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In addition to its disulfide reductase activity, glutathione is known to protect cells from many forms of physiological stress. This report represents the first investigation into the role of glutathione in the Gram-positive pathogen\n                    <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Streptococcus pneumoniae<\/jats:named-content>\n                    . We demonstrate that pneumococci import extracellular glutathione using the ABC transporter substrate binding protein GshT. Mutation of\n                    <jats:italic>gshT<\/jats:italic>\n                    and the gene encoding glutathione reductase (\n                    <jats:italic>gor<\/jats:italic>\n                    ) increases pneumococcal sensitivity to the superoxide generating compound paraquat, illustrating the importance of glutathione utilization in pneumococcal oxidative stress resistance. In addition, the\n                    <jats:italic>gshT<\/jats:italic>\n                    and\n                    <jats:italic>gor<\/jats:italic>\n                    mutant strains are hypersensitive to challenge with the divalent metal ions copper, cadmium, and zinc. The importance of glutathione utilization in pneumococcal colonization and invasion of the host is demonstrated by the attenuated phenotype of the\n                    <jats:italic>gshT<\/jats:italic>\n                    mutant strain in a mouse model of infection.\n                  <\/jats:p>","DOI":"10.1128\/jb.01393-12","type":"journal-article","created":{"date-parts":[[2012,9,15]],"date-time":"2012-09-15T06:26:41Z","timestamp":1347690401000},"page":"6248-6254","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":128,"title":["Streptococcus pneumoniae Uses Glutathione To Defend against Oxidative Stress and Metal Ion Toxicity"],"prefix":"10.1128","volume":"194","author":[{"given":"Adam J.","family":"Potter","sequence":"first","affiliation":[{"name":"Research Centre for Infectious Diseases, School of Molecular and Biomedical Science, University of Adelaide, South Australia, Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Claudia","family":"Trappetti","sequence":"additional","affiliation":[{"name":"Research Centre for Infectious Diseases, School of Molecular and Biomedical Science, University of Adelaide, South Australia, Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"James C.","family":"Paton","sequence":"additional","affiliation":[{"name":"Research Centre for Infectious Diseases, School of Molecular and Biomedical Science, University of Adelaide, South Australia, Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"publisher","DOI":"10.1371\/journal.ppat.1000284"},{"key":"e_1_3_2_3_2","doi-asserted-by":"crossref","first-page":"44","DOI":"10.1006\/jmbi.1994.1472","article-title":"Three highly homologous membrane-bound lipoproteins participate in oligopeptide transport by the Ami system of the Gram-positive Streptococcus pneumoniae","volume":"241","author":"Alloing G","year":"1994","unstructured":"AlloingG DephilipP ClaverysJP. 1994. 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