Protein inclusions produced by the entomopathogenic bacterium Xenorhabdus nematophilus subsp. nematophilus

Couche, Graham A.; Gregson, Richard P.

doi:10.1128/jb.169.11.5279-5288.1987

Cited by 37 publications

(32 citation statements)

References 35 publications

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“…Together, IP1 and IP2 represent Ͼ40% of the total cellular protein in stationary-phase cells (11). Immunodetection studies showed that IP1 was present in X. nematophila but not in other Xenorhabdus species (11).…”

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Analysis of the PixA Inclusion Body Protein of Xenorhabdus nematophila

et al. 2006

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The symbiotic pathogenic bacterium Xenorhabdus nematophila produces two distinct intracellular inclusion bodies. The pixA gene, which encodes the 185-residue methionine-rich PixA inclusion body protein, was analyzed in the present study. The pixA gene was optimally expressed under stationary-phase conditions but its expression did not require RpoS. Analysis of a pixA mutant strain showed that PixA was not required for virulence towards the insect host or for colonization of or survival within the nematode host, and was not essential for nematode reproduction. The pixA gene was not present in the genome of Xenorhabdus bovienii, which also produces proteinaceous inclusions, indicating that PixA is specifically produced in X. nematophila.

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“…produce two distinct proteinaceous intracellular inclusions during stationary phase in culture and in insects (2,10,11). The sister taxon of Xenorhabdus, Photorhabdus, which engages in mutualistic associations with nematodes of the Heterorhabditidae family (1,7,13), also produces two morphologically distinct proteinaceous inclusion bodies (4,8).…”

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Analysis of the PixA Inclusion Body Protein of Xenorhabdus nematophila

et al. 2006

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“…Recently, Clarke and Dowds (29) speculated that a secreted lipase is responsible for the insecticidal activity observed against Galleria mellonella. In addition to secreted factors, these bacteria are known to produce intracellular inclusion bodies similar to those produced by Bacillus thuringiensis (30,31). But unlike Bt endotoxin crystals they are not insecticidal and are thought to provide amino acid nutrients for the emerging nematodes (32).…”

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Photorhabdus luminescens W-14 Insecticidal Activity Consists of at Least Two Similar but Distinct Proteins

Guo¹,

Fatig²,

Orr³

et al. 1999

Journal of Biological Chemistry

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Both the bacterium Photorhabdus luminescens alone and its symbiotic Photorhabdus-nematode complex are known to be highly pathogenic to insects. The nature of the insecticidal activity of Photorhabdus bacteria was investigated for its potential application as an insect control agent. It was found that in the fermentation broth of P. luminescens strain W-14, at least two proteins, toxin A and toxin B, independently contributed to the oral insecticidal activity against Southern corn rootworm. Purified toxin A and toxin B exhibited single bands on native polyacrylamide gel electrophoresis and two peptides of 208 and 63 kDa on SDS-polyacrylamide gel electrophoresis. The native molecular weight of both the toxin A and toxin B was determined to be approximately 860 kDa, suggesting that they are tetrameric. NH 2 -terminal amino acid sequencing and Western analysis using monospecific antibodies to each toxin demonstrated that the two toxins were distinct but homologous. The oral potency (LD 50 ) of toxin A and toxin B against Southern corn rootworm larvae was determined to be similar to that observed with highly potent Bt toxins against lepidopteran pests. In addition, it was found that the two peptides present in toxin B could be processed in vitro from a 281-kDa protoxin by endogenous P. luminescens proteases. Proteolytic processing was shown to enhance insecticidal activity.

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“…Upon nutrient depletion, the nematodes molt into third-instar nonfeeding larvae (32), take on X. luminescens symbionts, and emerge from the insect cadaver in search of new prey (16,32). Besides bioluminescence, X. luminescens produces several other interesting products: antibiotic substances (2,30,33), extracellular proteases (3,35), extracellular lipase (3,17), intracellular protein crystals (10), and a red pigment (33). The insect cadaver does not putrefy, presumably because the antibiotic activity inhibits the growth of other bacteria.…”

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Cloning, organization, and expression of the bioluminescence genes of Xenorhabdus luminescens

1990

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The lux genes of Xenorhabdus luminescens, a symbiont of the nematode Heterorhabditis bacteriophora, were cloned and expressed in Escherichia coli. The expression of these genes in E. coli was qualitatively similar to their expression in X. luminescens. The organization of the genes is similar to that found in the marine luminous bacteria. Hybridization studies with the DNA that codes for the two subunits of luciferase revealed considerable homology among all of the strains of X. luminescens and with the DNA of other species of luminous bacteria, but none with the nonluminous Xenorhabdus species. Gross DNA alterations such as insertions, deletions, or inversions do not appear to be involved in the generation of dim variants known as secondary forms.Xenorhabdus luminescens is a luminous bacterium in the family Enterobacteriaceae (3,17,38 (1,6,7,18). The primary form is generally isolated from infective nematodes, but upon prolonged culture in various media secondary variants appear. In contrast to the primary form, the secondary variants are dim and lack detectable protease, lipase, antibiotic activity, protein crystals, and red pigment (6). The two forms also exhibit differences in colony morphology and staining properties (18). The secondary forms are deficient in providing optimum conditions for nematode reproduction (1, 7, 16).The physical and biochemical properties of the luminous system of X. luminescens are similar to those found in other bioluminescent bacteria (9,31,36 hyde to oxidized flavin and the corresponding long-chain fatty acid. A fatty acid reductase complex is required for the generation and recycling of fatty acid to aldehyde (34), and an NAD(P)H:flavin oxidoreductase supplies the reduced flavin (20). In rich media, the luminescence of X. luminescens increases dramatically during the late logarithmic or stationary phase of growth (36). The generation of secondary variants which are dim is another level of control of the luminous system of X. luminescens.The bioluminescence (lux) genes from Vibrio harveyi (8), Vibrio fischeri (12), Photobacterium leiognathi (11), and Photobacterium phosphoreum (22) have been cloned and expressed in Escherichia coli. Five structural genes are required for light emission: luxC, luxD, and luxE encode the fatty acid reductase complex, and luxA and luxB encode the alpha and beta subunits of bacterial luciferase (12,13,25). In all luminous bacteria that have been studied, these five genes are closely linked and luxA and luxB are flanked by the genes for the enzymes of the fatty acid reductase complex. In both P. phosphoreum and P. leiognathi there is another gene between luxB and luxE (19,22). The function of the product of this gene is not known.In this paper we report the cloning of the lux genes of X. luminescens and their expression when introduced into E. coli. We also present data showing the organization of the X. luminescens lux genes, the structure of the lux genes from the secondary form, and the homology of the luxA and luxB genes of X. luminescens Hm to DN...

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Protein inclusions produced by the entomopathogenic bacterium Xenorhabdus nematophilus subsp. nematophilus

Cited by 37 publications

References 35 publications

Analysis of the PixA Inclusion Body Protein of Xenorhabdus nematophila

Analysis of the PixA Inclusion Body Protein of Xenorhabdus nematophila

Photorhabdus luminescens W-14 Insecticidal Activity Consists of at Least Two Similar but Distinct Proteins

Cloning, organization, and expression of the bioluminescence genes of Xenorhabdus luminescens

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