Abstract
Cartography of the plasma proteome remains technically challenging, primarily due to the abundance and dynamic range of plasma proteins and their concentrations, exceeding ten orders of magnitude, including low-abundant tissue-derived proteins in the pg/mL range. Data-independent acquisition mass spectrometry (DIA-MS) has seen advances in unbiased mass spectrometry-based proteomic analysis of the plasma proteome. Here, we describe a comprehensive proteomic workflow of human plasma from clinically relevant sample (10 μL) that includes anti-protein immunodepletion and highly sensitive sample preparation workflow, with optimized scheduled isolation DIA-MS and deep learning analysis. This approach results in over 960 proteins quantified from a single-shot analysis of broad dynamic range, across 8 orders of magnitude (8.2 ng/L to 0.67 g/L). We further compare data-dependent acquisition (DDA) MS to highlight the advantage in protein quantification and inter-sample variation. These developments have provided streamlined identification of the human plasma proteome, including low-abundant tissue-enriched proteins, and applications toward understanding the plasma proteome.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Similar content being viewed by others
References
Geyer PE, Holdt LM, Teupser D et al (2017) Revisiting biomarker discovery by plasma proteomics. Mol Syst Biol 13:942
Shishkova E, Coon JJ (2021) Rapid preparation of human blood plasma for bottom-up proteomics analysis. STAR Protoc 2:100856
Messner CB, Demichev V, Wendisch D et al (2020) Ultra-high-throughput clinical proteomics reveals classifiers of COVID-19 infection. Cell Syst 11:11–24.e4
Gautam SS, Singh RP, Karsauliya K et al (2022) Label-free plasma proteomics for the identification of the putative biomarkers of oral squamous cell carcinoma. J Proteome 259:104541
Bauer W, Weber M, Diehl-Wiesenecker E et al (2021) Plasma proteome fingerprints reveal distinctiveness and clinical outcome of SARS-CoV-2 infection. Viruses 13:2456
Gummesson A, Björnson E, Fagerberg L et al (2021) Longitudinal plasma protein profiling of newly diagnosed type 2 diabetes. EBioMedicine 63:103147
Liu Y, Buil A, Collins BC et al (2015) Quantitative variability of 342 plasma proteins in a human twin population. Mol Syst Biol 11:786
Keshishian H, Burgess MW, Specht H et al (2017) Quantitative, multiplexed workflow for deep analysis of human blood plasma and biomarker discovery by mass spectrometry. Nat Protoc 12:1683–1701
Blume JE, Manning WC, Troiano G et al (2020) Rapid, deep and precise profiling of the plasma proteome with multi-nanoparticle protein corona. Nat Commun 11:1–14
Park J, Kim H, Kim SY et al (2020) In-depth blood proteome profiling analysis revealed distinct functional characteristics of plasma proteins between severe and non-severe COVID-19 patients. Sci Rep 10:1–10
Kimura Y, Yanagimachi M, Ino Y et al (2017) Identification of candidate diagnostic serum biomarkers for Kawasaki disease using proteomic analysis. Sci Rep 7:1–12
Zhang S, Raedschelders K, Venkatraman V et al (2020) A dual workflow to improve the proteomic coverage in plasma using data-independent acquisition-MS. J Proteome Res 19:2828–2837
Sato H, Inoue Y, Kawashima Y et al (2022) In-depth serum proteomics by DIA-MS with in silico spectral libraries reveals dynamics during the active phase of systemic juvenile idiopathic arthritis. ACS Omega 7:7012–7023
Kimura Y, Nakai Y, Shin J et al (2021) Identification of serum prognostic biomarkers of severe COVID-19 using a quantitative proteomic approach. Sci Rep 11:1–9
Bruderer R, Bernhardt OM, Gandhi T et al (2016) High-precision iRT prediction in the targeted analysis of data-independent acquisition and its impact on identification and quantitation. Proteomics 16:2246–2256
Yang Y, Liu X, Shen C et al (2020) In silico spectral libraries by deep learning facilitate data-independent acquisition proteomics. Nat Commun 11:1–11
Tran NH, Qiao R, Xin L et al (2019) Deep learning enables de novo peptide sequencing from data-independent-acquisition mass spectrometry. Nat Methods 16:63–66
Demichev V, Messner CB, Vernardis SI et al (2019) DIA-NN: neural networks and interference correction enable deep proteome coverage in high throughput. Nat Methods 17:41–44
Wichmann C, Meier F, Winter SV et al (2019) MaxQuant. Live enables global targeting of more than 25,000 peptides. Mol Cell Proteomics 18:982–994
Hughes CS, Moggridge S, Müller T et al (2019) Single-pot, solid-phase-enhanced sample preparation for proteomics experiments. Nat Protoc 14:68–85
Deutsch EW, Omenn GS, Sun Z et al (2021) Advances and utility of the human plasma proteome. J Proteome Res 20(12):5241–5263
Tyanova S, Temu T, Cox J (2016) The MaxQuant computational platform for mass spectrometry-based shotgun proteomics. Nat Protoc 11:2301–2319
Tyanova S, Cox J (2018) Perseus: a bioinformatics platform for integrative analysis of proteomics data in cancer research. Cancer Syst Biol 1711:133–148
MacLean B, Tomazela DM, Shulman N et al (2010) Skyline: an open source document editor for creating and analyzing targeted proteomics experiments. Bioinformatics 26(7):966–968
Kompa AR, Greening DW, Kong AM et al (2021) Sustained subcutaneous delivery of secretome of human cardiac stem cells promotes cardiac repair following myocardial infarction. Cardiovasc Res 117:918–929
Claridge B, Rai A, Fang H et al (2021) Proteome characterisation of extracellular vesicles isolated from heart. Proteomics 21:2100026
Rai A, Fang H, Claridge B et al (2021) Proteomic dissection of large extracellular vesicle surfaceome unravels interactive surface platform. J Extracell Vesicles 10:e12164
Poh QH, Rai A, Carmichael II et al (2021) Proteome reprogramming of endometrial epithelial cells by human trophectodermal small extracellular vesicles reveals key insights into embryo implantation. Proteomics 21:2000210
Rai A, Fang H, Fatmous M et al (2021) A protocol for isolation, purification, characterization, and functional dissection of exosomes. In: Methods in molecular biology. Humana Press Inc, pp 105–149
Kristensen K, Henriksen JR, Andresen TL (2015) Adsorption of cationic peptides to solid surfaces of glass and plastic. PLoS One 10:e0122419
Goebel-Stengel M, Stengel A, Taché Y et al (2011) The importance of using the optimal plasticware and glassware in studies involving peptides. Anal Biochem 414:38–46
Rosenberger G, Koh CC, Guo T et al (2014) A repository of assays to quantify 10,000 human proteins by SWATH-MS. Sci Data 1:1–15
Pino LK, Just SC, MacCoss MJ et al (2020) Acquiring and analyzing data independent acquisition proteomics experiments without spectrum libraries. Mol Cell Proteomics 19:1088–1103
Author information
Authors and Affiliations
Corresponding author
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2023 The Author(s), under exclusive license to Springer Science+Business Media, LLC, part of Springer Nature
About this protocol
Cite this protocol
Fang, H., Greening, D.W. (2023). An Optimized Data-Independent Acquisition Strategy for Comprehensive Analysis of Human Plasma Proteome. In: Greening, D.W., Simpson, R.J. (eds) Serum/Plasma Proteomics. Methods in Molecular Biology, vol 2628. Humana, New York, NY. https://doi.org/10.1007/978-1-0716-2978-9_7
Download citation
DOI: https://doi.org/10.1007/978-1-0716-2978-9_7
Published:
Publisher Name: Humana, New York, NY
Print ISBN: 978-1-0716-2977-2
Online ISBN: 978-1-0716-2978-9
eBook Packages: Springer Protocols