{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,7]],"date-time":"2026-10-07T03:25:20Z","timestamp":1791343520669,"version":"4.3.1"},"reference-count":38,"publisher":"Springer Science and Business Media LLC","issue":"1","content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["BMC Microbiol"],"published-print":{"date-parts":[[2007,12]]},"abstract":"<jats:title>Abstract<\/jats:title>\n          <jats:sec>\n            <jats:title>Background<\/jats:title>\n            <jats:p>In prokaryotes, the ureases are multi-subunit, nickel-containing enzymes that catalyze the hydrolysis of urea to carbon dioxide and ammonia. The <jats:italic>Brucella<\/jats:italic> genomes contain two urease operons designated as <jats:italic>ure<\/jats:italic> 1 and <jats:italic>ure<\/jats:italic> 2. We investigated the role of the two <jats:italic>Brucella suis<\/jats:italic> urease operons on the infection, intracellular persistence, growth, and resistance to low-pH killing.<\/jats:p>\n          <\/jats:sec>\n          <jats:sec>\n            <jats:title>Results<\/jats:title>\n            <jats:p>The deduced amino acid sequence of urease-\u03b1 subunits of operons-1 and -2 exhibited substantial identity with the structural ureases of alpha- and beta-proteobacteria, Gram-positive and Gram-negative bacteria, fungi, and higher plants. Four <jats:italic>ure<\/jats:italic> deficient strains were generated by deleting one or more of the genes encoding urease subunits of <jats:italic>B. suis<\/jats:italic> strain 1330 by allelic exchange: strain 1330\u0394<jats:italic>ure<\/jats:italic> 1K (generated by deleting <jats:italic>ureD<\/jats:italic> and <jats:italic>ureA<\/jats:italic> in <jats:italic>ure<\/jats:italic> 1 operon), strain 1330\u0394<jats:italic>ure<\/jats:italic> 2K (<jats:italic>ureB<\/jats:italic> and <jats:italic>ureC<\/jats:italic> in <jats:italic>ure<\/jats:italic> 2 operon), strain 1330\u0394<jats:italic>ure<\/jats:italic> 2C (<jats:italic>ureA<\/jats:italic>, <jats:italic>ureB<\/jats:italic>, and <jats:italic>ureC<\/jats:italic> in <jats:italic>ure<\/jats:italic> 2 operon), and strain 1330\u0394<jats:italic>ure<\/jats:italic> 1K\u0394<jats:italic>ure<\/jats:italic> 2C (<jats:italic>ureD<\/jats:italic> and <jats:italic>ureA<\/jats:italic> in <jats:italic>ure<\/jats:italic> 1 operon and <jats:italic>ureA<\/jats:italic>, <jats:italic>ureB<\/jats:italic>, and <jats:italic>ureC<\/jats:italic> in <jats:italic>ure<\/jats:italic> 2 operon). When grown in urease test broth, strains 1330, 1330\u0394<jats:italic>ure<\/jats:italic> 2K and 1330\u0394<jats:italic>ure<\/jats:italic> 2C displayed maximal urease enzyme activity within 24 hours, whereas, strains 1330\u0394<jats:italic>ure<\/jats:italic> 1K and 1330\u0394<jats:italic>ure<\/jats:italic> 1K\u0394<jats:italic>ure<\/jats:italic> 2C exhibited zero urease activity even 96 h after inoculation. Strains 1330\u0394<jats:italic>ure<\/jats:italic> 1K and 1330\u0394<jats:italic>ure<\/jats:italic> 1K\u0394<jats:italic>ure<\/jats:italic> 2C exhibited slower growth rates in tryptic soy broth relative to the wild type strain 1330. When the BALB\/c mice were infected intraperitoneally with the strains, six weeks after inoculation, the splenic recovery of the <jats:italic>ure<\/jats:italic> deficient strains did not differ from the wild type. In contrast, when the mice were inoculated by gavage, one week after inoculation, strain 1330\u0394<jats:italic>ure<\/jats:italic> 1K\u0394<jats:italic>ure<\/jats:italic> 2C was cleared from livers and spleens while the wild type strain 1330 was still present. All <jats:italic>B. suis<\/jats:italic> strains were killed when they were incubated <jats:italic>in-vitro<\/jats:italic> at pH 2.0. When the strains were incubated at pH 2.0 supplemented with 10 mM urea, strain 1330\u0394<jats:italic>ure<\/jats:italic> 1K was completely killed, strain 1330\u0394<jats:italic>ure<\/jats:italic> 2C was partially killed, but strains 1330 and 1330\u0394<jats:italic>ure<\/jats:italic> 2K were not killed.<\/jats:p>\n          <\/jats:sec>\n          <jats:sec>\n            <jats:title>Conclusion<\/jats:title>\n            <jats:p>These findings suggest that the <jats:italic>ure<\/jats:italic> 1 operon is necessary for optimal growth in culture, urease activity, resistance against low-pH killing, and <jats:italic>in vivo<\/jats:italic> persistence of <jats:italic>B. suis<\/jats:italic> when inoculated by gavage. The <jats:italic>ure<\/jats:italic> 2 operon apparently enhances the resistance to low-pH killing <jats:italic>in-vitro<\/jats:italic>.<\/jats:p>\n          <\/jats:sec>","DOI":"10.1186\/1471-2180-7-57","type":"journal-article","created":{"date-parts":[[2007,6,19]],"date-time":"2007-06-19T18:13:41Z","timestamp":1182276821000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":70,"title":["Brucella suis urease encoded by ure 1 but not ure 2 is necessary for intestinal infection of BALB\/c mice"],"prefix":"10.1186","volume":"7","author":[{"given":"Aloka B","family":"Bandara","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Andrea","family":"Contreras","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Araceli","family":"Contreras-Rodriguez","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ana M","family":"Martins","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Victor","family":"Dobrean","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sherry","family":"Poff-Reichow","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Parthiban","family":"Rajasekaran","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nammalwar","family":"Sriranganathan","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gerhardt G","family":"Schurig","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Stephen M","family":"Boyle","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2007,6,19]]},"reference":[{"key":"374_CR1","doi-asserted-by":"publisher","first-page":"907","DOI":"10.1111\/j.1365-2958.1993.tb01220.x","volume":"9","author":"CM Collins","year":"1993","unstructured":"Collins CM, D'Orazio SEF: Bacterial ureases: structure, regulation of expression and role in pathogenesis [Review]. 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