{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,18]],"date-time":"2026-01-18T14:17:18Z","timestamp":1768745838668,"version":"3.49.0"},"reference-count":46,"publisher":"American Society for Microbiology","issue":"9","license":[{"start":{"date-parts":[[2012,9,1]],"date-time":"2012-09-01T00:00:00Z","timestamp":1346457600000},"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":["Eukaryot Cell"],"published-print":{"date-parts":[[2012,9]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            We report the characterization of a bacterial-type oxygen reductase abundant in the cytoplasm of the anaerobic protozoan parasite\n            <jats:named-content content-type=\"genus-species\">Entamoeba histolytica<\/jats:named-content>\n            . Upon host infection,\n            <jats:named-content content-type=\"genus-species\">E. histolytica<\/jats:named-content>\n            is confronted with various oxygen tensions in the host intestine, as well as increased reactive oxygen and nitrogen species at the site of local tissue inflammation. Resistance to oxygen-derived stress thus plays an important role in the pathogenic potential of\n            <jats:named-content content-type=\"genus-species\">E. histolytica<\/jats:named-content>\n            . The genome of\n            <jats:named-content content-type=\"genus-species\">E. histolytica<\/jats:named-content>\n            has four genes that encode flavodiiron proteins, which are bacterial-type oxygen or nitric oxide reductases and were likely acquired by lateral gene transfer from prokaryotes. The\n            <jats:italic>EhFdp1<\/jats:italic>\n            gene has higher expression in virulent than in nonvirulent\n            <jats:named-content content-type=\"genus-species\">Entamoeba<\/jats:named-content>\n            strains and species, hinting that the response to oxidative stress may be one correlate of virulence potential. We demonstrate that EhFdp1 is abundantly expressed in the cytoplasm of\n            <jats:named-content content-type=\"genus-species\">E. histolytica<\/jats:named-content>\n            and that the protein levels are markedly increased (up to \u223c5-fold) upon oxygen exposure. Additionally, we produced fully functional recombinant EhFdp1 and demonstrated that this enzyme is a specific and robust oxygen reductase but has poor nitric oxide reductase activity. This observation represents a new mechanism of oxygen resistance in the anaerobic protozoan pathogen\n            <jats:named-content content-type=\"genus-species\">E. histolytica<\/jats:named-content>\n            .\n          <\/jats:p>","DOI":"10.1128\/ec.00149-12","type":"journal-article","created":{"date-parts":[[2012,7,14]],"date-time":"2012-07-14T10:13:49Z","timestamp":1342260829000},"page":"1112-1118","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":50,"title":["A Detoxifying Oxygen Reductase in the Anaerobic Protozoan Entamoeba histolytica"],"prefix":"10.1128","volume":"11","author":[{"given":"Jo\u00e3o B.","family":"Vicente","sequence":"first","affiliation":[{"name":"Departments of Internal Medicine and Microbiology and Immunology, Stanford University School of Medicine, Stanford, California, USA"},{"name":"Instituto de Tecnologia Qu\u00edmica e Biol\u00f3gica, Universidade Nova de Lisboa, Oeiras, Portugal"}]},{"given":"Vy","family":"Tran","sequence":"additional","affiliation":[{"name":"Departments of Internal Medicine and Microbiology and Immunology, Stanford University School of Medicine, Stanford, California, USA"}]},{"given":"Liliana","family":"Pinto","sequence":"additional","affiliation":[{"name":"Instituto de Tecnologia Qu\u00edmica e Biol\u00f3gica, Universidade Nova de Lisboa, Oeiras, Portugal"}]},{"given":"Miguel","family":"Teixeira","sequence":"additional","affiliation":[{"name":"Instituto de Tecnologia Qu\u00edmica e Biol\u00f3gica, Universidade Nova de Lisboa, Oeiras, Portugal"}]},{"given":"Upinder","family":"Singh","sequence":"additional","affiliation":[{"name":"Departments of Internal Medicine and Microbiology and Immunology, Stanford University School of Medicine, Stanford, California, USA"}]}],"member":"235","reference":[{"key":"e_1_3_3_2_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.molbiopara.2003.10.006"},{"key":"e_1_3_3_3_2","doi-asserted-by":"publisher","DOI":"10.1186\/1471-2164-8-7"},{"key":"e_1_3_3_4_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0960-9822(03)00003-4"},{"key":"e_1_3_3_5_2","doi-asserted-by":"publisher","DOI":"10.1186\/1471-2148-6-27"},{"key":"e_1_3_3_6_2","doi-asserted-by":"publisher","DOI":"10.1101\/gad.1667708"},{"key":"e_1_3_3_7_2","doi-asserted-by":"publisher","DOI":"10.1016\/0166-6851(95)00065-9"},{"key":"e_1_3_3_8_2","doi-asserted-by":"publisher","DOI":"10.1042\/bj3301217"},{"key":"e_1_3_3_9_2","doi-asserted-by":"publisher","DOI":"10.1128\/JB.183.5.1560-1567.2001"},{"key":"e_1_3_3_10_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1365-2958.2006.05344.x"},{"key":"e_1_3_3_11_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M705605200"},{"key":"e_1_3_3_12_2","doi-asserted-by":"publisher","DOI":"10.1186\/1471-2164-8-216"},{"key":"e_1_3_3_13_2","doi-asserted-by":"publisher","DOI":"10.1093\/clinchem\/10.1.21"},{"key":"e_1_3_3_14_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.molbiopara.2006.02.007"},{"key":"e_1_3_3_15_2","doi-asserted-by":"publisher","DOI":"10.1016\/0014-4894(80)90069-7"},{"key":"e_1_3_3_16_2","doi-asserted-by":"publisher","DOI":"10.1016\/0014-4894(81)90055-2"},{"key":"e_1_3_3_17_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.molbiopara.2007.11.014"},{"key":"e_1_3_3_18_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M110.106310"},{"key":"e_1_3_3_19_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1462-2920.2008.01823.x"},{"key":"e_1_3_3_20_2","doi-asserted-by":"publisher","DOI":"10.1039\/b710047g"},{"key":"e_1_3_3_21_2","doi-asserted-by":"publisher","DOI":"10.1007\/s00203-011-0687-8"},{"key":"e_1_3_3_22_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1462-2920.2008.01610.x"},{"key":"e_1_3_3_23_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1462-2920.2011.02439.x"},{"key":"e_1_3_3_24_2","doi-asserted-by":"publisher","DOI":"10.1038\/nature03291"},{"key":"e_1_3_3_25_2","doi-asserted-by":"publisher","DOI":"10.1128\/IAI.74.1.340-351.2006"},{"key":"e_1_3_3_26_2","doi-asserted-by":"publisher","DOI":"10.1002\/iub.409"},{"key":"e_1_3_3_27_2","doi-asserted-by":"publisher","DOI":"10.1016\/0166-6851(81)90038-4"},{"key":"e_1_3_3_28_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.str.2008.06.009"},{"key":"e_1_3_3_29_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.ijpara.2008.11.004"},{"key":"e_1_3_3_30_2","doi-asserted-by":"publisher","DOI":"10.1586\/14787210.5.5.893"},{"key":"e_1_3_3_31_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0065-2911(04)49002-X"},{"key":"e_1_3_3_32_2","first-page":"6492","article-title":"X-ray crystal structures of Moorella thermoacetica FprA","volume":"44","author":"Silaghi-Dumitrescu R","year":"2005","unstructured":"Silaghi-DumitrescuR KurtzDMJr LjungdahlLG LanzilottaWN. 2005. 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