Galleria defensin
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Galleria defensin

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Galleria defensin has antibacterial activity against the Gram-positive bacterium S.lutea (MIC=1.9 µM). Galleria defensin has antifungal activity against A.niger (MIC=2.9 µM), C.albicans (MIC=2.9 µM), C.fructus (MIC=2.9 µM), C.wickerhamii (MIC=2.9 µM), P.pastoris (MIC=2.9 µM), P.stiptis (MIC=2.9 µM), P.tannophilus (MIC=2.9 µM), T.harzianum (MIC=2.9 µM), and Z.marxianus (MIC=2.9 µM), but lacks antifungal activity against C.albidus, F.oxysporum, and S.cerevisiae.

Category
Functional Peptides
Catalog number
BAT-012148
Sequence
DTLIGSCVWGATNYTSDCNAECKRRGYKGGHCGSFLNVNCWCE
1. Anti-Legionella dumoffii activity of Galleria mellonella defensin and apolipophorin III
Marta Palusińska-Szysz, Agnieszka Zdybicka-Barabas, Bożena Pawlikowska-Pawlęga, Pawel Mak, Małgorzata Cytryńska Int J Mol Sci. 2012 Dec 12;13(12):17048-64. doi: 10.3390/ijms131217048.
The gram-negative bacterium Legionella dumoffii is, beside Legionella pneumophila, an etiological agent of Legionnaires' disease, an atypical form of pneumonia. The aim of this study was to determine the antimicrobial activity of Galleria mellonella defense polypeptides against L. dumoffii. The extract of immune hemolymph, containing a mixture of defense peptides and proteins, exhibited a dose-dependent bactericidal effect on L. dumoffii. The bacterium appeared sensitive to a main component of the hemolymph extract, apolipophorin III, as well as to a defense peptide, Galleria defensin, used at the concentrations 0.4 mg/mL and 40 μg/mL, respectively. L. dumoffii cells cultured in the presence of choline were more susceptible to both defense factors analyzed. A transmission electron microscopy study of bacterial cells demonstrated that Galleria defensin and apolipophorin III induced irreversible cell wall damage and strong intracellular alterations, i.e., increased vacuolization, cytoplasm condensation and the appearance of electron-white spaces in electron micrographs. Our findings suggest that insects, such as G. mellonella, with their great diversity of antimicrobial factors, can serve as a rich source of compounds for the testing of Legionella susceptibility to defense-related peptides and proteins.
2. Galleria mellonella: A Novel Invertebrate Model to Distinguish Intestinal Symbionts From Pathobionts
Anna Lange, Andrea Schäfer, Annika Bender, Alexander Steimle, Sina Beier, Raphael Parusel, Julia-Stefanie Frick Front Immunol. 2018 Sep 19;9:2114. doi: 10.3389/fimmu.2018.02114. eCollection 2018.
Insects and mammals share evolutionary conserved innate immune responses to maintain intestinal homeostasis. We investigated whether the larvae of the greater wax moth Galleria mellonella may be used as an experimental organism to distinguish between symbiotic Bacteroides vulgatus and pathobiotic Escherichia coli, which are mammalian intestinal commensals. Oral application of the symbiont or pathobiont to G. mellonella resulted in clearly distinguishable innate immune responses that could be verified by analyzing similar innate immune components in mice in vivo and in vitro. The differential innate immune responses were initiated by the recognition of bacterial components via pattern recognition receptors. The pathobiont detection resulted in increased expression of reactive oxygen and nitrogen species related genes as well as antimicrobial peptide gene expression. In contrast, the treatment/application with symbiotic bacteria led to weakened immune responses in both mammalian and insect models. As symbionts and pathobionts play a crucial role in development of inflammatory bowel diseases, we hence suggest G. mellonella as a future replacement organism in inflammatory bowel disease research.
3. Purification, cDNA cloning and expression of an insect defensin from the great wax moth, Galleria mellonella
Y S Lee, E K Yun, W S Jang, I Kim, J H Lee, S Y Park, K S Ryu, S J Seo, C H Kim, I H Lee Insect Mol Biol. 2004 Feb;13(1):65-72. doi: 10.1111/j.1365-2583.2004.00462.x.
An insect defensin, named Galleria defensin, was purified from the larval haemolymph of Galleria mellonella immunized against E. coli. The peptide was composed of forty-three amino acid residues containing six cysteines that might be engaged in intramolecular disulphide bridges. The primary structure of Galleria defensin shared about 90.7% identity to that of heliomicin, which was an insect defensin isolated from Heliothis virescens. The full-length cDNA encoding Galleria defensin was cloned from the fat body of the immunized G. mellonella larvae. Northern blot analysis revealed that Galleria defensin was expressed not only in the fat body but also in the midgut against invading bacteria into haemocoel. This is the first report presenting cDNA and expression of an insect defensin in the lepidopteran species.
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