticancer activities. Insect AMPs could be divided into four families based on their structures and sequences. That is the α-helical peptides, cysteine-rich peptides, proline-rich peptides, and glycine-rich peptides/proteins. For instance, cecropins, insect defensins, proline-rich peptides, and attacins are common insect AMPs, but gloverins and moricins have been identified only in lepidopteran species. This review focuses on AMPs from insects and discusses current knowledge and recent progress with potential applications of insect AMPs.

• Animal Bioscience
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• v.35 no.2_spc
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• pp.332-346
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• 2022

Shortage of protein feed resources is the major challenge to the world farm animal industry. Insects are known as an alternative protein source for poultry. A wide range of insects are available for use in poultry diets. Insect larvae thrive in manure, and organic waste, and produce antimicrobial peptides to protect themselves from microbial infections, and additionally these peptides might also be functional in poultry feed. The feed containing antimicrobial peptides can improve the growth performance, nutrient digestibility, intestinal health, and immune function in poultry. Insect meal contains a higher amount of essential amino acids compared to conventional feedstuffs. Black soldier fly, mealworm, housefly, cricket/Grasshopper/Locust (Orthoptera), silkworm, and earthworm are the commonly used insect meals in broiler and laying hen diets. This paper summarizes the nutrient profiles of the insect meals and reviews their efficacy when included in poultry diets. Due to the differences in insect meal products, and breeds of poultry, inconsistent results were noticed among studies. The main challenge for proper utilization, and the promising prospect of insect meal in poultry diet are also addressed in the paper. To fully exploit insect meal as an alternative protein resource, and exert their functional effects, modes of action need to be understood. With the emergence of more accurate and reliable studies, insect meals will undoubtedly play more important role in poultry feed industry.

• Proceedings of the Korean Society of Applied Entomolohy Conference
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• 2001.11a
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• pp.109-109
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• 2001

• Proceedings of the Zoological Society Korea Conference
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• 2001.10a
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• pp.208.2-208
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• 2001

No Abstract, See Full Text