ArticleInternational journal of proteomics2013
Proteomic Analysis and Label-Free Quantification of the Large Clostridium difficile Toxins.
Article in International journal of proteomics, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
8 citing papers in PubMed, 19 citations in OpenAlex.
- Binding of the extracellular matrix laminin-1 to Clostridioides difficile strains.Memorias do Instituto Oswaldo Cruz · 2022Article
- Exoproteomic analysis of two MLST clade 2 strains of Clostridioides difficile from Latin America reveal close similarities.Scientific reports · 2021Article
- Colonisation Factor CD0873, an Attractive Oral Vaccine Candidate againstMicroorganisms · 2021Article
- Effects of chlorpyrifos and trichloropyridinol on HEK 293 human embryonic kidney cells.Chemosphere · 2018Article
- Analysis of proteomes released from in vitro cultured eightGut pathogens · 2017Article
- Recent development of mass spectrometry and proteomics applications in identification and typing of bacteria.Proteomics. Clinical applications · 2016Review
- Personalized Proteomics: The Future of Precision Medicine.Proteomes · 2016Article
- Article
Corrections and comments
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Authors and funding
8 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Clostridium difficile is the leading cause of antibiotic-associated diarrhea in hospitals worldwide, due to hypervirulent epidemic strains with the ability to produce increased quantities of the large toxins TcdA and TcdB. Unfortunately, accurate quantification of TcdA and TcdB from different toxinotypes using small samples has not yet been reported. In the present study, we quantify C. difficile toxins in <0.1 mL of culture filtrate by quantitative label-free mass spectrometry (MS) using data-independent analysis (MS(E)). In addition, analyses of both purified TcdA and TcdB as well as a standard culture filtrate were performed using gel-based and gel-independent proteomic platforms. Gel-based proteomic analysis was then used to generate basic information on toxin integrity and provided sequence confirmation. Gel-independent in-solution digestion of both toxins using five different proteolytic enzymes with MS analysis generated broad amino acid sequence coverage (91% for TcdA and 95% for TcdB). Proteomic analysis of a culture filtrate identified a total of 101 proteins, among them TcdA, TcdB, and S-layer proteins.
Identifiers
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.