Expression and characterization of cecropinXJ, a bioactive antimicrobial peptide from Bombyx mori (Bombycidae, Lepidoptera) in Escherichia coli

Li, Xia; Zhang, Fuchun; Liu, Zhongyuan; Ma, Junsheng; Yang, Jianhua

doi:10.3892/etm.2013.1056

Cited by 31 publications

(40 citation statements)

References 43 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Some small α-helical peptides from insect hemolymph have antibacterial and antifungal activity. These include some cecropins (Boulanger et al, 2002; Cavallarin et al, 1998; Delucca et al, 1997; Ekengren and Hultmark, 1999; Kim et al, 2010; Vizioli et al, 2000; Xia et al, 2013) and moricins (Brown et al, 2008; Dia et al, 2008; Hemmi et al, 2002). Proline-rich peptides with antifungal activity include lebocins (Chowdhury et al, 1995; Rao et al, 2012) and metchnikowin (Levashina et al, 1995; Rahnamaeian et al, 2009; Rahnamaeian and Vilcinskas, 2012).…”

Section: Introductionmentioning

confidence: 99%

Characterization and regulation of expression of an antifungal peptide from hemolymph of an insect, Manduca sexta

Souhail

Hiromasa

Rahnamaeian

et al. 2016

Developmental & Comparative Immunology

View full text Add to dashboard Cite

Insects secrete antimicrobial peptides as part of the innate immune response. Most antimicrobial peptides from insects have antibacterial but not antifungal activity. We have characterized an antifungal peptide, diapausin-1 from hemolymph of a lepidopteran insect, Manduca sexta (tobacco hornworm). Diapausin-1 was isolated by size exclusion chromatography from hemolymph plasma of larvae that were previously injected with a yeast, Saccharomyces cerevisiae. Fractions containing activity against S. cerevisiae were analyzed by SDS-PAGE and MALDI-TOF MS/MS and found to contain a 45-residue peptide that was encoded by sequences identified in M. sexta transcriptome and genome databases. A cDNA for diapausin-1 was cloned from cDNA prepared from fat body RNA. Diapausin-1 is a member of the diapausin family of peptides, which includes members known to have antifungal activity. The M. sexta genome contains 14 genes with high similarity to diapausin-1, each with 6 conserved Cys residues. Diapausin-1 was produced as a recombinant protein in Escherichia coli. Purified recombinant diapausin-1 was active against S. cerevisiae, with IC50 of 12 μM, but had no detectable activity against bacteria. Spores of some plant fungal pathogens treated with diapausin-1 had curled germination tubes or reduced and branched hyphal growth. Diapausin-1 mRNA level in fat body strongly increased after larvae were injected with yeast or with Micrococcus luteus. In addition, diapausin-1 mRNA levels increased in midgut and fat body at the wandering larval stage prior to pupation, suggesting developmental regulation of the gene. Our results indicate that synthesis of diapausin-1 is part of an antifungal innate immune response to infection in M. sexta.

show abstract

Section: Introductionmentioning

confidence: 99%

Characterization and regulation of expression of an antifungal peptide from hemolymph of an insect, Manduca sexta

Souhail

Hiromasa

Rahnamaeian

et al. 2016

Developmental & Comparative Immunology

View full text Add to dashboard Cite

show abstract

“…It is positively charged and can form specific amphipathic a-helices to interact with the non-polar lipid cell membranes [12,22]. CecropinXJ could kill cancer cells but have no hemolytic activity against human erythrocytes and no toxicity to some normal cells [23]. In this study, we investigated the effects of cecropinXJ on cytoskeleton in human esophageal carcinoma Eca109 cells.…”

Section: Introductionmentioning

confidence: 99%

CecropinXJ, a silkworm antimicrobial peptide, induces cytoskeleton disruption in esophageal carcinoma cells

Li¹,

Wu²,

Kang³

et al. 2014

ABBS

Self Cite

View full text Add to dashboard Cite

Antimicrobial peptides exist in the non-specific immune system of organism and participate in the innate host defense of each species. CecropinXJ, a cationic antimicrobial peptide, possesses potent anticancer activity and acts preferentially on cancer cells instead of normal cells, but the mechanism of cancer cell death induced by cecropinXJ remains largely unknown. This study was performed to investigate the cytoskeleton-disrupting effects of cecropinXJ on human esophageal carcinoma cell line Eca109 using scanning electron microscopy observation, fluorescence imaging, cell migration and invasion assays, western blotting, and quantitative reverse transcription polymerase chain reaction (qRT-PCR) analysis. The electronic microscope and fluorescence imaging observation suggested that cecropinXJ could result in morphological changes and induce damage to microtubules and actin of Eca109 cells in a dose-dependent manner. The cell migration and invasion assays demonstrated that cecropinXJ could inhibit migration and invasion of tumor cells. Western blot and qRT-PCR analysis showed that there was obvious correlation between microtubule depolymerization and actin polymerization induced by cecropinXJ. Moreover, cecropinXJ might also cause decreased expression of a-actin, b-actin, g-actin, a-tubulin, and b-tubulin genes in concentration-and time-dependent manners. In summary, this study indicates that cecropinXJ triggers cytotoxicity in Eca109 cells through inducing the cytoskeleton destruction and regulating the expression of cytoskeleton proteins. This cecropinXJ-mediated cytoskeleton-destruction effect is instrumental in our understanding of the detailed action of antimicrobial peptides in human cancer cells and cecropinXJ might be a potential therapeutic agent for the treatment of cancer in the future.

show abstract

“…Our previous studies have shown that cecropinXJ can inhibit the proliferation of human gastric cancer in vitro such as AGS cells (21), but have no hemolytic activity against human erythrocytes and no toxicity to normal mammalian cells (22,23). Due to difficulty of AGS cells to form a solid tumor in vivo, we investigated the cytotoxicity and the mechanism of cecropinXJ against the human gastric cancer BGC823 cells in the present study.…”

Section: Introductionmentioning

confidence: 99%

CecropinXJ inhibits the proliferation of human gastric cancer BGC823 cells and induces cell death in vitro and in vivo

et al. 2015

International Journal of Oncology

View full text Add to dashboard Cite

Abstract. We have shown that an antimicrobial peptide (AMP) cecropinXJ isolated from the larvae of Bombyx mori selectively inhibits the proliferation of cancer cells. However, the mechanism remains to be determined. In the present study, we examined the antitumor activity of cecropinXJ against human gastric cancer BGC823 cells and explored the mechanism. The results showed that cecropinXJ inhibited the growth of gastric cancer BGC823 cells in vitro and in vivo. MTT and colony formation assays indicated that cecropinXJ suppressed cell proliferation and reduced colony formation of BGC823 cells in a dose-and time-dependent manner, but without inhibitory effect on normal gastric epithelia GES-1 cells. S-phase arrest in BGC823 cells was observed after treatment with cecropinXJ. Annexin V/PI staining suggested that cecropinXJ induced both early and late phases of apoptosis through activation of mitochondrial-mediated caspase pathway, upregulation of Bax expression and downregulation of Bcl-2 expression. Additionally, cecropinXJ treatment increased reactive oxygen species (ROS) production, disrupted the mitochondrial membrane potential (Δψ m ) and led to release of cytochrome c. Importantly, in vivo study showed that cecropinXJ significantly prevented the growth of xenograft tumor in the BGC823-bearing mice, possibly mediated by the induction of apoptosis and inhibition of angiogenesis. These results suggest that cecropinXJ may be a promising therapeutic candidate for the treatment of gastric cancer. IntroductionGastric cancer is one of the most common malignant tumors, >70% of new cases and deaths occur in developing countries each year (1). In China, the incidence and mortality rate of gastric cancer are increasing. Although there are distinct discrepancies in diagnosis, prognosis, and treatment efficacy for gastric cancer patients, the 5-year survival rate of gastric cancer is generally <20% (2). At present, the management of gastric cancer includes surgery, radiotherapy, conventional chemotherapy, molecular targeted therapy and biological therapy, but these methods have not reached expected clinical efficacy, which mainly focus on mass cell killing without high specificity and often causes severe side-effects and toxicities. Moreover, recurrences and metastasis frequently occur in the majority of patients (2). Hence, it is urgent to explore safe and effective therapeutic agents for gastric cancer to improve the survival rate and quality of life.Antimicrobial peptides (AMPs) are evolutionarilyconserved components of the innate immune system (3), which exert their activities against a broad range of microbial pathogens. Compared to conventional treatments, AMPs have many advantages, such as specific cytotoxicity for cancer cells, ability to bypass the multidrug-resistance mechanism, and additive effects in combination therapy (4), suggesting that AMPs has potential as a novel antitumor agent for the treatment of cancer.AMPs can directly kill cancer cells by a cell membranelytic effect (5), or trigger apoptosis in can...

show abstract

Expression and characterization of cecropinXJ, a bioactive antimicrobial peptide from Bombyx mori (Bombycidae, Lepidoptera) in Escherichia coli

Cited by 31 publications

References 43 publications

Characterization and regulation of expression of an antifungal peptide from hemolymph of an insect, Manduca sexta

Characterization and regulation of expression of an antifungal peptide from hemolymph of an insect, Manduca sexta

CecropinXJ, a silkworm antimicrobial peptide, induces cytoskeleton disruption in esophageal carcinoma cells

CecropinXJ inhibits the proliferation of human gastric cancer BGC823 cells and induces cell death in vitro and in vivo

Contact Info

Product

Resources

About