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The hypersusceptibility of <jats:styled-content style=\"fixed-case\"><jats:italic>gshA<\/jats:italic><\/jats:styled-content> and <jats:styled-content style=\"fixed-case\"><jats:italic>gshB<\/jats:italic><\/jats:styled-content> mutants lacking \u03b3\u2010glutamylcysteine and glutathione synthetases to <jats:styled-content style=\"fixed-case\">NO<\/jats:styled-content> and <jats:italic><jats:styled-content style=\"fixed-case\">S<\/jats:styled-content><\/jats:italic>\u2010nitrosoglutathione indicates that <jats:styled-content style=\"fixed-case\">GSH<\/jats:styled-content> antagonizes the bacteriostatic activity of reactive nitrogen species. Metabolites of the <jats:styled-content style=\"fixed-case\">GSH<\/jats:styled-content> biosynthetic pathway do not affect the enzymatic activity of classical <jats:styled-content style=\"fixed-case\">NO<\/jats:styled-content> targets such as quinol oxidases. In contrast, <jats:styled-content style=\"fixed-case\">LMW<\/jats:styled-content> thiols diminish the nitrosative stress experienced by enzymes, such as glutamine oxoglutarate amidotransferase, that contain redox active cysteines. <jats:styled-content style=\"fixed-case\">LMW<\/jats:styled-content> thiols also preserve the transcription of <jats:italic><jats:styled-content style=\"fixed-case\">S<\/jats:styled-content>almonella<\/jats:italic> pathogenicity island 2 gene targets from the inhibitory activity of nitrogen oxides. These findings are consistent with the idea that <jats:styled-content style=\"fixed-case\">GSH<\/jats:styled-content> scavenges reactive nitrogen species (<jats:styled-content style=\"fixed-case\">RNS<\/jats:styled-content>) other than <jats:styled-content style=\"fixed-case\">NO<\/jats:styled-content>. Compared with the adaptive response afforded by inducible systems such as the <jats:styled-content style=\"fixed-case\"><jats:italic>hmp<\/jats:italic><\/jats:styled-content>\u2010encoded flavohaemoprotein, <jats:styled-content style=\"fixed-case\"><jats:italic>gshA<\/jats:italic><\/jats:styled-content>, encoding the first step of <jats:styled-content style=\"fixed-case\">GSH<\/jats:styled-content> biosynthesis, is constitutively expressed in <jats:italic><jats:styled-content style=\"fixed-case\">S<\/jats:styled-content>almonella<\/jats:italic>. An acute model of salmonellosis has revealed that the antioxidant and antinitrosative properties associated with the <jats:styled-content style=\"fixed-case\">GSH<\/jats:styled-content> biosynthetic pathway represent a first line of <jats:italic><jats:styled-content style=\"fixed-case\">S<\/jats:styled-content>almonella<\/jats:italic> resistance against reactive oxygen and nitrogen species engendered in the context of a functional <jats:styled-content style=\"fixed-case\">NRAMP<\/jats:styled-content>1<jats:styled-content style=\"fixed-case\"><jats:sup>R<\/jats:sup><\/jats:styled-content> divalent metal transporter.<\/jats:p>","DOI":"10.1111\/mmi.12119","type":"journal-article","created":{"date-parts":[[2012,12,10]],"date-time":"2012-12-10T09:39:53Z","timestamp":1355132393000},"page":"609-622","source":"Crossref","is-referenced-by-count":48,"title":["Low\u2010molecular\u2010weight thiol\u2010dependent antioxidant and antinitrosative defences in <i><scp>S<\/scp>almonella<\/i> 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