ArticleClinical proteomics2018
Antigen 85B peptidomic analysis allows species-specific mycobacterial identification.
Article in Clinical proteomics, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers, 1 of them a synthesis that pooled it.
What it found
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Who cites it
7 citing papers in PubMed, 1 synthesis or guideline pooled it, 25 citations in OpenAlex.
- Current progress of functional nanobiosensors for potential tuberculosis diagnosis: The novel way for TB control?Frontiers in bioengineering and biotechnology · 2022Pooled it
- A multi-epitope vaccine incorporating adhesin-derived antigens protects againstFrontiers in immunology · 2025Article
- Tuberculosis Diagnosis: Current, Ongoing, and Future Approaches.Diseases (Basel, Switzerland) · 2024Review
- Rapid lateral flow test for Mycobacterium tuberculosis complex and non-tuberculous mycobacteria differentiation.Applied microbiology and biotechnology · 2024Article
- Antibodies against native proteins of Mycobacterium tuberculosis can detect pulmonary tuberculosis patients.Scientific reports · 2023Article
- Attenuated but immunostimulatory Mycobacterium tuberculosis variant bovis strain Ravenel shows variation in T cell epitopes.Scientific reports · 2023Article
- Application of antigenic biomarkers for Mycobacterium tuberculosis.Journal of Zhejiang University. Science. BReview
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
Abstract
backgroundNontuberculous mycobacteria (NTM)-mediated infections are a growing cause of worldwide morbidity, but lack of rapid diagnostics for specific NTM species can delay the initiation of appropriate treatment regimens. We thus examined whether mass spectrometry analysis of an abundantly secreted mycobacterial antigen could identify specific NTM species.
methodsWe analyzed predicted tryptic peptides of the major mycobacterial antigen Ag85B for their capacity to distinguish
resultsTheoretical tryptic digests of the Ag85B proteins of four common mycobacterial species produced peptides with distinct sequences, including two peptides that could each identify the species origin of each Ag85B protein. LC-MS/MS analysis of trypsinized culture supernatants of these four species detected one of these species-specific signature peptides in each sample. Subsequent LC-MS/MS analyses confirmed these results by targeting these species-specific Ag85B peptides.
conclusionsLC-MS/MS analysis of Ag85B peptides from trypsin-digested mycobacterial culture supernatants can rapidly detect and identify common mycobacteria responsible for most pulmonary infections caused by slow-growing mycobacteria, and has the potential to rapidly diagnose pulmonary infections caused by these mycobacteria through direct analysis of clinical specimens.
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