{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,11,11]],"date-time":"2025-11-11T13:26:17Z","timestamp":1762867577520},"reference-count":32,"publisher":"American Society for Microbiology","issue":"7","license":[{"start":{"date-parts":[[1998,7,1]],"date-time":"1998-07-01T00:00:00Z","timestamp":899251200000},"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":["Antimicrob Agents Chemother"],"published-print":{"date-parts":[[1998,7]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            Ceftazidime-resistant\n            <jats:italic>Escherichia coli<\/jats:italic>\n            and\n            <jats:italic>Klebsiella pneumoniae<\/jats:italic>\n            (49 and 102 isolates, respectively) were collected from Barnes-Jewish Hospital, St. Louis, Mo., from 1992 to 1996. They were uniformly resistant to ceftazidime, generally resistant to aztreonam, and variably susceptible to cefotaxime. Four representative\n            <jats:italic>E. coli<\/jats:italic>\n            strains and 15\n            <jats:italic>Klebsiella<\/jats:italic>\n            strains were examined. From one to four \u03b2-lactamases were produced per strain, with three possible enzymes related to ceftazidime resistance: enzymes with pI values of 5.6, 6.1, or 7.6. By pulsed-field gel electrophoresis there were at least 13 different\n            <jats:italic>Klebsiella<\/jats:italic>\n            strain types and 3 different\n            <jats:italic>E. coli<\/jats:italic>\n            strain types, indicating that the outbreak was not clonal. After cloning and sequencing of the \u03b2-lactamase-encoding genes, the enzyme with a pI of 5.6 was identified as TEM-10. The enzyme with a pI of 6.1 was a novel TEM variant (TEM-43) with Lys at 104, His at 164, and Thr at 182. TEM-43 showed broad-spectrum hydrolytic activity against all penicillins, with the highest hydrolysis rate for ceftazidime compared to those for the other expanded-spectrum cephalosporins. Aztreonam was also a good substrate for TEM-43, with hydrolytic activity similar to that of ceftazidime and affinity higher than that of ceftazidime. The TEM-43 \u03b2-lactamase was well inhibited by clavulanic acid and tazobactam at concentrations of &lt;10 nM. Sulbactam was less effective than the other inhibitors. The Thr182 mutation previously reported in an inhibitor-resistant \u03b2-lactamase did not cause the TEM-43 enzyme to become resistant to any of the inhibitors.\n          <\/jats:p>","DOI":"10.1128\/aac.42.7.1671","type":"journal-article","created":{"date-parts":[[2018,10,9]],"date-time":"2018-10-09T00:33:03Z","timestamp":1539045183000},"page":"1671-1676","update-policy":"http:\/\/dx.doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":37,"title":["Ceftazidime-Resistant\n            <i>Klebsiella pneumoniae<\/i>\n            and\n            <i>Escherichia coli<\/i>\n            Isolates Producing TEM-10 and TEM-43 \u03b2-Lactamases from St. Louis, Missouri"],"prefix":"10.1128","volume":"42","author":[{"given":"Youjun","family":"Yang","sequence":"first","affiliation":[{"name":"<!--label omitted: 1-->Wyeth-Ayerst Research, Pearl River, New York,1 and"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Niraja","family":"Bhachech","sequence":"additional","affiliation":[{"name":"<!--label omitted: 1-->Wyeth-Ayerst Research, Pearl River, New York,1 and"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Patricia A.","family":"Bradford","sequence":"additional","affiliation":[{"name":"<!--label omitted: 1-->Wyeth-Ayerst Research, Pearl River, New York,1 and"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Bradley D.","family":"Jett","sequence":"additional","affiliation":[{"name":"<!--label omitted: 2-->Barnes-Jewish Hospital, Washington University School of Medicine, St. Louis, Missouri2"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Daniel F.","family":"Sahm","sequence":"additional","affiliation":[{"name":"<!--label omitted: 2-->Barnes-Jewish Hospital, Washington University School of Medicine, St. Louis, Missouri2"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Karen","family":"Bush","sequence":"additional","affiliation":[{"name":"<!--label omitted: 1-->Wyeth-Ayerst Research, Pearl River, New York,1 and"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"publisher","DOI":"10.1093\/nar\/7.6.1513"},{"key":"e_1_3_2_3_2","doi-asserted-by":"publisher","DOI":"10.1128\/AAC.37.10.2059"},{"key":"e_1_3_2_4_2","doi-asserted-by":"publisher","DOI":"10.1128\/AAC.38.4.761"},{"key":"e_1_3_2_5_2","doi-asserted-by":"publisher","DOI":"10.1128\/AAC.39.4.899"},{"key":"e_1_3_2_6_2","doi-asserted-by":"publisher","DOI":"10.1128\/AAC.40.1.260"},{"key":"e_1_3_2_7_2","doi-asserted-by":"publisher","DOI":"10.1128\/AAC.39.6.1211"},{"key":"e_1_3_2_8_2","doi-asserted-by":"publisher","DOI":"10.1128\/AAC.40.10.2434"},{"key":"e_1_3_2_9_2","doi-asserted-by":"publisher","DOI":"10.1128\/AAC.39.2.427"},{"key":"e_1_3_2_10_2","doi-asserted-by":"crossref","first-page":"8801","DOI":"10.1073\/pnas.94.16.8801","article-title":"A natural polymorphism in \u03b2-lactamase is a global suppressor.","volume":"94","author":"Huang W.","year":"1997","unstructured":"Huang W. Palzkill T. A natural polymorphism in \u03b2-lactamase is a global suppressor. Proc. Natl. Acad. Sci. USA 94 1997 8801 8806","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"e_1_3_2_11_2","doi-asserted-by":"publisher","DOI":"10.1128\/AAC.35.9.1697"},{"key":"e_1_3_2_12_2","doi-asserted-by":"publisher","DOI":"10.1128\/AAC.39.5.1187"},{"key":"e_1_3_2_13_2","doi-asserted-by":"publisher","DOI":"10.1128\/AAC.39.12.2593"},{"key":"e_1_3_2_14_2","doi-asserted-by":"publisher","DOI":"10.1093\/jac\/38.3.409"},{"key":"e_1_3_2_15_2","doi-asserted-by":"publisher","DOI":"10.1128\/AAC.34.11.2210"},{"key":"e_1_3_2_16_2","unstructured":"Maslow\n              J. N.\n              Slutshy\n              A. M.\n              Arbeit\n              R. D.\n          Application of pulsed-field gel electrophoresis to molecular epidemiology\n          Diagnostic molecular microbiology principles and applications.\n              Persing\n              D. H.\n              Smith\n              T. F.\n              Tenover\n              F. C.\n              White\n              T. J.\n          1993\n          563\n          572\n          American Society for Microbiology\n          Washington D.C"},{"key":"e_1_3_2_17_2","doi-asserted-by":"publisher","DOI":"10.1099\/00221287-88-1-169"},{"key":"e_1_3_2_18_2","unstructured":"National Committee for Clinical Laboratory Standards\n          Performance standards for antimicrobial disk susceptibility tests. Approved standard M2-A4.\n          1997\n          National Committee for Clinical Laboratory Standards\n          Wayne Pa"},{"key":"e_1_3_2_19_2","unstructured":"National Committee for Clinical Laboratory Standards\n          Methods for dilution antimicrobial susceptibility test for bacterial that grow aerobically. Approved standard M7-A.\n          1997\n          National Committee for Clinical Laboratory Standards\n          Wayne Pa"},{"key":"e_1_3_2_20_2","doi-asserted-by":"publisher","DOI":"10.1128\/AAC.36.9.1991"},{"key":"e_1_3_2_21_2","doi-asserted-by":"publisher","DOI":"10.1128\/AAC.39.5.1199"},{"key":"e_1_3_2_22_2","doi-asserted-by":"publisher","DOI":"10.1128\/AAC.34.11.2200"},{"key":"e_1_3_2_23_2","doi-asserted-by":"publisher","DOI":"10.1128\/AAC.33.8.1131"},{"key":"e_1_3_2_24_2","doi-asserted-by":"publisher","DOI":"10.1128\/AAC.42.1.108"},{"key":"e_1_3_2_25_2","doi-asserted-by":"publisher","DOI":"10.1128\/AAC.33.9.1451"},{"key":"e_1_3_2_26_2","doi-asserted-by":"publisher","DOI":"10.1128\/AAC.34.8.1590"},{"key":"e_1_3_2_27_2","doi-asserted-by":"publisher","DOI":"10.1128\/AAC.37.9.1989"},{"key":"e_1_3_2_28_2","doi-asserted-by":"publisher","DOI":"10.1093\/clinids\/23.1.118"},{"key":"e_1_3_2_29_2","unstructured":"Sambrook\n              J.\n              Fritsch\n              E. F.\n              Maniatis\n              T.\n          Molecular cloning: a laboratory manual\n          2nd ed.\n          1989\n          Cold Spring Harbor Laboratory Press\n          Cold Spring Harbor N.Y"},{"key":"e_1_3_2_30_2","doi-asserted-by":"crossref","first-page":"3179","DOI":"10.1021\/bi00227a004","article-title":"Substitution of lysine at position 104 or 240 of TEM-1pTZ18R \u03b2-lactamase enhances the effect of serine-164 substitution on hydrolysis or affinity for cephalosporins and the monobactam aztreonam.","volume":"30","author":"Sowek J. A.","year":"1991","unstructured":"Sowek J. A. Singer S. B. Ohringer S. Malley M. F. Dougherty T. J. Gougoutas J. Z. Bush K. Substitution of lysine at position 104 or 240 of TEM-1pTZ18R \u03b2-lactamase enhances the effect of serine-164 substitution on hydrolysis or affinity for cephalosporins and the monobactam aztreonam. Biochemistry 30 1991 3179 3188","journal-title":"Biochemistry"},{"key":"e_1_3_2_31_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.75.8.3737"},{"key":"e_1_3_2_32_2","first-page":"193","article-title":"Biochemical characterization of the carbapenem-hydrolyzing \u03b2-lactamase AsbM1 from Aeromonas sobria AER 14M: a member of a novel subgroup of metallo-\u03b2-lactamases.","volume":"137","author":"Yang Y.","year":"1996","unstructured":"Yang Y. Bush K. Biochemical characterization of the carbapenem-hydrolyzing \u03b2-lactamase AsbM1 from Aeromonas sobria AER 14M: a member of a novel subgroup of metallo-\u03b2-lactamases. FEMS Microbiol. Lett. 137 1996 193 200","journal-title":"FEMS Microbiol. Lett."},{"key":"e_1_3_2_33_2","unstructured":"Yang\n              Y.\n              Bhachech\n              N.\n              Bradford\n              P. A.\n              Jett\n              B. D.\n              Sahm\n              D. F.\n              Bush\n              K.\n          Ceftazidime-resistant Klebsiella pneumoniae and E. coli isolates producing TEM-10 and TEM-43 \u03b2-lactamases from St. Louis abstr. C-25\n          Program and abstracts of the 36th Interscience Conference on Antimicrobial Agents and Chemotherapy.\n          1996\n          38\n          American Society for Microbiology\n          Washington D.C"}],"container-title":["Antimicrobial Agents and Chemotherapy"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/journals.asm.org\/doi\/pdf\/10.1128\/AAC.42.7.1671","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/journals.asm.org\/doi\/pdf\/10.1128\/AAC.42.7.1671","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,2,21]],"date-time":"2022-02-21T16:11:54Z","timestamp":1645459914000},"score":1,"resource":{"primary":{"URL":"https:\/\/journals.asm.org\/doi\/10.1128\/AAC.42.7.1671"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1998,7]]},"references-count":32,"journal-issue":{"issue":"7","published-print":{"date-parts":[[1998,7]]}},"alternative-id":["10.1128\/AAC.42.7.1671"],"URL":"https:\/\/doi.org\/10.1128\/aac.42.7.1671","relation":{},"ISSN":["0066-4804","1098-6596"],"issn-type":[{"value":"0066-4804","type":"print"},{"value":"1098-6596","type":"electronic"}],"subject":[],"published":{"date-parts":[[1998,7]]},"assertion":[{"value":"1997-11-03","order":0,"name":"received","label":"Received","group":{"name":"publication_history","label":"Publication History"}},{"value":"1998-04-09","order":1,"name":"accepted","label":"Accepted","group":{"name":"publication_history","label":"Publication History"}},{"value":"1998-07-01","order":2,"name":"published","label":"Published","group":{"name":"publication_history","label":"Publication History"}}]}}