Fluorescence proteomic technology to analyze peripheral blood mononuclear cells in chronic chagas disease

John E Wiktorowicz, M. Paola Zago, Nisha J. Garg

    Research output: Chapter in Book/Report/Conference proceedingChapter

    Abstract

    The thiol moieties of cysteinyl residues in proteins undergo a number of modifications including nitrosylation, oxidation, persulfidation, sulfenylation, and others. These protein modifications may influence gain as well as loss of function in biological and disease conditions. Herein, we describe a quantitative approach that combines accurate, sensitive fluorescence modification of cysteinyl-S-nitrosyl (SNOFlo) groups that leaves electrophoretic mobility unaffected and offers the measurement of changes in S-nitrosylation (SNO) status relative to protein abundance. This approach has been useful in evaluating the global protein abundance and SNO profile of Chagas seropositive individuals that were categorized in clinically asymptomatic (C/A) and clinically symptomatic (C/S) subgroups and compared to normal healthy (N/H) controls. Through analyzing the proteome datasets with different bioinformatics and statistics tools, potential pathologic mechanisms in disease progression are identified. We also propose a panel of protein biomarkers that have a potential to identify the infected individuals at risk of developing clinical Chagas disease.

    Original languageEnglish (US)
    Title of host publicationMethods in Molecular Biology
    PublisherHumana Press Inc.
    Pages363-380
    Number of pages18
    DOIs
    StatePublished - Jan 1 2019

    Publication series

    NameMethods in Molecular Biology
    Volume1955
    ISSN (Print)1064-3745

    Keywords

    • 2DE
    • Chagas cardiomyopathy
    • Mass spectrometry
    • Peripheral blood mononuclear cells
    • S-nitrosylation
    • Trypanosoma cruzi

    ASJC Scopus subject areas

    • Molecular Biology
    • Genetics

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