Xenorhabdus nematophila
Ontology highlight
ABSTRACT:
PROVIDER: PRJNA35493 | ENA |
REPOSITORIES: ENA
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| Other | ||||
| CAVM01.dat.gz | Other | |||
| CAVM01.fasta.gz | Fasta.gz | |||
| CAVM01.master.dat | Other | |||
| CCWM01.dat.gz | Other |
Items per page: 5 1 - 5 of 128 |
Similar Datasets
Project description:A fliZ mutant in the entomopathogenic bacterium X. nematophila is attenuated in virulence in the insect. The goal of this study is to compare transcriptomes of the fliZ mutant and wild type strain to identify the FliZ regulon.
2013-05-27 | GSE47365 | GEO
Project description:A fliZ mutant in the entomopathogenic bacterium X. nematophila is attenuated in virulence in the insect. The goal of this study is to compare transcriptomes of the fliZ mutant and wild type strain to identify the FliZ regulon. Two biological replicates of total RNA from exponential cultures of WT strain and fliZ mutant were analysed by deep sequencing, using Illumina HiSeq 2000.
2013-05-27 | E-GEOD-47365 | biostudies-arrayexpress
Project description:A nematode symbiont that is pathogenic to insect larvae
| PRJNA13400 | ENA
Project description:Analysis of size selected RNA samples to identify sRNAs using wild-type and rpoS mutant strains.
2013-03-26 | GSE45298 | GEO
Project description:The CpxRA signal transduction system, which in Escherichia coli regulates surface structure assembly and envelope maintenance, is involved in the pathogenic and mutualistic interactions of the entomopathogenic bacterium Xenorhabdus nematophila. When DeltacpxR1 cells were injected into Manduca sexta insects, the time required to kill 50% of the insects was twofold longer than the time observed for wild-type cells and the DeltacpxR1 cells ultimately killed 16% fewer insects than wild-type cells killed. During mutualistic colonization of Steinernema carpocapsae nematodes, the DeltacpxR1 mutant achieved colonization levels that were only 38% of the wild-type levels. DeltacpxR1 cells exhibited an extended lag phase when they were grown in liquid LB or hemolymph, formed irregular colonies on solid medium, and had a filamentous cell morphology. A mutant with a cpxRp-lacZ fusion had peaks of expression in the log and stationary phases that were conversely influenced by CpxR; the DeltacpxR1 mutant produced 130 and 17% of the wild-type beta-galactosidase activity in the log and stationary phases, respectively. CpxR positively influences motility and secreted lipase activity, as well as transcription of genes necessary for mutualistic colonization of nematodes. CpxR negatively influences the production of secreted hemolysin, protease, and antibiotic activities, as well as the expression of mrxA, encoding the pilin subunit. Thus, X. nematophila CpxRA controls expression of envelope-localized and secreted products, and its activity is necessary for both mutualistic and pathogenic functions.
| S-EPMC2168154 | biostudies-literature
Project description:Draft genome of the entomopathogenic bacterium Xenorhabdus nematophila strain F1
| PRJEB1529 | ENA
Project description:Xenorhabdus nematophila is an insect pathogen and produces protein toxins which kill the larval host. Previously, we characterized an orally toxic, large, outer membrane-associated protein complex from the culture medium of X. nematophila. Here, we describe the cloning, expression, and characterization of a 17-kDa pilin subunit of X. nematophila isolated from that protein complex. The gene was amplified by PCR, cloned, and expressed in Escherichia coli. The recombinant protein was refolded in vitro in the absence of its cognate chaperone by using a urea gradient. The protein oligomerized during in vitro refolding, forming multimers. Point mutations in the conserved N-terminal residues of the pilin protein greatly destabilized its oligomeric organization, demonstrating the importance of the N terminus in refolding and oligomerization of the pilin subunit by donor strand complementation. The recombinant protein was cytotoxic to cultured Helicoverpa armigera larval hemocytes, causing agglutination and subsequent release of the cytoplasmic enzyme lactate dehydrogenase. The agglutination of larval cells by the 17-kDa protein was inhibited by several sugar derivatives. The biological activity of the purified recombinant protein indicated that it has a conformation similar to that of the native protein. The 17-kDa pilin subunit was found to be orally toxic to fourth- or fifth-instar larvae of an important crop pest, H. armigera, causing extensive damage to the midgut epithelial membrane. To our knowledge, this is first report describing an insecticidal pilin subunit of a bacterium.
| S-EPMC516617 | biostudies-literature
Project description:Xenorhabdus nematophila FliZ regulon identification by RNA-Seq
| PRJNA205296 | ENA
Project description:RNA-seq analysis of Xenorhabdus nematophila
| PRJNA194148 | ENA