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      MALDI Imaging Mass Spectrometry of Fresh Water Cyanobacteria: Spatial Distribution of Toxins and Other Metabolites

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          Abstract

          Cyanobacteria are among the most ancient forms of life, yet they are known to synthesize highly sophisticated defense molecules, such as the highly hepatotoxic cyclic peptides microcystins and nodularins produced by the genera Microcystis, Anabaena and Nodularia. These metabolites are released by cyanobacteria to water environments causing episodes of fatalities among animals and humans. To better understand the releasing of these metabolites, imaging mass spectrometry (IMS) using matrix-assisted laser desorption ionization-time of flight (MALDI-TOF) was herein applied to determine the spatial distribution of such toxins directly on agar-based cultures. Other key metabolites such as aeruginosin 602 and the siderophore anachelin were also mapped in mixed cyanobacterial cultures, showing the great potential of IMS to spatially monitor the biochemical details of cyanobacterial defense and interactions.

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          Most cited references22

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          J. Proteomics

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              Fully automated multidimensional reversed-phase liquid chromatography with tandem anion/cation exchange columns for simultaneous global endogenous tyrosine nitration detection, integral membrane protein characterization, and quantitative proteomics mapping in cerebral infarcts.

              Protein tyrosine nitration (PTN) is a signature hallmark of radical-induced nitrative stress in a wide range of pathophysiological conditions, with naturally occurring abundances at substoichiometric levels. In this present study, a fully automated four-dimensional platform, consisting of high-/low-pH reversed-phase dimensions with two additional complementary, strong anion (SAX) and cation exchange (SCX), chromatographic separation stages inserted in tandem, was implemented for the simultaneous mapping of endogenous nitrated tyrosine-containing peptides within the global proteomic context of a Macaca fascicularis cerebral ischemic stroke model. This integrated RP-SA(C)X-RP platform was initially benchmarked through proteomic analyses of Saccharomyces cerevisiae, revealing extended proteome and protein coverage. A total of 27 144 unique peptides from 3684 nonredundant proteins [1% global false discovery rate (FDR)] were identified from M. fascicularis cerebral cortex tissue. The inclusion of the S(A/C)X columns contributed to the increased detection of acidic, hydrophilic, and hydrophobic peptide populations; these separation features enabled the concomitant identification of 127 endogenous nitrated peptides and 137 transmembrane domain-containing peptides corresponding to integral membrane proteins, without the need for specific targeted enrichment strategies. The enhanced diversity of the peptide inventory obtained from the RP-SA(C)X-RP platform also improved analytical confidence in isobaric tags for relative and absolute quantitation (iTRAQ)-based proteomic analyses.
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                Author and article information

                Contributors
                Role: ND
                Role: ND
                Role: ND
                Role: ND
                Role: ND
                Role: ND
                Journal
                jbchs
                Journal of the Brazilian Chemical Society
                J. Braz. Chem. Soc.
                Sociedade Brasileira de Química (São Paulo, SP, Brazil )
                0103-5053
                1678-4790
                April 2017
                : 28
                : 4
                : 521-528
                Affiliations
                [2] Campinas São Paulo orgnameUniversidade Estadual de Campinas orgdiv1Instituto de Química orgdiv2Laboratório Thomson de Espectrometria de Massas Brazil
                [1] Araraquara São Paulo orgnameUniversidade Estadual Paulista orgdiv1Instituto de Química Brazil
                Article
                S0103-50532017000400521
                10.5935/0103-5053.20160191
                bf1d11aa-4a27-449e-8c45-81f80f2218f3

                This work is licensed under a Creative Commons Attribution 4.0 International License.

                History
                : 28 June 2016
                : 21 February 2016
                Page count
                Figures: 0, Tables: 0, Equations: 0, References: 22, Pages: 8
                Product

                SciELO Brazil


                cyanobacteria,MALDI-TOF,mass spectrometry,imaging
                cyanobacteria, MALDI-TOF, mass spectrometry, imaging

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