• 한국잠사학회:학술대회논문집
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• 한국잠사학회 2005년도 제48회 추계 학술연구 발표회
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• pp.61-61
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• 2005

• 한국응용곤충학회지
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• 제36권3호
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• pp.264-269
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• 1997

뽕나무하늘소(Apriona germari) 및 왕똥풍뎅이 (Aphodius apicalis) 사충으로부터 4종의 Bacillus thuringiensis를 분리하였다. B. thuringiensis의 편모 항원에 의한 동정 결과, 4종의 분리된 B. thuringiensis 중에서 1종은 darmstadiensis 아종으로 판명되었으나, 나머지 3종은 33종의 어느 B. thuringiensis 편모 항체와도 반응하지 않았다. 분리된 균주의 포자와 내독소 단백질 혼합물을 이용하여 뽕나무하늘소와 왕똥풍뎅이, 누에(Bombyx mori) 및 빨간집모가(Cules pipiens pallens) 유충에 대하여 생물검정한 결과, 이들 분리주들은 검정된 곤충에 대하여 독성을 갖지 않는 것으로 나타났다. 아울러 SDS-PAGE와 agarose gel electrophoresis를 이용하여 분리된 4종의 B. thuringiensis의 내독소 단백질과 plasmid DNA 패턴을 조사한 결과, darmstadiensis와 이미 보고된 20종의 무독성 B. thuringiensis와 차이를 보여 새로운 무독성 균주로 사료된다.

• 생명과학회지
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• 제25권6호
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• pp.715-723
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• 2015

지구상에 존재하는 전체 동물 중 가장 큰 부분을 차지 하고 있는 곤충은 예로부터 인간의 식품, 농업, 산업, 의약 등의 일상 생활에 이용되어 왔다. 많은 수와 높은 영양학적 가치로 곤충의 생리활성물질이 미개발 생물자원으로 재평가 되고 있다. 곤충은 면역세포, 곤충 혈구세포, 효소들의 연쇄반응 혹은 항균 단백질/펩타이드 같은 방법으로 외부의 감염에 저항성을 가지게 된다. 항균 펩타이드는 곤충의 혈림프의 선천성 면역 시스템 중 주요한 성분중의 하나로 항생제 내성 균주의 출몰이 빈번하게 일어나 해결책으로 새로운 항생제 개발이 시급한 시점에서 유력한 후보물질로 주목 받고 있다. 곤충 유래 항균 펩타이드는 150개가 넘게 분리되었으며 크게 세크로핀, 디펜신, 글라이신/프롤린이 풍부한 펩타이드로 이루어진다. 이 논문에서, 향균 펩타이드를 생산하는 여러 곤충 중에서 벌, 소똥구리, 울도하늘소, 나비 그리고 울도하늘소에서 얻을 수 있는 펩타이드의 종류 그리고 작용 기작에 대해 알아보았다. 이 펩타이드들은 항균효과를 가지고 있으며 멜리틴을 제외하고 적혈구의 용혈 현상이 나타나지 않고 주로 세포막을 붕괴시키거나 세포자살기작을 유도하여 병원성 미생물의 성장을 억제한다. 곤충 유래 펩타이드와 같은 생리활성물질이 그 활용 가능성의 면에서 엄청난 가능성을 가지고 있어 이에 대한 연구는 앞으로 더 주목을 받을 것이다.

• 한국응용곤충학회지
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• 제46권3호
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• pp.357-362
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• 2007

토양의 비옥도를 높여주는 분식성 곤충으로써 우리나라에 서식하고 있는 애기뿔소똥구리(Copris tripartitus)의 발육생태를 각 온도에서 관찰하였다. 대량증식 및 환경변화 모델 적용을 위해 15, 17.5, 20, 25, 27.5 및 $30^{\circ}C$(16L:8D)에서 발육실험을 한 결과 알에서 우화까지의 발육기간은 $17.5^{\circ}C$에서 118.0일이고, $27.5^{\circ}C$에서는 49.3일이었다. 온도가 높을수록 짧은 발육기간을 보였으며, 알, 유충, 용, 알에서 우화까지의 발육영점온도와 유효적산온도는 각각 12.1, 11.2, 12.1, $9.2^{\circ}C$, 그리고 82.7, 462.0, 225.7, 947.2일도이었다. 난 및 유충의 발육단계에서 사망률은 $25^{\circ}C$에서 가장 낮게 나타나 애기뿔소똥구리의 성장에 적합한 온도는 $25^{\circ}C$이었다.

• BMB Reports
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• 제48권6호
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• pp.324-329
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• 2015

CopA3 is a homodimeric ${\alpha}$-helical peptide derived from coprisin which is a defensin-like antimicrobial peptide that was identified from the dung beetle, Copris tripartitus. CopA3 has been reported to have anticancer activity against leukemia cancer cells. In the present study, we investigated the anticancer activity of CopA3 in human gastric cancer cells. CopA3 reduced cell viability and it was cytotoxic to gastric cancer cells in the MTS and LDH release assay, respectively. CopA3 was shown to induce necrotic cell death of the gastric cancer cells by flow cytometric analysis and acridine orange/ethidium bromide staining. CopA3-induced cell death was mediated by specific interactions with phosphatidylserine, a membrane component of cancer cells. Taken together, these data indicated that CopA3 mainly caused necrosis of gastric cancer cells, probably through interactions with phosphatidylserine, which suggests the potential utility of CopA3 as a cancer therapeutic. [BMB Reports 2015; 48(6): 324-329]

• BMB Reports
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• 제47권11호
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• pp.625-630
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• 2014

Defensins, which are small cationic molecules produced by organisms as part of their innate immune response, share a common structural scaffold that is stabilized by three disulfide bridges. Coprisin is a 43-amino acid defensin-like peptide from Copris tripartitus. Here, we report the intramolecular disulfide connectivity of cysteine-rich coprisin, and show that it is the same as in other insect defensins. The disulfide bond pairings of coprisin were determined by combining the enzymatic cleavage and mass analysis. We found that the loss of any single disulfide bond in coprisin eliminated all antibacterial, but not antifungal, activity. Circular dichroism (CD) analysis showed that two disulfide bonds, Cys20-Cys39 and Cys24-Cys41, stabilize coprisin's ${\alpha}$-helical region. Moreover, a BLAST search against UniProtKB database revealed that coprisin's ${\alpha}$-helical region is highly homologous to those of other insect defensins.

• Journal of Microbiology and Biotechnology
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• 제22권1호
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• pp.156-158
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• 2012

A synthetic coprisin analog peptide, 9-mer dimer CopA3 (CopA3) was designed based on a defensin-like peptide, Coprisin, isolated from the bacteria-immunized dung beetle Copris tripartitus. Here, CopA3 was investigated for its antimicrobial activity and cancer cell growth inhibition. CopA3 showed antimicrobial activities against various pathogenic bacteria and yeast fungus with MIC values in 2~32 ${\mu}M$ ranges, and inhibited the cell viabilities of pancreatic and hepatocellular cancer cells, except MIA-Paca2, Hep3B, and HepG2 cells, in a dose-dependent manner. The average $IC_{50}$ values of CopA3 against pancreatic and hepatocellular cancer cells were 61.7 ${\mu}M$ and 67.8 ${\mu}M$, respectively. The results indicate that CopA3 has potential in the treatments of pancreatic and hepatocellular cancers as well as microorganism infection disease.

• Journal of Microbiology and Biotechnology
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• 제27권2호
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• pp.350-356
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• 2017

We previously reported that the CopA3 peptide (LLCIALRKK, ${\small{D}}-form$) originally isolated from the Korean dung beetle has antimicrobial and immunosuppressive effects. However, the high cost of producing the synthetic peptide, especially the ${\small{D}}-form$, has limited the development of CopA3 for therapeutic purposes. Here, we investigated whether the CopA3 deletion derivative, CopA5, which is composed of only five amino acids (LLCIA) and has the ${\small{L}}-form$ structure, could inhibit the lipopolysaccharide (LPS)-induced activation of macrophages. Peritoneal exudate macrophages (PEM) were isolated from mice and exposed to LPS in the presence or absence of CopA5, and biomarkers of macrophage activation were measured. Our results revealed that LPS-induced nitric oxide (NO) production, tumor necrosis factor $(TNF)-{\alpha}$ secretion, and phagocytic activity of PEM were significantly inhibited by CopA5 treatment. Similar to CopA3, the structurally modified CopA5 peptide had no cell toxicity (as assessed by measurement of cell viability loss and apoptosis) in PEM. Moreover, the LPS-induced upregulation of the activating phosphorylation of signal transducer and activator of transcription 1 (STAT1) was markedly inhibited by CopA5 treatment. These results suggest that, similar to CopA3, CopA5 inhibits macrophage activation by inhibiting STAT1 phosphorylation and blocking the release of NO and $TNF-{\alpha}$. CopA5 may therefore prove therapeutically useful in the realm of immune suppression.

• Journal of Microbiology and Biotechnology
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• 제29권1호
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• pp.30-36
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• 2019

Numerous studies have reported that enteric neurons involved in controlling neurotransmitter secretion and motility in the gut critically contribute to the progression of gut inflammation. Clostridium difficile toxins, which cause severe colonic inflammation, are also known to affect enteric neurons. Our previous study showed that C. difficile toxin A directly induces neural cell toxicities, such as viability loss and apoptosis. In the current study, we attempted to identify a potent inhibitor of toxin A-induced neural cell toxicity that may aid in managing toxin A-induced gut inflammation. In our recent study, we found that the Korea dung beetle-derived antimicrobial peptide CopA3 completely blocked neural cell apoptosis caused by okadaic acid or 6-OHDA. Here, we examined whether the antimicrobial peptide CopA3 inhibited toxin A-induced neural cell damage. In neuroblastoma SH-SY5Y cells, CopA3 treatment protected against both apoptosis and viability loss caused by toxin A. CopA3 also completely inhibited activation of the pro-apoptotic factor, caspase-3. Additionally, CopA3 rescued toxin A-induced downregulation of neural cell proliferation. However, CopA3 had no effect on signaling through ROS/p38 $MAPK/p27^{kip1}$, suggesting that CopA3 inhibits toxin A-induced neural cell toxicity independent of this well-characterized toxin A pathway. Our data further suggest that ability of CopA3 to rescue toxin A-induced neural cell damage may also ameliorate the gut inflammation caused by toxin A.

• Journal of Animal Science and Technology
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• 제64권6호
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• pp.1132-1143
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• 2022

Insects are a valuable natural source that can produce a variety of bioactive compounds due to their increasing species diversity. CopA3 is an antimicrobial peptide derived from Copris tripartitus (i.e., the dung beetle). It is known to increase the proliferation of colonic epithelial and neuronal stem cells by regulating cell cycle. This research hypothesized that CopA3 can promote the proliferation of porcine muscle satellite cells (MSCs). The effects of CopA3 on porcine MSCs, which are important for muscle growth and regeneration, remain unclear. Here, we investigated the effects of CopA3 on porcine MSCs. According to viability results, we designed four groups: control (without CopA3) and three treatment groups (treated with 5,10, and 25 ㎍/mL of CopA3). At a CopA3 concentration of 5 ㎍/mL and 10 ㎍/mL, the proliferation of MSCs increased more than that observed in the control group. Furthermore, compared to that in the control, CopA3 treatment increased the S phase but decreased the G0/G1 phase ratio. Additionally, early and late apoptotic cells were found to be decreased in the 5 ㎍/mL group. The expressions of the myogenesis-related transcription factor PAX7 and MYOD proteins were significantly upregulated in the 5 ㎍/mL and 10 ㎍/mL groups, whereas the MYOG protein remained undetected in all group. This study suggested that CopA3 promotes muscle cell proliferation by regulating the cell cycle of MSCs and can regulate the activity of MSCs by increasing the expressions of PAX7 and MYOD.