Insect Inducible Antimicrobial Peptides and Their Applications

Ezzati-Tabrizi, Reyhaneh; Farrokhi, Naser; Talaei-Hassanloui, Reza; Alavi, Seyed Mehdi; Hosseininaveh, Vahıd

doi:10.2174/1389203711209070620

Cited by 20 publications

(10 citation statements)

References 147 publications

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“…Another reason is that its hemolymph is a rich source of defense molecules that can be purified and sequenced. They are considered an alternative to antibiotics due to the fact that they do not induce resistance (Vilcinskas, ; Yeung, ; Ezzati‐Tabrizi et al ., ; Li et al ., ; Yi et al ., ). Finally, we can follow the interaction of G. mellonella with natural insect pathogens and consider this in the light of a host–pathogen evolutionary arms race.…”

Section: Discussionmentioning

confidence: 99%

Immunity of the greater wax mothGalleria mellonella

2016

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Investigation of insect immune mechanisms provides important information concerning innate immunity, which in many aspects is conserved in animals. This is one of the reasons why insects serve as model organisms to study virulence mechanisms of human pathogens. From the evolutionary point of view, we also learn a lot about host-pathogen interaction and adaptation of organisms to conditions of life. Additionally, insect-derived antibacterial and antifungal peptides and proteins are considered for their potential to be applied as alternatives to antibiotics. While Drosophila melanogaster is used to study the genetic aspect of insect immunity, Galleria mellonella serves as a good model for biochemical research. Given the size of the insect, it is possible to obtain easily hemolymph and other tissues as a source of many immune-relevant polypeptides. This review article summarizes our knowledge concerning G. mellonella immunity. The best-characterized immune-related proteins and peptides are recalled and their short characteristic is given. Some other proteins identified at the mRNA level are also mentioned. The infectious routes used by Galleria natural pathogens such as Bacillus thuringiensis and Beauveria bassiana are also described in the context of host-pathogen interaction. Finally, the plasticity of G. mellonella immune response influenced by abiotic and biotic factors is described.

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Section: Discussionmentioning

confidence: 99%

Immunity of the greater wax mothGalleria mellonella

2016

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“…The insect represents an undercultivated natural resource that exists abundantly in both number and variety, and there is a possibility to identify new insect-derived substances useful for either probing the PrP conversion mechanism or developing therapeutic or prophylactic drugs for prion diseases. In fact, anticancer, antiviral, or antimicrobial compounds are present in extracts from insects (18)(19)(20)(21). In this study, we report antiprion substances derived from insects that have not been previously reported.…”

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confidence: 61%

Melanin or a Melanin-Like Substance Interacts with the N-Terminal Portion of Prion Protein and Inhibits Abnormal Prion Protein Formation in Prion-Infected Cells

Hamanaka

Nishizawa

Sakasegawa

et al. 2017

J Virol

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Prion diseases are progressive fatal neurodegenerative illnesses caused by the accumulation of transmissible abnormal prion protein (PrP). To find treatments for prion diseases, we searched for substances from natural resources that inhibit abnormal PrP formation in prion-infected cells. We found that high-molecular-weight components from insect cuticle extracts reduced abnormal PrP levels. The chemical nature of these components was consistent with that of melanin. In fact, synthetic melanin produced from tyrosine or 3-hydroxy-l-tyrosine inhibited abnormal PrP formation. Melanin did not modify cellular or cell surface PrP levels, nor did it modify lipid raft or cellular cholesterol levels. Neither did it enhance autophagy or lysosomal function. Melanin was capable of interacting with PrP at two N-terminal domains. Specifically, it strongly interacted with the PrP region of amino acids 23 to 50 including a positively charged amino acid cluster and weakly interacted with the PrP octarepeat peptide region of residues 51 to 90. However, the and data were inconsistent with those of prion-infected cells. Abnormal PrP formation in protein misfolding cyclic amplification was not inhibited by melanin. Survival after prion infection was not significantly altered in albino mice or exogenously melanin-injected mice compared with that of control mice. These data suggest that melanin, a main determinant of skin color, is not likely to modify prion disease pathogenesis, even though racial differences in the incidence of human prion diseases have been reported. Thus, the findings identify an interaction between melanin and the N terminus of PrP, but the pathophysiological roles of the PrP-melanin interaction remain unclear. The N-terminal region of PrP is reportedly important for neuroprotection, neurotoxicity, and abnormal PrP formation, as this region is bound by many factors, such as metal ions, lipids, nucleic acids, antiprion compounds, and several proteins, including abnormal PrP in prion disease and the Aβ oligomer in Alzheimer's disease. In the present study, melanin, a main determinant of skin color, was newly found to interact with this N-terminal region and inhibits abnormal PrP formation in prion-infected cells. However, the data for prion infection in mice lacking melanin production suggest that melanin is not associated with the prion disease mechanism, although the incidence of prion disease is reportedly much higher in white people than in black people. Thus, the roles of the PrP-melanin interaction remain to be further elucidated, but melanin might be a useful competitive tool for evaluating the functions of other ligands at the N-terminal region.

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“…In insects, many signaling pathways have been reported to be involved in immune defense against pathogens, such as the melanization [ 28 ], Toll [ 29 ], immune deficiency (Imd) [ 30 ], and Jun-kinase (JNK) [ 31 ] pathways. Quinones [ 32 ], antimicrobial peptides [ 33 ] and lysozyme [ 34 ] are the final products of these pathways that directly kill pathogens or inhibit their growth. Many immune related components have been reported in the cocoon.…”

Section: Discussionmentioning

confidence: 99%

Proteins in the Cocoon of Silkworm Inhibit the Growth of Beauveria bassiana

et al. 2016

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Silk cocoons are composed of fiber proteins (fibroins) and adhesive glue proteins (sericins), which provide a physical barrier to protect the inside pupa. Moreover, other proteins were identified in the cocoon silk, many of which are immune related proteins. In this study, we extracted proteins from the silkworm cocoon by Tris-HCl buffer (pH7.5), and found that they had a strong inhibitory activity against fungal proteases and they had higher abundance in the outer cocoon layers than in the inner cocoon layers. Moreover, we found that extracted cocoon proteins can inhibit the germination of Beauveria bassiana spores. Consistent with the distribution of protease inhibitors, we found that proteins from the outer cocoon layers showed better inhibitory effects against B. bassiana spores than proteins from the inner layers. Liquid chromatography-tandem mass spectrometry was used to reveal the extracted components in the scaffold silk, the outermost cocoon layer. A total of 129 proteins were identified, 30 of which were annotated as protease inhibitors. Protease inhibitors accounted for 89.1% in abundance among extracted proteins. These protease inhibitors have many intramolecular disulfide bonds to maintain their stable structure, and remained active after being boiled. This study added a new understanding to the antimicrobial function of the cocoon.

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Insect Inducible Antimicrobial Peptides and Their Applications

Cited by 20 publications

References 147 publications

Immunity of the greater wax mothGalleria mellonella

Immunity of the greater wax mothGalleria mellonella

Melanin or a Melanin-Like Substance Interacts with the N-Terminal Portion of Prion Protein and Inhibits Abnormal Prion Protein Formation in Prion-Infected Cells

Proteins in the Cocoon of Silkworm Inhibit the Growth of Beauveria bassiana

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