Dataset Information

Proteome analysis of serum proteins enriched by lectins

ABSTRACT: Serum proteins enriched by 37 different lectins were analyzed by LC-MS/MS. It was found that the enrichment process with Solanum tuberosum lectin (STL) and Lycopersicon esculentum lectin (LEL) detected many trace proteins in the serum. In addition, combinations of lectins were examined, and the combination of STL and LEL was found to be optimal for observing serum trace proteins. The enrichment method by STL/LEL was able to collect trace proteins from sera of various animal species as well as humans. We further applied this STL/LEL method to systemic lupus erythematosus (SLE) models and control mouse serum to search for serum proteins altered by SLE.

ORGANISM(S): Homo Sapiens (human) Gallus Gallus Rattus Norvegicus Ovis Aries Cellular Organisms Capra Hircus Bos Taurus Mus Musculus (mouse)

SUBMITTER: Yusuke Kawashima

PROVIDER: PXD047848 | JPOST Repository | Fri Feb 23 00:00:00 GMT 2024

REPOSITORIES: jPOST

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Proteome Analysis of Serum Purified Using <i>Solanum tuberosum</i> and <i>Lycopersicon esculentum</i> Lectins.

Nakajima Daisuke D Konno Ryo R Miyashita Yasuomi Y Ishikawa Masaki M Ohara Osamu O Kawashima Yusuke Y

International journal of molecular sciences 20240121 2

Serum and plasma exhibit a broad dynamic range of protein concentrations, posing challenges for proteome analysis. Various technologies have been developed to reduce this complexity, including high-abundance depletion methods utilizing antibody columns, extracellular vesicle enrichment techniques, and trace protein enrichment using nanobead cocktails. Here, we employed lectins to address this, thereby extending the scope of biomarker discovery in serum or plasma using a novel approach. We enrich ...[more]

PMID: 38279312

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Project description:Objectives: Hashimoto’s thyroiditis (HT) is one of the most common autoimmune disorders; however, its underlying pathological mechanisms remain unclear. Although aberrant glycosylation has been implicated in the N-glycome of immunoglobulin G (IgG), changes in serum proteins have not been comprehensively characterized. This study aimed to investigate the glycosylation profile of serum samples of HT patients that were depleted of highly abundant proteins by and propose the potential functions of glycoproteins for the further study of pathological mechanisms of HT . Methods: A lectin microarray containing 70 lectins was used to detect and analyze glycosylation of serum proteins using serum samples (N=27 HT; N=26 healthy control [HC]) depleted of abundant proteins. Significant differences in glycosylation status between HT patients and the HC group were verified by lectin blot analysis. A lectin-based pull-down assay combined with mass spectrometry was used to investigate potential glycoproteins combined with differentially present lectins, and an enzyme-linked immunosorbent assay (ELISA) was used to identify the expression of targeted glycoproteins in 131 patients with papillary thyroid carcinoma (PTC), 131 patients with benign thyroid nodules (BTN) patients, 130 patients with HT, and 128 HCs. Results: Compared with the HC group, the majority of the lectin binding signals in HT group were weakened, while the Vicia villosa agglutinin (VVA) binding signal was increased. The difference in VVA binding signals verified by lectin blotting was consistent with the results of the lectin microarray. A total of 113 potential VVA-binding glycoproteins were identified by mass spectrometry and classified by gene ontology (GO) and kyoto encyclopedia of genes and genomes (KEGG) analyses . Using ELISA, we confirmed that lactoferrin (LTF) and mannan-binding lectin-associated serine protease 1 (MASP-1) levels were elevated in the serum of patients with HT and PTC. Conclusions: Following depletion of abundant proteins, remaining serum proteins in HT patients exhibited lower glycosylation levels than those observed in HCs. An increased level of potential VVA-binding glycoproteins may play an important role in HT development. LTF and MASP-1 expression was significantly higher in the serum of HT and PTC patients, suggesting key roles played by glycosylation in pathological mechanisms underlying HT and PTC.

Project description:More humans have died of tuberculosis (TB) than any other infectious disease and millions still die each year. Experts advocate for blood-based, protein biomarkers to help diagnosis TB, which is critical in high-burden countries. However, the protein biomarker pipeline is small. Here, we used the Diversity Outbred (DO) mouse population to address this gap, identifying five protein biomarker candidates. One biomarker, serum CXCL1, met the World Health Organization’s Targeted Product Profile for a triage test to diagnose active TB from latent M.tb infection (LTBI), non-TB lung disease, and normal sera in HIV-negative, adults from South Africa and Vietnam. To find the biomarker candidates, we quantified seven immune mediators and four proteins corresponding to a subset of highly expressed genes unique to progressor DO mice. Next, we applied statistical and machine learning methods to the data, i.e., 11 proteins in lungs from 453 infected and 29 non-infected mice. After searching all combinations of five algorithms and 239 protein subsets, validating, and testing the findings on independent data, two combinations accurately diagnosed progressor DO mice: Logistic Regression using MMP8; and Gradient Tree Boosting using a panel of 4: CXCL1, CXCL2, TNF, IL-10. Of those five protein biomarker candidates, two (MMP8 and CXCL1) were crucial for classifying DO mice; were above the limit of detection in most human serum samples; and had not been widely assessed for diagnostic performance in humans before. In patient sera, CXCL1 exceeded the triage diagnostic test criteria (>90% sensitivity; >70% specificity), while MMP8 did not. Using Area Under the Curve analyses, CXCL1 averaged 94.5% sensitivity and 88.8% specificity for active pulmonary TB (ATB) vs LTBI; 90.9% sensitivity and 71.4% specificity for ATB vs non-TB; and 100.0% sensitivity and 98.4% specificity for ATB vs normal sera. Our findings overall show that the DO mouse population can discover diagnostic-quality, serum protein biomarkers of human TB.

			Action	DRS
	DIA-T60-Serum_PHA-L.raw	Raw
	DIA-T60-Serum_PNA.raw	Raw
	DIA-T60-Serum_PSA.raw	Raw
	DIA-T60-Serum_RCA-I.raw	Raw
	DIA-T60-Serum_SBA.raw	Raw

Dataset Information

Proteome analysis of serum proteins enriched by lectins

Dataset's files

Publications

Proteome Analysis of Serum Purified Using <i>Solanum tuberosum</i> and <i>Lycopersicon esculentum</i> Lectins.

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OmicsDI is part of the ELIXIR infrastructure

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Dataset Information

Proteome analysis of serum proteins enriched by lectins

Dataset's files

Publications

Proteome Analysis of Serum Purified Using &lt;i&gt;Solanum tuberosum&lt;/i&gt; and &lt;i&gt;Lycopersicon esculentum&lt;/i&gt; Lectins.

Similar Datasets

OmicsDI is part of the ELIXIR infrastructure

Tweets

Proteome Analysis of Serum Purified Using <i>Solanum tuberosum</i> and <i>Lycopersicon esculentum</i> Lectins.