The lipopolysaccharide (LPS) of Photorhabdus luminescens TT01 can elicit dose- and time-dependent immune priming in Galleria mellonella larvae

2015 ◽  
Vol 127 ◽  
pp. 63-72 ◽  
Author(s):  
Gongqing Wu ◽  
Yunhong Yi ◽  
Yingying Lv ◽  
Mei Li ◽  
Jia Wang ◽  
...  
Keyword(s):  
Galleria Mellonella ◽  
Time Dependent ◽  
Photorhabdus Luminescens ◽  
Immune Priming

scholarly journals Proteomic profiling of bacterial and fungal induced immune priming in Galleria mellonella larvae

2021 ◽  
Vol 131 ◽  
pp. 104213
Author(s):  
Gerard Sheehan ◽  
Anatte Margalit ◽  
David Sheehan ◽  
Kevin Kavanagh
Keyword(s):  
Galleria Mellonella ◽  
Proteomic Profiling ◽  
Immune Priming

scholarly journals Description and charactrization of the Amazonian entomopathogenic bacterium Photorhabdus luminescens MN7

2018 ◽  
Author(s):  
Fernando L. Kamitani ◽  
Daniela P. Almenara ◽  
Carolina Rossi ◽  
Maira R. Camargo Neves ◽  
Lissandra M. A. Müller ◽  
...  
Keyword(s):  
Galleria Mellonella ◽  
Entomopathogenic Nematode ◽  
Hydrolytic Enzymes ◽  
Variant Form ◽  
Photorhabdus Luminescens ◽  
Greater Wax Moth ◽  
Toxin Secretion ◽  
Molecular Masses ◽  
I Cells ◽  
Wax Moth

AbstractMany isolates of the genus Photorhabdus have been reported around the world. Here we describe the first Brazilian Photorhabdus isolate, found in association with the entomopathogenic nematode Heterorhabditis baujardi LPP7, from the Amazonian forest in Monte Negro (RO, Brazil). The new isolate can be grouped with the Hb-Hm clade of P. luminescens subsp. luminescens, close to the new subspecies P. luminescens subsp. sonorensis. P. luminescens MN7 has several characteristics expected of variant form I cells, such as the presence of intracellular crystals, secretion of hydrolytic enzymes (lipases and proteases) and bioluminescence. Although H. baujardi LPP7 is not prolific when compared to H. bacteriophora HP88, P. luminescens MN7 is clearly pathogenic and probably secretes the same toxins as P. luminescens subsp. luminescens W14, when fed to larvae of the greater wax moth Galleria mellonella. This behavior is different from what is found in Photorhabdus luminescens subsp. laumondii HP88, which was used as a control in our experiments, and P. l. subsp. laumondii TT01. Besides the toxin secretion, P. luminescens MN7 secretes proteolytic polypeptides that have molecular masses different from those found in P. l. subsp. laumondii TT01. Finally, the crude extract from spent culture medium was shown to contain 3,5-dihydroxy-4-isopropyl-cis-stilbene and 1,3,8-trihydroxy-9,10-anthraquinone as the major compounds, similarly to other Photorhabdus luminescens strains.

Comparison of metabolites produced in vitro and in vivo by Photorhabdus luminescens, a bacterial symbiont of the entomopathogenic nematode Heterorhabditis megidis

1998 ◽  
Vol 44 (11) ◽  
pp. 1072-1077 ◽  
Author(s):  
Kaiji Hu ◽  
Jianxiong Li ◽  
Wenjie Wang ◽  
Houming Wu ◽  
Hai Lin ◽  
...  
Keyword(s):  
Galleria Mellonella ◽  
Entomopathogenic Nematode ◽  
Culture Broth ◽  
Bacterial Symbiont ◽  
Natural Source ◽  
Photorhabdus Luminescens ◽  
Heterorhabditis Megidis ◽  
Organic Extracts

The types of metabolites produced by Photorhabdus luminescens C9 when it is introduced by Heterorhabditis megidis 90 into Galleria mellonella larvae are different from those produced in tryptic soy broth. Only 3,5-dihydroxy-4-isopropylstilbene 1 was identified from the organic extracts of P. luminescens culture broth, but both 3,5-dihydroxy-4-isopropylstilbene 1 and 3,5-dihydroxy-4-ethylstilbene 3 were isolated from the organic extracts of nematode-bacterium infected G. mellonella larvae. In addition to two pigments, both of which had been previously reported from P. luminescens C9 culture broth, three pigments, 1,8-dihydroxy-3-methoxy-9,10-anthraquinone 2, 1-hydroxy-2,6,8-trimethoxy-9,10-anthraquinone 6, and 1,4-dihydroxy-2,5-dimethoxy-9,10-anthraquinone 7 were isolated from the organic extracts of G. mellonella larvae infected by the nematode-bacterium complex. Among these, compounds 6 and 7 are novel and isolated from a natural source for the first time.Key words: Photorhabdus luminescens, Heterorhabditis megidis, 1-hydroxy-2,6,8-trimethoxy-9,10-anthraquinone, 1,4-dihydroxy-2,5-dimethoxy-9,10-anthraquinone, pigment.

scholarly journals Photorhabdus luminescens subsp. akhurstii SL0708 pathogenicity in Spodoptera frugiperda (Lepidoptera: Noctuidae) and Galleria mellonella (Lepidoptera: Pyralidae)

2017 ◽  
Vol 20 (4) ◽  
pp. 1112-1121 ◽  
Author(s):  
Julián David Salazar-Gutiérrez ◽  
Andrés Castelblanco ◽  
María Ximena Rodríguez-Bocanegra ◽  
Wilson Teran ◽  
Adriana Sáenz-Aponte
Keyword(s):  
Spodoptera Frugiperda ◽  
Galleria Mellonella ◽  
Photorhabdus Luminescens ◽  
Lepidoptera Pyralidae ◽  
Lepidoptera Noctuidae

scholarly journals A Metalloprotease Secreted by the Insect Pathogen Photorhabdus luminescens Induces Melanization

2007 ◽  
Vol 73 (23) ◽  
pp. 7622-7628 ◽  
Author(s):  
Kiara G. Held ◽  
Christopher N. LaRock ◽  
David A. D'Argenio ◽  
Celeste A. Berg ◽  
Carleen M. Collins
Keyword(s):  
Galleria Mellonella ◽  
Gel Filtration ◽  
Secreted Proteins ◽  
Photorhabdus Luminescens ◽  
Insect Pathogen ◽  
Ionization Time ◽  
Exact Function ◽  
Single Protein ◽  
Culture Supernatants

ABSTRACT Photorhabdus luminescens is a gram-negative insect pathogen that enters the hemocoel of infected hosts and produces a number of secreted proteins that promote colonization and subsequent death of the insect. In initial studies to determine the exact role of individual secreted proteins in insect pathogenesis, concentrated culture supernatants from various P. luminescens strains were injected into the tobacco hornworm Manduca sexta. Culture supernatants from P. luminescens TT01, the genome-sequenced strain, stimulated a rapid melanization reaction in M. sexta. Comparison of the profiles of secreted proteins from the various Photorhabdus strains revealed a single protein of approximately 37 kDa that was significantly overrepresented in the TT01 culture supernatant. This protein was purified by DEAE ion-exchange and Superdex 75 gel filtration chromatography and identified by matrix-assisted laser desorption ionization-time of flight analysis as the product of the TT01 gene plu1382 (NCBI accession number NC_005126); we refer to it here as PrtS. PrtS is a member of the M4 metalloprotease family. Injection of PrtS into larvae of M. sexta and Galleria mellonella and into adult Drosophila melanogaster and D. melanogaster melanization mutants (Bc) confirmed that the purified protein induced the melanization reaction. The prtS gene was transcribed by P. luminescens injected into M. sexta before death of the insect, suggesting that the protein was produced during infection. The exact function of this protease during infection is not clear. The bacteria might survive inside the insect despite the melanization process, or it might be that the bacterium is specifically activating melanization in an attempt to circumvent this innate immune response.

Photorhabdus luminescens subsp. noenieputensis subsp. nov., a symbiotic bacterium associated with a novel Heterorhabditis species related to Heterorhabditis indica

2013 ◽  
Vol 63 (Pt_5) ◽  
pp. 1853-1858 ◽  
Author(s):  
Tiarin Ferreira ◽  
Carol van Reenen ◽  
Sylvie Pagès ◽  
Patrick Tailliez ◽  
Antoinette P. Malan ◽  
...  
Keyword(s):  
Type Species ◽  
Galleria Mellonella ◽  
Entomopathogenic Nematode ◽  
Symbiotic Bacterium ◽  
Tween 20 ◽  
Haemolytic Activity ◽  
Phenotypic Traits ◽  
Photorhabdus Luminescens ◽  
Content Type ◽  
Link Type

The bacterial symbiont AM7T, isolated from a novel entomopathogenic nematode species of the genus Heterorhabditis, displays the main phenotypic traits of the genus Photorhabdus and is highly pathogenic to Galleria mellonella. Phylogenetic analysis based on a multigene approach (16S rRNA, recA, gyrB, dnaN, gltX and infB) confirmed the classification of isolate AM7T within the species Photorhabdus luminescens and revealed its close relatedness to Photorhabdus luminescens subsp. caribbeanensis , P. luminescens subsp. akhurstii and P. luminescens subsp. hainanensis . The five concatenated protein-encoding sequences (4197 nt) of strain AM7T revealed 95.8, 95.4 and 94.9 % nucleotide identity to sequences of P. luminescens subsp. caribbeanensis HG29T, P. luminescens subsp. akhurstii FRG04T and P. luminescens subsp. hainanensis C8404T, respectively. These identity values are less than the threshold of 97 % proposed for classification within one of the existing subspecies of P. luminescens . Unlike other strains described for P. luminescens , strain AM7T produces acid from adonitol, sorbitol and xylitol, assimilates xylitol and has no lipase activity on medium containing Tween 20 or 60. Strain AM7T is differentiated from P. luminescens subsp. caribbeanensis by the assimilation of N-acetylglucosamine and the absence of haemolytic activity. Unlike P. luminescens subsp. akhurstii , strain AM7T does not assimilate mannitol, and it is distinguished from P. luminescens subsp. hainanensis by the assimilation of trehalose and citrate, the inability to produce indole from tryptophan and the presence of acetoin production and urease activity. Strain AM7T ( = ATCC BAA-2407T  = DSM 25462T) belongs to a novel subspecies, and is proposed as the type strain of Photorhabdus luminescens subsp. noenieputensis sp. nov.

scholarly journals The Use of Galleria mellonella Larvae to Identify Novel Antimicrobial Agents against Fungal Species of Medical Interest

2018 ◽  
Vol 4 (3) ◽  
pp. 113 ◽  
Author(s):  
Kevin Kavanagh ◽  
Gerard Sheehan
Keyword(s):  
Fungal Pathogens ◽  
Antimicrobial Agents ◽  
Galleria Mellonella ◽  
Fungal Infections ◽  
Fungal Species ◽  
Molecular Techniques ◽  
Antifungal Drugs ◽  
Immune Priming ◽  
Greater Wax Moth

The immune system of insects and the innate immune response of mammals share many similarities and, as a result, insects may be used to assess the virulence of fungal pathogens and give results similar to those from mammals. Larvae of the greater wax moth Galleria mellonella are widely used in this capacity and also for assessing the toxicity and in vivo efficacy of antifungal drugs. G. mellonella larvae are easy to use, inexpensive to purchase and house, and have none of the legal/ethical restrictions that are associated with use of mammals. Larvae may be inoculated by intra-hemocoel injection or by force-feeding. Larvae can be used to assess the in vivo toxicity of antifungal drugs using a variety of cellular, proteomic, and molecular techniques. Larvae have also been used to identify the optimum combinations of antifungal drugs for use in the treatment of recalcitrant fungal infections in mammals. The introduction of foreign material into the hemocoel of larvae can induce an immune priming effect which may operate independently with the activity of the antifungal drug. Procedures to identify this effect and limit its action are required.

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