Photorhabdus asymbiotica strain:UENP 3 | isolate:UENP 3
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ABSTRACT:
PROVIDER: PRJNA1200738 | ENA |
REPOSITORIES: ENA
Similar Datasets
Project description:Photorhabdus asymbiotica asymbiotica DSM 15149 genome sequencing
| PRJNA332059 | ENA
Project description:Photorhabdus asymbiotica subsp. asymbiotica ATCC 43949 genome sequencing project
| PRJEA31267 | ENA
Project description:Photorhabdus asymbiotica subsp. asymbiotica ATCC 43949 Transcriptome or Gene expression
| PRJNA258576 | ENA
Project description:Photorhabdus and Xenorhabdus reference collection
| PRJNA678161 | ENA
Project description:Photorhabdus and Xenorhabdus reference collection
| PRJNA678162 | ENA
Project description:Photorhabdus asymbiotica is an emerging human pathogen shown to display a dramatic metabolic shift when growing at a temperature associated with mammalian body temperature compared to the temperature of an insect, its typical host. This genome-scale metabolic model is one the first steps to investigate the metabolism of this organism further in an attempt to elucidate the metabolic adaptations facilitating the survival of this pathogen at higher temperatures.
2024-08-02 | MODEL2309110001 | BioModels
Project description:BackgroundThe Gram-negative bacterium Photorhabdus asymbiotica (Pa) has been recovered from human infections in both North America and Australia. Recently, Pa has been shown to have a nematode vector that can also infect insects, like its sister species the insect pathogen P. luminescens (Pl). To understand the relationship between pathogenicity to insects and humans in Photorhabdus we have sequenced the complete genome of Pa strain ATCC43949 from North America. This strain (formerly referred to as Xenorhabdus luminescens strain 2) was isolated in 1977 from the blood of an 80 year old female patient with endocarditis, in Maryland, USA. Here we compare the complete genome of Pa ATCC43949 with that of the previously sequenced insect pathogen P. luminescens strain TT01 which was isolated from its entomopathogenic nematode vector collected from soil in Trinidad and Tobago.ResultsWe found that the human pathogen Pa had a smaller genome (5,064,808 bp) than that of the insect pathogen Pl (5,688,987 bp) but that each pathogen carries approximately one megabase of DNA that is unique to each strain. The reduced size of the Pa genome is associated with a smaller diversity in insecticidal genes such as those encoding the Toxin complexes (Tc's), Makes caterpillars floppy (Mcf) toxins and the Photorhabdus Virulence Cassettes (PVCs). The Pa genome, however, also shows the addition of a plasmid related to pMT1 from Yersinia pestis and several novel pathogenicity islands including a novel Type Three Secretion System (TTSS) encoding island. Together these data suggest that Pa may show virulence against man via the acquisition of the pMT1-like plasmid and specific effectors, such as SopB, that promote its persistence inside human macrophages. Interestingly the loss of insecticidal genes in Pa is not reflected by a loss of pathogenicity towards insects.ConclusionOur results suggest that North American isolates of Pa have acquired virulence against man via the acquisition of a plasmid and specific virulence factors with similarity to those shown to play roles in pathogenicity against humans in other bacteria.
| S-EPMC2717986 | biostudies-literature
Project description:Photorhabdus luminescens bacteria alternate lifestyles between its pathogenic insect host and its mutualistic nematode host. We found that Photorhabdus changes radically from the insect pathogenic form (P-form) to slow growing small cells when initiating mutualism (M-form). Here we characterize the gene expression of the M-form relative to the P-form.
2011-09-15 | GSE32088 | GEO
Project description:A recently described bangle lectin (PHL) from the bacterium Photorhabdus asymbiotica was identified as a mainly fucose-binding protein that could play an important role in the host-pathogen interaction and in the modulation of host immune response. Structural studies showed that PHL is a homo-dimer that contains up to seven L-fucose-specific binding sites per monomer. For these reasons, potential ligands of the PHL lectin: α-L-fucopyranosyl-containing mono-, di-, tetra-, hexa- and dodecavalent ligands were tested. Two types of polyvalent structures were investigated - calix[4]arenes and dendrimers. The shared feature of all these structures was a C-glycosidic bond instead of the more common but physiologically unstable O-glycosidic bond. The inhibition potential of the tested structures was assessed using different techniques - hemagglutination, surface plasmon resonance, isothermal titration calorimetry, and cell cross-linking. All the ligands proved to be better than free L-fucose. The most active hexavalent dendrimer exhibited affinity three orders of magnitude higher than that of standard L-fucose. To determine the binding mode of some ligands, crystal complex PHL/fucosides 2 - 4 were prepared and studied using X-ray crystallography. The electron density in complexes proved the presence of the compounds in 6 out of 7 fucose-binding sites.
| S-EPMC6797808 | biostudies-literature