{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,28]],"date-time":"2026-05-28T01:13:32Z","timestamp":1779930812999,"version":"3.53.1"},"reference-count":125,"publisher":"American Society for Microbiology","issue":"24","license":[{"start":{"date-parts":[[2015,12,15]],"date-time":"2015-12-15T00:00:00Z","timestamp":1450137600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["J Bacteriol"],"published-print":{"date-parts":[[2015,12,15]]},"abstract":"<jats:title>ABSTRACT<\/jats:title><jats:p>Bacterial pathogens<jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Neisseria meningitidis<\/jats:named-content>and<jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Brucella abortus<\/jats:named-content>pose threats to human and animal health worldwide, causing meningococcal disease and brucellosis, respectively. Mortality from acute<jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">N. meningitidis<\/jats:named-content>infections remains high despite antibiotics, and brucellosis presents alimentary and health consequences. Superoxide dismutases are master regulators of reactive oxygen and general pathogenicity factors and are therefore therapeutic targets. Cu,Zn superoxide dismutases (SODs) localized to the periplasm promote survival by detoxifying superoxide radicals generated by major host antimicrobial immune responses. We discovered that passive immunization with an antibody directed at<jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">N. meningitidis<\/jats:named-content>SOD (NmSOD) was protective in a mouse infection model. To define the relevant atomic details and solution assembly states of this important virulence factor, we report high-resolution and X-ray scattering analyses of NmSOD and of SOD from<jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">B. abortus<\/jats:named-content>(BaSOD). The NmSOD structures revealed an auxiliary tetrahedral Cu-binding site bridging the dimer interface; mutational analyses suggested that this metal site contributes to protein stability, with implications for bacterial defense mechanisms. Biochemical and structural analyses informed us about electrostatic substrate guidance, dimer assembly, and an exposed C-terminal epitope in the NmSOD dimer. In contrast, the monomeric BaSOD structure provided insights for extending immunogenic peptide epitopes derived from the protein. These collective results reveal unique contributions of SOD to pathogenic virulence, refine predictive motifs for distinguishing SOD classes, and suggest general targets for antibacterial immune responses. The identified functional contributions, motifs, and targets distinguishing bacterial and eukaryotic SOD assemblies presented here provide a foundation for efforts to develop SOD-specific inhibitors of or vaccines against these harmful pathogens.<\/jats:p><jats:p><jats:bold>IMPORTANCE<\/jats:bold>By protecting microbes against reactive oxygen insults, SODs aid survival of many bacteria within their hosts. Despite the ubiquity and conservation of these key enzymes, notable species-specific differences relevant to pathogenesis remain undefined. To probe mechanisms that govern the functioning of<jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Neisseria meningitidis<\/jats:named-content>and<jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Brucella abortus<\/jats:named-content>SODs, we used X-ray structures, enzymology, modeling, and murine infection experiments. We identified virulence determinants common to the two homologs, assembly differences, and a unique metal reservoir within meningococcal SOD that stabilizes the enzyme and may provide a safeguard against copper toxicity. The insights reported here provide a rationale and a basis for SOD-specific drug design and an extension of immunogen design to target two important pathogens that continue to pose global health threats.<\/jats:p>","DOI":"10.1128\/jb.00343-15","type":"journal-article","created":{"date-parts":[[2015,10,13]],"date-time":"2015-10-13T18:54:43Z","timestamp":1444762483000},"page":"3834-3847","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":20,"title":["Structural, Functional, and Immunogenic Insights on Cu,Zn Superoxide Dismutase Pathogenic Virulence Factors from Neisseria meningitidis and Brucella abortus"],"prefix":"10.1128","volume":"197","author":[{"given":"Ashley J.","family":"Pratt","sequence":"first","affiliation":[{"name":"Department of Integrative Structural and Computational Biology and The Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, California, USA"},{"name":"Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, California, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Michael","family":"DiDonato","sequence":"additional","affiliation":[{"name":"Department of Integrative Structural and Computational Biology and The Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, California, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"David S.","family":"Shin","sequence":"additional","affiliation":[{"name":"Department of Integrative Structural and Computational Biology and The Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, California, USA"},{"name":"Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, California, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Diane E.","family":"Cabelli","sequence":"additional","affiliation":[{"name":"Chemistry Department, Brookhaven National Laboratory, Upton, New York, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Cami K.","family":"Bruns","sequence":"additional","affiliation":[{"name":"Department of Integrative Structural and Computational Biology and The Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, California, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Carol A.","family":"Belzer","sequence":"additional","affiliation":[{"name":"National Animal Disease Center, Ruminant Diseases and Immunology, Ames, Iowa, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Andrew R.","family":"Gorringe","sequence":"additional","affiliation":[{"name":"Public Health England, Porton Down, Salisbury, United Kingdom"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Paul R.","family":"Langford","sequence":"additional","affiliation":[{"name":"Section of Paediatrics, Department of Medicine, Imperial College London, St. Mary's Campus, London, England, United Kingdom"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Louisa B.","family":"Tabatabai","sequence":"additional","affiliation":[{"name":"National Animal Disease Center, Ruminant Diseases and Immunology, Ames, Iowa, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"J. Simon","family":"Kroll","sequence":"additional","affiliation":[{"name":"Section of Paediatrics, Department of Medicine, Imperial College London, St. Mary's Campus, London, England, United Kingdom"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"John A.","family":"Tainer","sequence":"additional","affiliation":[{"name":"Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, California, USA"},{"name":"Department of Molecular and Cellular Oncology, The University of Texas M. D. Anderson Cancer Center, Houston, Texas, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Elizabeth D.","family":"Getzoff","sequence":"additional","affiliation":[{"name":"Department of Integrative Structural and Computational Biology and The Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, California, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_3_2_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.neuroscience.2006.10.045"},{"key":"e_1_3_3_3_2","doi-asserted-by":"publisher","DOI":"10.1126\/scitranslmed.3006567"},{"key":"e_1_3_3_4_2","doi-asserted-by":"publisher","DOI":"10.1038\/nrmicro3032"},{"key":"e_1_3_3_5_2","doi-asserted-by":"publisher","DOI":"10.1038\/nchembio.85"},{"key":"e_1_3_3_6_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.molcel.2012.09.025"},{"key":"e_1_3_3_7_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M112.395079"},{"key":"e_1_3_3_8_2","doi-asserted-by":"publisher","DOI":"10.1038\/nrmicro1022"},{"key":"e_1_3_3_9_2","doi-asserted-by":"publisher","DOI":"10.1093\/jb\/mvj023"},{"key":"e_1_3_3_10_2","first-page":"61","article-title":"Superoxide dismutases","volume":"58","author":"Fridovich I","year":"1986","unstructured":"Fridovich I. 1986. Superoxide dismutases. Adv Enzymol Relat Areas Mol Biol 58:61\u201397.","journal-title":"Adv Enzymol Relat Areas Mol Biol"},{"key":"e_1_3_3_11_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.bbapap.2009.11.004"},{"key":"e_1_3_3_12_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.jmb.2008.11.031"},{"key":"e_1_3_3_13_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.89.13.6109"},{"key":"e_1_3_3_14_2","doi-asserted-by":"publisher","DOI":"10.1016\/0022-2836(82)90174-7"},{"key":"e_1_3_3_15_2","doi-asserted-by":"crossref","first-page":"2271","DOI":"10.1099\/13500872-141-9-2271","article-title":"Bacterial [Cu,Zn]-superoxide dismutase: phylogenetically distinct from the eukaryotic enzyme, and not so rare after all!","volume":"141","author":"Kroll JS","year":"1995","unstructured":"Kroll JS, Langford PR, Wilks KE, Keil AD. 1995. Bacterial [Cu,Zn]-superoxide dismutase: phylogenetically distinct from the eukaryotic enzyme, and not so rare after all! Microbiology 141:2271\u20132279.","journal-title":"Microbiology"},{"key":"e_1_3_3_16_2","doi-asserted-by":"publisher","DOI":"10.1128\/jb.178.9.2564-2571.1996"},{"key":"e_1_3_3_17_2","doi-asserted-by":"publisher","DOI":"10.1021\/bi00454a010"},{"key":"e_1_3_3_18_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.jmb.2009.03.026"},{"key":"e_1_3_3_19_2","doi-asserted-by":"publisher","DOI":"10.1038\/358347a0"},{"key":"e_1_3_3_20_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.93.23.12774"},{"key":"e_1_3_3_21_2","doi-asserted-by":"publisher","DOI":"10.1002\/prot.340190105"},{"key":"e_1_3_3_22_2","doi-asserted-by":"publisher","DOI":"10.1038\/306287a0"},{"key":"e_1_3_3_23_2","doi-asserted-by":"publisher","DOI":"10.1038\/306284a0"},{"key":"e_1_3_3_24_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1574-6976.2006.00051.x"},{"key":"e_1_3_3_25_2","doi-asserted-by":"publisher","DOI":"10.3389\/fcimb.2012.00130"},{"key":"e_1_3_3_26_2","doi-asserted-by":"publisher","DOI":"10.1038\/nrmicro2295"},{"key":"e_1_3_3_27_2","doi-asserted-by":"publisher","DOI":"10.1007\/978-1-61779-346-2_1"},{"key":"e_1_3_3_28_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.vaccine.2009.04.061"},{"key":"e_1_3_3_29_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.vaccine.2011.12.032"},{"key":"e_1_3_3_30_2","doi-asserted-by":"publisher","DOI":"10.1517\/14656566.2015.973851"},{"key":"e_1_3_3_31_2","doi-asserted-by":"publisher","DOI":"10.1016\/S1473-3099(06)70382-6"},{"key":"e_1_3_3_32_2","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pntd.0001929"},{"key":"e_1_3_3_33_2","doi-asserted-by":"publisher","DOI":"10.1016\/S1473-3099(13)70341-4"},{"key":"e_1_3_3_34_2","doi-asserted-by":"publisher","DOI":"10.1155\/2013\/743509"},{"key":"e_1_3_3_35_2","doi-asserted-by":"crossref","first-page":"60","DOI":"10.1007\/s11515-012-1196-0","article-title":"Progress in Brucella vaccine development","volume":"8","author":"Yang X","year":"2013","unstructured":"Yang X, Skyberg JA, Cao L, Clapp B, Thornburg T, Pascual DW. 2013. Progress in Brucella vaccine development. Front Biol (Beijing) 8:60\u201377.","journal-title":"Front Biol (Beijing)"},{"key":"e_1_3_3_36_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1574-6976.2010.00211.x"},{"key":"e_1_3_3_37_2","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0004975"},{"key":"e_1_3_3_38_2","doi-asserted-by":"publisher","DOI":"10.1128\/JB.00554-06"},{"key":"e_1_3_3_39_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1365-2958.2011.07612.x"},{"key":"e_1_3_3_40_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.micinf.2005.01.005"},{"key":"e_1_3_3_41_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.94.25.13997"},{"key":"e_1_3_3_42_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.96.13.7502"},{"key":"e_1_3_3_43_2","doi-asserted-by":"publisher","DOI":"10.1128\/JB.00534-09"},{"key":"e_1_3_3_44_2","doi-asserted-by":"publisher","DOI":"10.1128\/IAI.68.8.4778-4781.2000"},{"key":"e_1_3_3_45_2","doi-asserted-by":"publisher","DOI":"10.1128\/IAI.66.1.213-217.1998"},{"key":"e_1_3_3_46_2","doi-asserted-by":"publisher","DOI":"10.1128\/IAI.71.3.1604-1607.2003"},{"key":"e_1_3_3_47_2","doi-asserted-by":"publisher","DOI":"10.1128\/IAI.73.5.2873-2880.2005"},{"key":"e_1_3_3_48_2","doi-asserted-by":"publisher","DOI":"10.1128\/iai.60.7.2863-2869.1992"},{"key":"e_1_3_3_49_2","doi-asserted-by":"publisher","DOI":"10.1016\/0264-410X(94)90035-3"},{"key":"e_1_3_3_50_2","doi-asserted-by":"publisher","DOI":"10.1128\/JCM.01376-06"},{"key":"e_1_3_3_51_2","doi-asserted-by":"publisher","DOI":"10.1017\/S0033583507004635"},{"key":"e_1_3_3_52_2","doi-asserted-by":"crossref","first-page":"14697","DOI":"10.1016\/S0021-9258(18)47851-9","article-title":"Human copper-zinc superoxide dismutase complements superoxide dismutase-deficient Escherichia coli mutants","volume":"262","author":"Natvig DO","year":"1987","unstructured":"Natvig DO, Imlay K, Touati D, Hallewell RA. 1987. Human copper-zinc superoxide dismutase complements superoxide dismutase-deficient Escherichia coli mutants. J Biol Chem 262:14697\u201314701.","journal-title":"J Biol Chem"},{"key":"e_1_3_3_53_2","doi-asserted-by":"publisher","DOI":"10.1093\/emboj\/16.9.2171"},{"key":"e_1_3_3_54_2","doi-asserted-by":"publisher","DOI":"10.1021\/bi00038a022"},{"key":"e_1_3_3_55_2","doi-asserted-by":"publisher","DOI":"10.1128\/iai.58.9.2935-2939.1990"},{"key":"e_1_3_3_56_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.1308531111"},{"key":"e_1_3_3_57_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0022-2836(03)00889-1"},{"key":"e_1_3_3_58_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0076-6879(84)05013-8"},{"key":"e_1_3_3_59_2","doi-asserted-by":"publisher","DOI":"10.1107\/S0108767393007597"},{"key":"e_1_3_3_60_2","doi-asserted-by":"crossref","first-page":"905","DOI":"10.1107\/S0907444998003254","article-title":"Crystallography & NMR system: a new software suite for macromolecular structure determination","volume":"54","author":"Br\u00fcnger AT","year":"1998","unstructured":"Br\u00fcnger AT, Adams PD, Clore GM, DeLano WL, Gros P, Grosse-Kunstleve RW, Jiang J-S, Kuszewski J, Nilges M, Pannu NS, Read RJ, Rice LM, Simonson T, Warren GL. 1998. Crystallography & NMR system: a new software suite for macromolecular structure determination. Acta Crystallogr D Biol Crystallogr 54:905\u2013921.","journal-title":"Acta Crystallogr D Biol Crystallogr"},{"key":"e_1_3_3_61_2","doi-asserted-by":"publisher","DOI":"10.1006\/jsbi.1999.4094"},{"key":"e_1_3_3_62_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0076-6879(97)77018-6"},{"key":"e_1_3_3_63_2","doi-asserted-by":"publisher","DOI":"10.1107\/S0907444909052925"},{"key":"e_1_3_3_64_2","doi-asserted-by":"publisher","DOI":"10.1107\/S0021889812048698"},{"key":"e_1_3_3_65_2","doi-asserted-by":"publisher","DOI":"10.1107\/S0021889803012779"},{"key":"e_1_3_3_66_2","doi-asserted-by":"publisher","DOI":"10.1107\/S002188989100081X"},{"key":"e_1_3_3_67_2","doi-asserted-by":"publisher","DOI":"10.1107\/S0021889809000338"},{"key":"e_1_3_3_68_2","doi-asserted-by":"publisher","DOI":"10.1107\/S0021889803000268"},{"key":"e_1_3_3_69_2","doi-asserted-by":"publisher","DOI":"10.1093\/nar\/gkq461"},{"key":"e_1_3_3_70_2","doi-asserted-by":"publisher","DOI":"10.1002\/jcc.20084"},{"key":"e_1_3_3_71_2","doi-asserted-by":"publisher","DOI":"10.1093\/nar\/gkh368"},{"key":"e_1_3_3_72_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M010527200"},{"key":"e_1_3_3_73_2","first-page":"574","article-title":"Updated recommendations for use of VariZIG\u2014United States, 2013","volume":"62","author":"Centers for Disease Control and Prevention (CDC)","year":"2013","unstructured":"Centers for Disease Control and Prevention (CDC). 2013. Updated recommendations for use of VariZIG\u2014United States, 2013. MMWR Morb Mortal Wkly Rep 62:574\u2013576.","journal-title":"MMWR Morb Mortal Wkly Rep"},{"key":"e_1_3_3_74_2","doi-asserted-by":"publisher","DOI":"10.2174\/1871526515666150320161630"},{"key":"e_1_3_3_75_2","doi-asserted-by":"publisher","DOI":"10.1006\/jmbi.1999.3448"},{"key":"e_1_3_3_76_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.jmb.2008.12.004"},{"key":"e_1_3_3_77_2","doi-asserted-by":"publisher","DOI":"10.1006\/jmbi.1998.2267"},{"key":"e_1_3_3_78_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0022-2836(03)00047-0"},{"key":"e_1_3_3_79_2","doi-asserted-by":"publisher","DOI":"10.1006\/jmbi.2000.4074"},{"key":"e_1_3_3_80_2","doi-asserted-by":"publisher","DOI":"10.1038\/nmeth.2453"},{"key":"e_1_3_3_81_2","doi-asserted-by":"publisher","DOI":"10.1038\/nature12070"},{"key":"e_1_3_3_82_2","doi-asserted-by":"publisher","DOI":"10.1002\/bip.21638"},{"key":"e_1_3_3_83_2","doi-asserted-by":"publisher","DOI":"10.1021\/bi951930b"},{"key":"e_1_3_3_84_2","doi-asserted-by":"publisher","DOI":"10.1006\/bbrc.1998.8364"},{"key":"e_1_3_3_85_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M010488200"},{"key":"e_1_3_3_86_2","volume-title":"A study of enzymes II","author":"Tainer JA","year":"1991","unstructured":"Tainer JA, Roberts VA, Fisher CL, Hallewell RA, Getzoff ED. 1991. Mechanism and structure of superoxide dismutases. In Kuby SA (ed), A study of enzymes II. Mechanism of enzyme action. CRC, Boca Raton, FL."},{"key":"e_1_3_3_87_2","doi-asserted-by":"publisher","DOI":"10.1006\/jmbi.1997.1400"},{"key":"e_1_3_3_88_2","doi-asserted-by":"publisher","DOI":"10.1021\/bi801252e"},{"key":"e_1_3_3_89_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.0502450102"},{"key":"e_1_3_3_90_2","doi-asserted-by":"crossref","first-page":"5260","DOI":"10.1016\/S0021-9258(18)83727-9","article-title":"Genetically engineered polymers of human Cu,Zn superoxide-dismutase\u2014biochemistry and serum half-lives","volume":"264","author":"Hallewell RA","year":"1989","unstructured":"Hallewell RA, Laria I, Tabrizi A, Carlin G, Getzoff ED, Tainer JA, Cousens LS, Mullenbach GT. 1989. Genetically engineered polymers of human Cu,Zn superoxide-dismutase\u2014biochemistry and serum half-lives. J Biol Chem 264:5260\u20135268.","journal-title":"J Biol Chem"},{"key":"e_1_3_3_91_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M404699200"},{"key":"e_1_3_3_92_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.1400137111"},{"key":"e_1_3_3_93_2","doi-asserted-by":"publisher","DOI":"10.1038\/nsb935"},{"key":"e_1_3_3_94_2","doi-asserted-by":"publisher","DOI":"10.1146\/annurev-biophys-083012-130301"},{"key":"e_1_3_3_95_2","doi-asserted-by":"publisher","DOI":"10.1038\/nmeth.1353"},{"key":"e_1_3_3_96_2","doi-asserted-by":"crossref","first-page":"14234","DOI":"10.1016\/S0021-9258(18)77291-8","article-title":"Changes in crystallographic structure and thermostability of a Cu,Zn superoxide dismutase mutant resulting from the removal of a buried cysteine","volume":"265","author":"McRee DE","year":"1990","unstructured":"McRee DE, Redford SM, Getzoff ED, Lepock JR, Hallewell RA, Tainer JA. 1990. Changes in crystallographic structure and thermostability of a Cu,Zn superoxide dismutase mutant resulting from the removal of a buried cysteine. J Biol Chem 265:14234\u201314241.","journal-title":"J Biol Chem"},{"key":"e_1_3_3_97_2","doi-asserted-by":"publisher","DOI":"10.1089\/ars.2010.3187"},{"key":"e_1_3_3_98_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.0804621105"},{"key":"e_1_3_3_99_2","doi-asserted-by":"publisher","DOI":"10.1002\/prot.340050408"},{"key":"e_1_3_3_100_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1365-2958.2011.07884.x"},{"key":"e_1_3_3_101_2","doi-asserted-by":"publisher","DOI":"10.1128\/JVI.02031-14"},{"key":"e_1_3_3_102_2","doi-asserted-by":"publisher","DOI":"10.1128\/JVI.02588-14"},{"key":"e_1_3_3_103_2","doi-asserted-by":"publisher","DOI":"10.1093\/protein\/2.3.239"},{"key":"e_1_3_3_104_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.0912491107"},{"key":"e_1_3_3_105_2","doi-asserted-by":"publisher","DOI":"10.1371\/journal.ppat.1002887"},{"key":"e_1_3_3_106_2","doi-asserted-by":"publisher","DOI":"10.1016\/S1386-1425(01)00713-2"},{"key":"e_1_3_3_107_2","doi-asserted-by":"publisher","DOI":"10.1021\/bi050925x"},{"key":"e_1_3_3_108_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.jinorgbio.2011.09.029"},{"key":"e_1_3_3_109_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M800591200"},{"key":"e_1_3_3_110_2","doi-asserted-by":"publisher","DOI":"10.1038\/nature09265"},{"key":"e_1_3_3_111_2","doi-asserted-by":"publisher","DOI":"10.1080\/07391102.2012.680028"},{"key":"e_1_3_3_112_2","doi-asserted-by":"publisher","DOI":"10.1006\/jmbi.2001.4606"},{"key":"e_1_3_3_113_2","doi-asserted-by":"publisher","DOI":"10.1586\/14760584.2015.1016915"},{"key":"e_1_3_3_114_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.vaccine.2004.02.041"},{"key":"e_1_3_3_115_2","doi-asserted-by":"publisher","DOI":"10.2174\/1574891X11308010006"},{"key":"e_1_3_3_116_2","doi-asserted-by":"crossref","first-page":"1591","DOI":"10.2460\/ajvr.1993.54.10.1591","article-title":"Immune responses and protection against infection and abortion in cattle experimentally vaccinated with mutant strains of Brucella abortus","volume":"54","author":"Cheville NF","year":"1993","unstructured":"Cheville NF, Stevens MG, Jensen AE, Tatum FM, Halling SM. 1993. Immune responses and protection against infection and abortion in cattle experimentally vaccinated with mutant strains of Brucella abortus. Am J Vet Res 54:1591\u20131597.","journal-title":"Am J Vet Res"},{"key":"e_1_3_3_117_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.vaccine.2011.12.088"},{"key":"e_1_3_3_118_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.vaccine.2011.02.054"},{"key":"e_1_3_3_119_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.vaccine.2011.04.088"},{"key":"e_1_3_3_120_2","doi-asserted-by":"publisher","DOI":"10.1128\/CVI.00554-14"},{"key":"e_1_3_3_121_2","doi-asserted-by":"publisher","DOI":"10.1038\/312127a0"},{"key":"e_1_3_3_122_2","doi-asserted-by":"publisher","DOI":"10.1128\/iai.64.2.644-652.1996"},{"key":"e_1_3_3_123_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0065-2776(08)60363-6"},{"key":"e_1_3_3_124_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0140-6736(12)61186-6"},{"key":"e_1_3_3_125_2","doi-asserted-by":"publisher","DOI":"10.1128\/CMR.00059-12"},{"key":"e_1_3_3_126_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.C113.526475"}],"container-title":["Journal of Bacteriology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/journals.asm.org\/doi\/pdf\/10.1128\/JB.00343-15","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/journals.asm.org\/doi\/pdf\/10.1128\/JB.00343-15","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2024,6,11]],"date-time":"2024-06-11T19:29:17Z","timestamp":1718134157000},"score":1,"resource":{"primary":{"URL":"https:\/\/journals.asm.org\/doi\/10.1128\/JB.00343-15"}},"subtitle":[],"editor":[{"given":"A. M.","family":"Stock","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"editor"}]}],"short-title":[],"issued":{"date-parts":[[2015,12,15]]},"references-count":125,"journal-issue":{"issue":"24","published-print":{"date-parts":[[2015,12,15]]}},"alternative-id":["10.1128\/JB.00343-15"],"URL":"https:\/\/doi.org\/10.1128\/jb.00343-15","relation":{},"ISSN":["0021-9193","1098-5530"],"issn-type":[{"value":"0021-9193","type":"print"},{"value":"1098-5530","type":"electronic"}],"subject":[],"published":{"date-parts":[[2015,12,15]]},"assertion":[{"value":"2015-06-24","order":0,"name":"received","label":"Received","group":{"name":"publication_history","label":"Publication History"}},{"value":"2015-09-29","order":1,"name":"accepted","label":"Accepted","group":{"name":"publication_history","label":"Publication History"}},{"value":"2015-11-18","order":2,"name":"published","label":"Published","group":{"name":"publication_history","label":"Publication History"}}]}}