Development of a rapid and specific MALDI-TOF mass spectrometric assay for SARS-CoV-2 detection

Kollhoff, Lydia; Kipping, Marc; Rauh, Manfred; Ceglarek, Uta; Barka, Günes; Barka, Frederik; Sinz, Andrea

doi:10.1186/s12014-023-09415-y

Cited by 6 publications

(3 citation statements)

References 19 publications

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“…85 A MALDI-ToF-MS method was optimized for the rapid detection of the SARS-CoV-2 nucleoprotein at a level of 8 amol/μL. 86 Demonstrating the significance of the clinical application of proteomics, analysis of diverse clinical specimens from thousands of patients identified proteomic signatures that can distinguish between severe and mild disease outcomes. 87 Tissue-specific alterations in host proteomes were discovered, pointing to opportunities for organ-specific therapeutic interventions.…”

Section: Infectious Diseasesmentioning

confidence: 99%

“…From continued work on the COVID-19 pandemic, databases were constructed for the MS identification of mutated peptides from SARS-CoV-2 variants across different geographical regions . A MALDI-ToF-MS method was optimized for the rapid detection of the SARS-CoV-2 nucleoprotein at a level of 8 amol/μL . Demonstrating the significance of the clinical application of proteomics, analysis of diverse clinical specimens from thousands of patients identified proteomic signatures that can distinguish between severe and mild disease outcomes .…”

Section: Biology and Disease-driven Hppmentioning

confidence: 99%

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The 2023 Report on the Proteome from the HUPO Human Proteome Project

Omenn,

Lane,

Overall

et al. 2024

J. Proteome Res.

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Since 2010, the Human Proteome Project (HPP), the flagship initiative of the Human Proteome Organization (HUPO), has pursued two goals: (1) to credibly identify the protein parts list and (2) to make proteomics an integral part of multiomics studies of human health and disease. The HPP relies on international collaboration, data sharing, standardized reanalysis of MS data sets by PeptideAtlas and MassIVE-KB using HPP Guidelines for quality assurance, integration and curation of MS and non-MS protein data by neXtProt, plus extensive use of antibody profiling carried out by the Human Protein Atlas. According to the neXtProt release 2023-04-18, protein expression has now been credibly detected (PE1) for 18,397 of the 19,778 neXtProt predicted proteins coded in the human genome (93%). Of these PE1 proteins, 17,453 were detected with mass spectrometry (MS) in accordance with HPP Guidelines and 944 by a variety of non-MS methods. The number of neXtProt PE2, PE3, and PE4 missing proteins now stands at 1381. Achieving the unambiguous identification of 93% of predicted proteins encoded from across all chromosomes represents remarkable experimental progress on the Human Proteome parts list. Meanwhile, there are several categories of predicted proteins that have proved resistant to detection regardless of protein-based methods used. Additionally there are some PE1–4 proteins that probably should be reclassified to PE5, specifically 21 LINC entries and ∼30 HERV entries; these are being addressed in the present year. Applying proteomics in a wide array of biological and clinical studies ensures integration with other omics platforms as reported by the Biology and Disease-driven HPP teams and the antibody and pathology resource pillars. Current progress has positioned the HPP to transition to its Grand Challenge Project focused on determining the primary function(s) of every protein itself and in networks and pathways within the context of human health and disease.

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Section: Infectious Diseasesmentioning

confidence: 99%

Section: Biology and Disease-driven Hppmentioning

confidence: 99%

The 2023 Report on the Proteome from the HUPO Human Proteome Project

Omenn,

Lane,

Overall

et al. 2024

J. Proteome Res.

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“…Therefore, an immunoaffinity step, applied during sample preparation, purifies the target peptides to improve the sensitivity of this targeted assay and substantially shorten the LC-MS run to 1–2 min 8 , 9 . Most recently, a MALDI-TOF approach describes considerably higher throughput, albeit with a compromise in sensitivity 14 .…”

Section: Introductionmentioning

confidence: 99%

Acoustic ejection mass spectrometry empowers ultra-fast protein biomarker quantification

Van Puyvelde,

Hunter,

Zhgamadze

et al. 2024

Nat Commun

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The global scientific response to COVID 19 highlighted the urgent need for increased throughput and capacity in bioanalytical laboratories, especially for the precise quantification of proteins that pertain to health and disease. Acoustic ejection mass spectrometry (AEMS) represents a much-needed paradigm shift for ultra-fast biomarker screening. Here, a quantitative AEMS assays is presented, employing peptide immunocapture to enrich (i) 10 acute phase response (APR) protein markers from plasma, and (ii) SARS-CoV-2 NCAP peptides from nasopharyngeal swabs. The APR proteins were quantified in 267 plasma samples, in triplicate in 4.8 h, with %CV from 4.2% to 10.5%. SARS-CoV-2 peptides were quantified in triplicate from 145 viral swabs in 10 min. This assay represents a 15-fold speed improvement over LC-MS, with instrument stability demonstrated across 10,000 peptide measurements. The combination of speed from AEMS and selectivity from peptide immunocapture enables ultra-high throughput, reproducible quantitative biomarker screening in very large cohorts.

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