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The\n                    <jats:italic>SOD2<\/jats:italic>\n                    protein (SOD2p) encoded 225 amino acids, with 36\u201366% identity with other fungal SOD2ps.\n                    <jats:italic>SOD2<\/jats:italic>\n                    deletion rendered\n                    <jats:italic>Cn<\/jats:italic>\n                    highly growth\u2010defective at 37\u00b0C in 19\u201320% oxygen (normal air), and this defect was reversed by limiting oxygen to 1.3% as well in the presence of antioxidant, ascorbic acid. The\n                    <jats:italic>sod2<\/jats:italic>\n                    mutant accumulated significantly more reactive oxygen species (ROS) at 37\u00b0C as well at 30\u00b0C in the presence of antimycin A, suggesting that SOD2p is the primary defence of\n                    <jats:italic>Cn<\/jats:italic>\n                    against the superoxide anion (O\n                    <jats:sub>2<\/jats:sub>\n                    <jats:sup>\u2022\u200a\u2212<\/jats:sup>\n                    ) in the mitochondria. The\n                    <jats:italic>sod2<\/jats:italic>\n                    was also highly susceptible to redox\u2010cycling agents, high salt and nutrient limitations. The\n                    <jats:italic>sod2<\/jats:italic>\n                    mutant was avirulent in intranasally infected mice and markedly attenuated in its virulence in intravenously infected mice. The virulence defect of\n                    <jats:italic>sod2<\/jats:italic>\n                    mutant appeared related to its growth defects in high oxygen environment, but not resulting from increased sensitivity to oxidative killing by phagocytes. The\n                    <jats:italic>sod1sod2<\/jats:italic>\n                    double mutants were avirulent in mice. Additionally,\n                    <jats:italic>sod1sod2<\/jats:italic>\n                    double mutants showed a marked reduction in the activities of other known\n                    <jats:italic>Cn<\/jats:italic>\n                    virulence factors; and they were more susceptible to PMN killing than was the\n                    <jats:italic>sod2<\/jats:italic>\n                    single mutant. Previously, we reported that the attenuation of\n                    <jats:italic>sod1<\/jats:italic>\n                    mutant in mice was resulting from enhanced susceptibility to phagocyte killing, combined with a reduction in the activities of a number of virulence factors. Thus, SOD1p and SOD2p play distinct roles in the biology and virulence of\n                    <jats:italic>Cn<\/jats:italic>\n                    var.\n                    <jats:italic>gattii<\/jats:italic>\n                    via independent modes of action.\n                  <\/jats:p>","DOI":"10.1111\/j.1365-2958.2005.04503.x","type":"journal-article","created":{"date-parts":[[2005,3,2]],"date-time":"2005-03-02T13:23:30Z","timestamp":1109769810000},"page":"1782-1800","source":"Crossref","is-referenced-by-count":107,"title":["Characterization of\n                    <i>Cryptococcus neoformans<\/i>\n                    variety\n                    <i>gattii SOD2<\/i>\n                    reveals distinct roles of the two superoxide dismutases in fungal biology and virulence"],"prefix":"10.1111","volume":"55","author":[{"given":"Srinivas D.","family":"Narasipura","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Vishnu","family":"Chaturvedi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sudha","family":"Chaturvedi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2005,1,21]]},"reference":[{"key":"e_1_2_6_2_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.83.11.3820"},{"key":"e_1_2_6_3_1","doi-asserted-by":"publisher","DOI":"10.1128\/IAI.71.10.5794-5802.2003"},{"key":"e_1_2_6_4_1","doi-asserted-by":"publisher","DOI":"10.1101\/gad.11.23.3206"},{"key":"e_1_2_6_5_1","doi-asserted-by":"publisher","DOI":"10.1046\/j.1365-2958.2000.01852.x"},{"key":"e_1_2_6_6_1","doi-asserted-by":"publisher","DOI":"10.1128\/AAC.45.10.2939-2942.2001"},{"key":"e_1_2_6_7_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M408918200"},{"key":"e_1_2_6_8_1","doi-asserted-by":"publisher","DOI":"10.1128\/iai.60.4.1625-1632.1992"},{"key":"e_1_2_6_9_1","doi-asserted-by":"publisher","DOI":"10.1016\/0003-2697(71)90370-8"},{"key":"e_1_2_6_10_1","doi-asserted-by":"publisher","DOI":"10.1128\/IAI.69.1.108-114.2001"},{"key":"e_1_2_6_11_1","doi-asserted-by":"publisher","DOI":"10.1128\/MCB.14.7.4912"},{"key":"e_1_2_6_12_1","doi-asserted-by":"publisher","DOI":"10.1128\/IAI.64.6.1977-1983.1996"},{"key":"e_1_2_6_13_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0378-1119(01)00408-5"},{"key":"e_1_2_6_14_1","doi-asserted-by":"publisher","DOI":"10.1111\/j.1432-1033.1996.00779.x"},{"key":"e_1_2_6_15_1","doi-asserted-by":"publisher","DOI":"10.1099\/00221287-143-5-1649"},{"key":"e_1_2_6_16_1","doi-asserted-by":"publisher","DOI":"10.1128\/IAI.68.2.443-448.2000"},{"key":"e_1_2_6_17_1","doi-asserted-by":"publisher","DOI":"10.1046\/j.1365-2958.2001.02236.x"},{"key":"e_1_2_6_18_1","doi-asserted-by":"publisher","DOI":"10.1111\/j.1365-2958.2004.03921.x"},{"key":"e_1_2_6_19_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0021-9258(18)33617-2"},{"key":"e_1_2_6_20_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.93.10.5116"},{"key":"e_1_2_6_21_1","doi-asserted-by":"publisher","DOI":"10.1091\/mbc.01-12-0588"},{"key":"e_1_2_6_22_1","doi-asserted-by":"crossref","first-page":"2700","DOI":"10.1128\/iai.65.7.2700-2706.1997","article-title":"Role of bacterial Mn\u2010cofactored superoxide dismutase in oxidative stress responses, nasopharyngeal colonization, and sustained bacteremia caused by Haemophilus influenzae type b","volume":"65","author":"D\u2019Mello R.A.","year":"1997","journal-title":"Infect Immun"},{"key":"e_1_2_6_23_1","doi-asserted-by":"publisher","DOI":"10.1128\/MCB.21.9.3179-3191.2001"},{"key":"e_1_2_6_24_1","doi-asserted-by":"publisher","DOI":"10.1111\/j.1432-1033.1996.0648r.x"},{"key":"e_1_2_6_25_1","doi-asserted-by":"publisher","DOI":"10.1128\/IAI.71.9.5332-5343.2003"},{"key":"e_1_2_6_26_1","doi-asserted-by":"publisher","DOI":"10.1016\/B978-0-12-566505-6.50010-7"},{"key":"e_1_2_6_27_1","doi-asserted-by":"publisher","DOI":"10.1128\/EC.2.5.1036-1045.2003"},{"key":"e_1_2_6_28_1","doi-asserted-by":"publisher","DOI":"10.1146\/annurev.bi.64.070195.000525"},{"key":"e_1_2_6_29_1","doi-asserted-by":"publisher","DOI":"10.1091\/mbc.E03-11-0789"},{"key":"e_1_2_6_30_1","unstructured":"Fyfe M. 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