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<datestamp>2017-12-21</datestamp>
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<title lang=en>Two-dimensional fluorescence difference gel electrophoresis analysis of Listeria monocytogenes submitted to a redox shock.</title>
<creator>Ignatova, Maria</creator>
<creator>Guével, Blandine</creator>
<creator>Com, Emmanuelle</creator>
<creator>Haddad, Nabila</creator>
<creator>Rossero, Albert</creator>
<creator>Bogard, Philippe</creator>
<creator>Prévost, Hervé</creator>
<creator>Guillou, Sandrine</creator>
<contributor>Sécurité des Aliments (SECALIM) ; Institut National de la Recherche Agronomique (INRA) - Ecole Nationale Vétérinaire de Nantes</contributor>
<contributor>Plateforme Protéomique-Biogenouest (PPB) ; Institut de recherche, santé, environnement et travail [Rennes] (Irset) ; Université d'Angers (UA) - Université des Antilles et de la Guyane (UAG) - Université de Rennes 1 (UR1) - École des Hautes Études en Santé Publique [EHESP] (EHESP) - Institut National de la Santé et de la Recherche Médicale (INSERM) - Structure Fédérative de Recherche en Biologie et Santé de Rennes ( Biosit : Biologie - Santé - Innovation Technologique ) - Université d'Angers (UA) - Université des Antilles et de la Guyane (UAG) - Université de Rennes 1 (UR1) - École des Hautes Études en Santé Publique [EHESP] (EHESP) - Institut National de la Santé et de la Recherche Médicale (INSERM) - Structure Fédérative de Recherche en Biologie et Santé de Rennes ( Biosit : Biologie - Santé - Innovation Technologique ) - Proteomics Core Facility (Protim) ; Université de Rennes 1 (UR1) - Plateforme Génomique Santé Biogenouest® - Plateforme Génomique Santé Biogenouest®</contributor>
<contributor>Nonlinear Dynamics ; Nonlinear Dynamics</contributor>
<contributor>Proteomics Core Facility, Biogenouest ; AISQAL, Région Pays de la Loire ;</contributor>
<description>International audience</description>
<source>ISSN: 1874-3919</source>
<source>EISSN: 1876-7737</source>
<source>Journal of Proteomics</source>
<publisher>Elsevier</publisher>
<identifier>hal-00877138</identifier>
<identifier>https://hal-univ-rennes1.archives-ouvertes.fr/hal-00877138</identifier>
<source>https://hal-univ-rennes1.archives-ouvertes.fr/hal-00877138</source>
<source>Journal of Proteomics, Elsevier, 2013, 79, pp.13-27. 〈10.1016/j.jprot.2012.11.010〉</source>
<identifier>DOI : 10.1016/j.jprot.2012.11.010</identifier>
<relation>info:eu-repo/semantics/altIdentifier/doi/10.1016/j.jprot.2012.11.010</relation>
<identifier>PUBMED : 23195917</identifier>
<relation>info:eu-repo/semantics/altIdentifier/pmid/23195917</relation>
<language>en</language>
<subject lang=it>Proteomics</subject>
<subject lang=it>Two-dimensional fluorescence difference gel electrophoresis (2D-DIGE)</subject>
<subject lang=it>Listeria monocytogenes</subject>
<subject lang=it>Redox potential</subject>
<subject>[SDV.BC] Life Sciences [q-bio]/Cellular Biology</subject>
<type>info:eu-repo/semantics/article</type>
<type>Journal articles</type>
<description lang=en>The influence of redox alteration on the growth and proteomic pattern of Listeria monocytogenes was investigated. A redox shock was induced in cultures by addition of 3mM ferricyanide (FeCN) and 6mM dithiothreitol (DTT) to increase or to decrease respectively the redox potential naturally occurring at the beginning of growth. In both conditions, the reducing and oxidizing redox shock had a strong influence, decreasing the maximum growth rate by half compared to a control culture. The proteomic analysis of L. monocytogenes performed by two-dimensional difference gel electrophoresis (2D-DIGE) exhibited twenty-three proteins differentially expressed (P<0.05), among these, many were oxidoreductases, and proteins involved in cellular metabolism (glycolysis, protein synthesis), detoxification (kat) or adhesion (Lmo1634).</description>
<date>2013-02-21</date>
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