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ProteomicsHelpful dirt: Why diphtheria toxoid vaccines may also protect against non-toxigenic Corynebacterium diphtheriae strains
Diphtheria toxoid vaccines are among the oldest and safest vaccines known. The basic principle of production is the inactivation of purified diphtheria toxin by formaldehyde cross-linking, which converts the potentially fatal toxin in a completely harmless protein aggregate, which is still immunogen...
ORGANISM(S): Corynebacterium diphtheriae NCTC 13129 Clostridium tetani E88 
2019-04-17 | PXD009289 | Pride
Proteomics Corynebacterium ulcerans Mass spectrometry Corynebacteria Exoproteome Vaccination Secretome 
ProteomicsCorynebacterium diphtheriae proteome adaptation to cell culture medium and serum
ost-pathogen interactions are often studied in vitro using primary or immortal cell lines. This set-up avoids ethical problems of animal testing and has the additional advantage of lower costs. However, the influence of cell culture media on bacterial growth and metabolism is not considered or inves...
ORGANISM(S): Corynebacterium diphtheriae bv. mitis str. ISS 3319 
2021-03-12 | PXD024381 | Pride
Metabolic pathway Proteomics Host-pathogen interaction Label-free Diphtheria 
TranscriptomicsL-Glutamine metabolism and its regulation in C. glutamicum
Corynebacterium glutamicum, a gram-positive soil bacterium used for the industrial production of amino acids such as L-glutamate and L-lysine, is able to use a number of different nitrogen sources, such as ammonium, urea, or creatinine. In this communication, we show that L-glutamine serves as an ex...
ORGANISM(S): Corynebacterium glutamicum ATCC 13032 
2010-10-05 | E-GEOD-19779 | biostudies-arrayexpress
ProteomicsProteomics of diphtheria toxoid vaccines reveals multiple proteins that are immunogenic and may contribute to protection of humans against Corynebacterium diphtheriae
Introduced for mass immunization in the 1920s, vaccines against diphtheria are among the oldest and safest vaccines known. The basic principle of their production is the inactivation of purified diphtheria toxin by formaldehyde cross-linking, which converts the potentially fatal toxin in a completel...
ORGANISM(S): Corynebacterium diphtheriae NCTC 13129 Clostridium tetani E88 
2019-04-18 | PXD012806 | Pride
Proteomics Mass spectrometry Coryebacteria Exoproteome Vaccination Secretome 
ProteomicsCellular and extracellular proteome of the animal pathogen Corynebacterium silvaticum, a close relative of zoonotic Corynebacterium ulcerans and Corynebacterium pseudotuberculosis
A single paragraph of about 200 words maximum. For research articles, abstracts should give a pertinent overview of the work. We strongly encourage authors to use the following style of structured abstracts, but without headings: (1) Background: Place the question addressed in a broad context and hi...
ORGANISM(S): Corynebacterium ulcerans bv. belfanti 
2020-08-12 | PXD020400 | Pride
Exoproteome  mass spectrometry  necrotizing lymphadenitis  secretome  zoonosis  lc-ms/ms analysis 
ProteomicsProteome analysis of Corynebacterium diphtheriae - macrophage interaction
Contact of Corynebacterium diphtheriae with macrophages induce adaptations on both bacterial and cellular sides. Using an experimental design involving gentamicin protection and liquid chromagraphy followed by mass-spectrometry, a multi-species proteomic dataset was analyzed at different time points...
ORGANISM(S): Corynebacterium Diphtheriae Bv. Mitis Str. Iss3319 Homo Sapiens (ncbitaxon:9606) Corynebacterium Diphtheriae Nctc 13129 (ncbitaxon:257309) 
2025-03-13 | MSV000097308 | MassIVE
ProteomicsWhole cellular and secreted proteins of C. diphtheriae ISS3319 grown in rich medium
Validation of essential proteins by using mass spectrometry based proteomics of C. diphtheriae ISS3319 identified in a Tn5 approach. For this purpose, a theoretical proteome was conducted from sequencing data. Bacteria were grown in rich medium and proteins from the whole cell and secreted proteins ...
ORGANISM(S): Corynebacterium diphtheriae bv. mitis str. ISS 3319 
2023-04-13 | PXD036352 | Pride
Essential proteins Microbial proteomics Diphtheria 
ProteomicsProteomics of Bordetella pertussis whole-cell and acellular vaccines
Bordetella pertussis is the etiological agent of whooping cough, a bacterial infection of especially children, which may be fatal without treatment. In frame of studies to investigate putative effects of vaccination on host-pathogen interaction and clonal distribution of strains, in addition to Cory...
ORGANISM(S): Corynebacterium diphtheriae NCTC 13129 Clostridium tetani E88 Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251) 
2019-05-14 | PXD013804 | Pride
Whooping cough Mass spectrometry Bordetella Dtp vaccine Vaccination Pertussis Lc-ms/ms 
TranscriptomicsMycobacterium smegmatis - Comparison of wild type SMR5 and amtR deletion strain YL1 under nitrogen surplus
In this approach, total transcript of the Mycobacterium smegmatis wild type was compared to a amtR deletion strain under nitrogen surplus. With this experiment, putative target genes of AmtR, a regulator protein of nitrogen metabolism, were identified. Two biological replicates were analyzed. Nadja,...
ORGANISM(S): Mycobacterium smegmatis 
2011-07-01 | E-GEOD-30235 | biostudies-arrayexpress
TranscriptomicsMycobacterium smegmatis - Comparison of wild type SMR5 and amtR deletion strain YL1 under nitrogen starvation
In this approach, total transcript of the Mycobacterium smegmatis wild type was compared to a amtR deletion strain under nitrogen starvation. With this experiment, putative target genes of AmtR, a regulator protein of nitrogen metabolism, were identified. Two biological replicates were analyzed. Nad...
ORGANISM(S): Mycobacterium smegmatis 
2011-07-01 | E-GEOD-30231 | biostudies-arrayexpress
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