Ontology highlight
ABSTRACT:
PROVIDER: PRJNA811115 | ENA |
REPOSITORIES: ENA
Similar Datasets
Project description:<p>Rapid evaporative ionisation mass spectrometry (REIMS) has been demonstrated capable of bacterial speciation by differentiation of their metabolic/lipidomic profiles. Previous work has shown the use of hand-held probes [1,2], and this dataset makes use of a robotic sampling probe which allows for high-throughput analysis [3]. This dataset consists of 651 isolates spanning 38 bacterial (564 isolates) and 6 (87 isolates) fungal species. Data are provided as Waters .raw and .mzXML files, with taxonomic and sample culturing information.</p><p><br></p><p>[1] Strittmatter, N. et al., Analysis of intact bacteria using rapid evaporative ionisation mass spectrometry. <em>Chem. Commun.</em>, 2013, 49, 6188-6190. https://doi.org/10.1039/C3CC42015A</p><p>[2] Strittmatter, N. et al., Characterization and Identification of Clinically Relevant Microorganisms Using Rapid Evaporative Ionization Mass Spectrometry. <em>Anal. Chem.</em>, 2014, 86, 6555-6562. https://doi.org/10.1021/ac501075f</p><p>[3] Bolt, F. et al., Automated High-Throughput Identification and Characterization of Clinically Important Bacteria and Fungi using Rapid Evaporative Ionization Mass Spectrometry. <em>Anal. Chem</em>., 2016, 88, 9419-9426. https://doi.org:10.1021/acs.analchem.6b01016</p>
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Project description:Many clinically relevant bacterial pathogens are encapsulated, as exemplified by Salmonella enterica serovar Typhi. S. Typhi, the causative agent of the life-threatening systemic disease enteric fever, expresses Vi as the outermost surface glycan that protects the bacteria from host immune responses. Multidrug-resistant (MDR) and extensively drug-resistant (XDR) S. Typhi strains, as well as Vi variants, are widespread globally. Our WGS analyses indicate that almost all S. Typhi clinical isolates are susceptible to rifamycins and azithromycin. Rifampin, even at sub-MIC levels, eliminates the protective capsule Vi, a process referred to as ‘decapsulation’, thereby enhancing bacterial clearance. Antibiotic-mediated decapsulation of S. Typhi appears specific to rifamycins, since azithromycin does not decapsulate S. Typhi. Rifampin mediated decapsulation occurs at the transcriptional level, where both high AT content and specific RpoB residues play a crucial role. Rifampin also effectively decapsulates Vi variants, which accounts for 1 in 5 S. Typhi isolates at the global level. A mechanistic explanation for rifampin mediated decapsulation of S. Typhi appears to be applicable to other encapsulated pathogens, including S. Paratyphi C.
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Project description:The aim of the study was to carry out a CGH study utilizing a set of 39 diverse Bacillus isolates. Thirty four B. cereus and five B. anthracis strains and isolates were chosen so as to represent different lineages based on previous characterizations, including MLEE and MLST (Helgason, Okstad et al. 2000; Helgason, Tourasse et al. 2004). They represent the spectrum of B. cereus phenotypic diversity by including soil, dairy and periodontal isolates in addition to virulent B. anthracis strains.
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Project description:WGS analysys of mcr positive bacterial isolates
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Project description:Precise definition of porin profiles is of critical importance to understand the role of porins in antimicrobial resistance. In this study, the outer membrane proteins (OMP) profiles of 26 clinical isolates of Klebsiella pneumoniae and of strain ATCC 13883 (wild-type) and ATCC 700603 (producing SHV-18) have been determined using both sodium-dodecyl-sulphate polyacrylamide gel electrophoresis (SDS-PAGE) and matrix-assisted laser desorption/ionization–time of flight/mass spectrometry (MALDI-TOF/MS). SDS-PAGE was performed using both homemade and commercial gels, and protein bands were identified by liquid chromatography coupled to mass spectrometry. A rapid extraction method was used to analyse OMPs by MALDI-TOF/MS. The sequences of porin genes were obtained by whole genome sequencing (WGS) and mutations were defined by BLAST. Same results were obtained for all strains either using SDS-PAGE or MALDI-TOF/MS. SDS-PAGE showed protein bands of ~35, ~36, and ~37 KDa, identified as OmpA, OmpK36 and OmpK35, respectively. By MALDI-TOF/MS, peaks at ~35700 (OmpA), ~37000 (OmpK35), and ~38000 (OmpK36) m/z were detected. ompK35 was intact in nine wild-type isolates and was truncated in 13 isolates, but OmpK35 was not observed in 3 isolates without mutations in ompK35. One point mutation was detected in another isolate and multiple mutations were detected in the remaining isolate. ompK36 was truncated in two isolates lacking this protein and presented one point mutation (n=1) or multiple mutations in the remaining isolates. In conclusion, MALDI-TOF/MS was reliable for porin detection, but because of the complex regulation of porin genes, WGS cannot always anticipate protein expression, as observed with SDS-PAGE and MALDI-TOF/MS.
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Project description:We compare the transcriptome of gnotobiotic Ae. aegypti generated by contaminating axenic (bacteria-free) larvae with bacterial isolates found in natural mosquito breeding sites. We focused on four bacterial isolates (Lysobacter, Flavobacterium, Paenibacillus and Enterobacteriaceae) and found that different gnotobiotic treatments resulted in massive transcriptomic changes throughout the mosquito development.
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