Citrobacter koseri
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ABSTRACT:
PROVIDER: PRJNA35377 | ENA |
REPOSITORIES: ENA
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Project description:Causative agent of neonatal meningitis and brain abscesses.
| PRJNA12716 | ENA
Project description:Citrobacter koseri, an aerobic Gram-negative bacterium, is isolated from the human skin and intestinal tract. Here, we report the complete genome sequence of Citrobacter koseri strain MPUCK001, which has a 4.9-Mbp genome, containing 4,536 protein-coding sequences.
| S-EPMC7729419 | biostudies-literature
Project description:Citrobacter species are opportunistic bacterial pathogens that have been implicated in both nosocomial and community-acquired infections. Among the genus Citrobacter, Citrobacter koseri is often isolated from clinical material, and has been known to cause meningitis and brain abscess in neonates and immunocompromised individuals. The virulence determinants of Citrobacter, however, remain largely unknown. Based on traditional methods, the genus Citrobacter has been divided into 11 species, but this has been problematic. Here, we determined an improved, detailed, and more accurate phylogeny of the genus Citrobacter based on whole genome sequence (WGS) data from 129 Citrobacter genomes, 31 of which were sequenced in this study. A maximum likelihood (ML) phylogeny constructed with core genome single-nucleotide polymorphisms (SNPs) classified all Citrobacter isolates into 11 distinct groups, with all C. koseri strains clustering into a single group. For comprehensive and systematic comparative genomic analyses, we investigated the distribution of virulence factors, resistance genes, and macromolecular secretion systems among the Citrobacter genus. Moreover, combined with group-specific genes analysis, we identified a key gene cluster for iron transport, which is present in the C. koseri group, but absent in other the groups, suggesting that the high-pathogenicity island (HPI) cluster may be important for the pathogenicity of C. koseri. Animal experiments showed that loss of the HPI cluster significantly decreased C. koseri virulence in mice and rat. Further, we provide evidence to explain why Citrobacter freundii is less susceptible than C. koseri to several antibiotics in silico. Overall, our data reveal novel virulence clusters specific to the predominantly pathogenic C. koseri strains, which form the basis for elucidating the virulence mechanisms underlying these important pathogens.
| S-EPMC6908497 | biostudies-literature
Project description:Citrobacter koseri (formerly Citrobacter diversus) is a motile gram-negative bacillus usually arising from urinary and gastrointestinal tracts. C. koseri rarely causes infection in immunocompetent patients and, thus far, has been considered an opportunistic pathogen. We report on a 30-year-old man, with no medical past, hospitalized for infective aortic endocarditis due to C. koseri. Four weeks of antibiotherapy led to a full recovery for this patient. However, this case is unusual, as previous history and 1 year of follow-up showed no features of intercurrent immunosuppression. Microbiological diagnosis was based on using 16S rRNA gene sequencing.
| S-EPMC2786675 | biostudies-literature
Project description:Citrobacter koseri that causes nosocomial infection
| PRJNA816192 | ENA
Project description:Whole genome sequencing of Citrobacter diversus, an opportunistic pathogen
| PRJDB2515 | ENA
Project description:Citrobacter koseri Genome sequencing and assembly
| PRJNA855482 | ENA
Project description:Whole genome sequencing of Citrobacter diversus, an opportunistic pathogen
| PRJDB2832 | ENA
Project description:Causative agent of meningitis, endocarditis, septicemia and arthritis in swine
| PRJNA12461 | ENA
Project description:Acetate is an important metabolite in metabolism and cell signaling. Succinate-Acetate Permease (SatP) superfamily proteins are known to be responsible for acetate transport across membranes, but the nature of this transport remains unknown. Here, we show that the SatP homolog from Citrobacter koseri (SatP_Ck) is an anion channel that can unidirectionally translocate acetate at rates of the order of ~107?ions/s. Crystal structures of SatP_Ck in complex with multiple acetates at 1.8?Å reveal that the acetate pathway consists of four acetate-binding sites aligned in a single file that are interrupted by three hydrophobic constrictions. The bound acetates at the four sites are each orientated differently. The acetate at the cytoplasmic vestibule is partially dehydrated, whereas those in the main pore body are fully dehydrated. Aromatic residues within the substrate pathway may coordinate translocation of acetates via anion-? interactions. SatP_Ck reveals a new type of selective anion channel and provides a structural and functional template for understanding organic anion transport.
| S-EPMC5993801 | biostudies-literature