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<article article-type="research-article" dtd-version="1.3" xmlns:mml="http://www.w3.org/1998/Math/MathML" xmlns:xlink="http://www.w3.org/1999/xlink" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xml:lang="ru"><front><journal-meta><journal-id journal-id-type="publisher-id">actabiomedica</journal-id><journal-title-group><journal-title xml:lang="ru">Acta Biomedica Scientifica</journal-title><trans-title-group xml:lang="en"><trans-title>Acta Biomedica Scientifica</trans-title></trans-title-group></journal-title-group><issn pub-type="ppub">2541-9420</issn><issn pub-type="epub">2587-9596</issn><publisher><publisher-name>Scientific Centre for Family Health and Human Reproduction Problems</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="doi">10.29413/ABS.2020-5.6.11</article-id><article-id custom-type="elpub" pub-id-type="custom">actabiomedica-2501</article-id><article-categories><subj-group subj-group-type="heading"><subject>Research Article</subject></subj-group><subj-group subj-group-type="section-heading" xml:lang="ru"><subject>МИКРОБИОЛОГИЯ И ВИРУСОЛОГИЯ</subject></subj-group><subj-group subj-group-type="section-heading" xml:lang="en"><subject>MICROBIOLOGY AND VIRUSOLOGY</subject></subj-group></article-categories><title-group><article-title>Карбапенемазы как фактор устойчивости к антибактериальным препаратам</article-title><trans-title-group xml:lang="en"><trans-title>Carbapenemases as factors of Resistance to Antibacterial Drugs</trans-title></trans-title-group></title-group><contrib-group><contrib contrib-type="author" corresp="yes"><name-alternatives><name name-style="eastern" xml:lang="ru"><surname>Невежина</surname><given-names>А. В.</given-names></name><name name-style="western" xml:lang="en"><surname>Nevezhina</surname><given-names>A. V.</given-names></name></name-alternatives><bio xml:lang="ru"><p>младший научный сотрудник лаборатории клеточных технологий и регенеративной медицины</p><p>664003, г. Иркутск, ул. Борцов Революции, 1, Россия </p></bio><bio xml:lang="en"><p>Junior Research Officer at the Laboratory of Cell Technologies and Regenerative Medicine</p><p>Bortsov Revolyutsii str. 1, Irkutsk 664003, Russian Federation </p></bio><email xlink:type="simple">hannanevezhina@gmail.com</email><xref ref-type="aff" rid="aff-1"/></contrib></contrib-group><aff-alternatives id="aff-1"><aff xml:lang="ru"><institution>ФГБНУ «Иркутский научный центр хирургии и травматологии»</institution></aff><aff xml:lang="en"><institution>Irkutsk Scientific Centre of Surgery and Traumatology</institution></aff></aff-alternatives><pub-date pub-type="collection"><year>2020</year></pub-date><pub-date pub-type="epub"><day>14</day><month>01</month><year>2021</year></pub-date><volume>5</volume><issue>6</issue><fpage>95</fpage><lpage>105</lpage><permissions><copyright-statement>Copyright &amp;#x00A9; Невежина А.В., 2021</copyright-statement><copyright-year>2021</copyright-year><copyright-holder xml:lang="ru">Невежина А.В.</copyright-holder><copyright-holder xml:lang="en">Nevezhina A.V.</copyright-holder><license xml:lang="ru" license-type="creative-commons-attribution" xlink:href="https://creativecommons.org/licenses/by/4.0/" xlink:type="simple"><license-p>Данная работа распространяется под лицензией Creative Commons Attribution 4.0.</license-p></license><license xml:lang="en" license-type="creative-commons-attribution" xlink:href="https://creativecommons.org/licenses/by/4.0/" xlink:type="simple"><license-p>This work is licensed under a Creative Commons Attribution 4.0 License.</license-p></license></permissions><self-uri xlink:href="https://www.actabiomedica.ru/jour/article/view/2501">https://www.actabiomedica.ru/jour/article/view/2501</self-uri><abstract/><trans-abstract xml:lang="en"/><kwd-group xml:lang="ru"><kwd>антибиотики</kwd><kwd>резистентность</kwd><kwd>карбапенемы</kwd><kwd>карбапенемазы</kwd></kwd-group><kwd-group xml:lang="en"><kwd>carbapenemase</kwd><kwd>beta-lactamase</kwd><kwd>antibiotic</kwd></kwd-group></article-meta></front><back><ref-list><title>References</title><ref id="cit1"><label>1</label><citation-alternatives><mixed-citation xml:lang="ru">Meletis G. Carbapenem resistance: Overview of the problem and future perspectives. Ther Adv Infect Dis. 2016; 3(1): 15-21. doi: 10.1177/2049936115621709</mixed-citation><mixed-citation xml:lang="en">Meletis G. Carbapenem resistance: Overview of the problem and future perspectives. Ther Adv Infect Dis. 2016; 3(1): 15-21. doi: 10.1177/2049936115621709</mixed-citation></citation-alternatives></ref><ref id="cit2"><label>2</label><citation-alternatives><mixed-citation xml:lang="ru">Codjoe FS, Donkor ES. Carbapenem resistance: A review. Med Sci (Basel). 2017; 6(1): 1. doi: 10.3390/medsci6010001</mixed-citation><mixed-citation xml:lang="en">Codjoe FS, Donkor ES. Carbapenem resistance: A review. Med Sci (Basel). 2017; 6(1): 1. doi: 10.3390/medsci6010001</mixed-citation></citation-alternatives></ref><ref id="cit3"><label>3</label><citation-alternatives><mixed-citation xml:lang="ru">Dadgostar P. Antimicrobial resistance: Implications and costs. Infect Drug Resist. 2019; 12: 3903-3910. doi: 10.2147/IDR.S234610</mixed-citation><mixed-citation xml:lang="en">Dadgostar P. Antimicrobial resistance: Implications and costs. Infect Drug Resist. 2019; 12: 3903-3910. doi: 10.2147/IDR.S234610</mixed-citation></citation-alternatives></ref><ref id="cit4"><label>4</label><citation-alternatives><mixed-citation xml:lang="ru">Walther-Rasmussen J, Hoiby N. OXA-type carbapenemases. J Antimicrob Chemother. 2006; 57(3): 373-383. doi: 10.1093/jac/dki482</mixed-citation><mixed-citation xml:lang="en">Walther-Rasmussen J, Hoiby N. OXA-type carbapenemases. J Antimicrob Chemother. 2006; 57(3): 373-383. doi: 10.1093/jac/dki482</mixed-citation></citation-alternatives></ref><ref id="cit5"><label>5</label><citation-alternatives><mixed-citation xml:lang="ru">Hammoudi HD, Ayoub MC. The current burden of carbapenemases: Review of significant properties and dissemination among gram-negative bacteria. Antibiotics (Basel). 2020; 9(4): 186. doi: 10.3390/antibiotics9040186</mixed-citation><mixed-citation xml:lang="en">Hammoudi HD, Ayoub MC. The current burden of carbapenemases: Review of significant properties and dissemination among gram-negative bacteria. Antibiotics (Basel). 2020; 9(4): 186. doi: 10.3390/antibiotics9040186</mixed-citation></citation-alternatives></ref><ref id="cit6"><label>6</label><citation-alternatives><mixed-citation xml:lang="ru">Mangat CS, Vadlamani G, Holicek V, et al. Molecular basis for the potent inhibition of the emerging carbapenemase VCC-1 by avibactam. Antimicrob Agents Chemother. 2019; 63(4). doi: 10.1128/aac.02112-18</mixed-citation><mixed-citation xml:lang="en">Mangat CS, Vadlamani G, Holicek V, et al. Molecular basis for the potent inhibition of the emerging carbapenemase VCC-1 by avibactam. Antimicrob Agents Chemother. 2019; 63(4). doi: 10.1128/aac.02112-18</mixed-citation></citation-alternatives></ref><ref id="cit7"><label>7</label><citation-alternatives><mixed-citation xml:lang="ru">Roschanski N, Guenther S, Vu TTT, et al. VIM-1 carbapenemase-producing Escherichia coli isolated from retail seafood, Germany 2016 [published correction appears in Euro Surveill. 2017 Nov;22(45):]. Euro Surveill. 2017; 22(43): 17-00032. doi: 10.2807/1560-7917.ES.2017.22.43.17-00032</mixed-citation><mixed-citation xml:lang="en">Roschanski N, Guenther S, Vu TTT, et al. VIM-1 carbapenemase-producing Escherichia coli isolated from retail seafood, Germany 2016 [published correction appears in Euro Surveill. 2017 Nov;22(45):]. Euro Surveill. 2017; 22(43): 17-00032. doi: 10.2807/1560-7917.ES.2017.22.43.17-00032</mixed-citation></citation-alternatives></ref><ref id="cit8"><label>8</label><citation-alternatives><mixed-citation xml:lang="ru">Sugawara Y, Hagiya H, Akeda Y, et al. Dissemination of carbapenemase-producing Enterobacteriaceae harbouring bla NDM or blaIMI in local market foods of Yangon, Myanmar. Sci Rep. 2019; 9: 14455. doi: 10.1038/s41598-019-51002-5</mixed-citation><mixed-citation xml:lang="en">Sugawara Y, Hagiya H, Akeda Y, et al. Dissemination of carbapenemase-producing Enterobacteriaceae harbouring bla NDM or blaIMI in local market foods of Yangon, Myanmar. Sci Rep. 2019; 9: 14455. doi: 10.1038/s41598-019-51002-5</mixed-citation></citation-alternatives></ref><ref id="cit9"><label>9</label><citation-alternatives><mixed-citation xml:lang="ru">Elshamy AA, Aboshanab KM. A review on bacterial resistance to carbapenems: Epidemiology, detection and treatment options. Future Sci OA. 2020; 6: 3. doi: 10.2144/fsoa-2019-0098</mixed-citation><mixed-citation xml:lang="en">Elshamy AA, Aboshanab KM. A review on bacterial resistance to carbapenems: Epidemiology, detection and treatment options. Future Sci OA. 2020; 6: 3. doi: 10.2144/fsoa-2019-0098</mixed-citation></citation-alternatives></ref><ref id="cit10"><label>10</label><citation-alternatives><mixed-citation xml:lang="ru">Полищук А.Г., Якубович Е.И., Полухина О.В., Осовских В.В., Евтушенко В.И. Карбапенемаза- продуцирующие грамотрицательные бактерии в специализированном стационаре Санкт-Петербурга. Инфекция и иммунитет. 2017; 7(2): 181-192. doi: 10.15789/2220-7619-2017-2-181-192.</mixed-citation><mixed-citation xml:lang="en">Polishchuk AG, Iakubovich EI, Polukhina OV, Osovskikh VV, Evtushenko VI. Carbapenemase-producing gram-negative bacteria in a specialized hospital in St. Petersburg. Russian Journal of Infection and Immunity. 2017; 7(2): 181-192. doi: 10.15789/2220-7619-2017-2-181-192. (In Russ.)</mixed-citation></citation-alternatives></ref><ref id="cit11"><label>11</label><citation-alternatives><mixed-citation xml:lang="ru">Jeon JH, Lee JH, Lee JJ, et al. Structural basis for carbapenem-hydrolyzing mechanisms of carbapenemases conferring antibiotic resistance. Int J Mol Sci. 2015; 16(5): 9654-9692. doi: 10.3390/ijms16059654</mixed-citation><mixed-citation xml:lang="en">Jeon JH, Lee JH, Lee JJ, et al. Structural basis for carbapenem-hydrolyzing mechanisms of carbapenemases conferring antibiotic resistance. Int J Mol Sci. 2015; 16(5): 9654-9692. doi: 10.3390/ijms16059654</mixed-citation></citation-alternatives></ref><ref id="cit12"><label>12</label><citation-alternatives><mixed-citation xml:lang="ru">Sawa T, Kooguchi K, Moriyama K. Molecular diversity of extended-spectrum β-lactamases and carbapenemases, and antimicrobial resistance. J intensive care. 2020; 8(13). doi: 10.1186/s40560-020-0429-6</mixed-citation><mixed-citation xml:lang="en">Sawa T, Kooguchi K, Moriyama K. Molecular diversity of extended-spectrum β-lactamases and carbapenemases, and antimicrobial resistance. J intensive care. 2020; 8(13). doi: 10.1186/s40560-020-0429-6</mixed-citation></citation-alternatives></ref><ref id="cit13"><label>13</label><citation-alternatives><mixed-citation xml:lang="ru">Reyes JA, Melano R, Cardenas PA, Trueba G. Mobile genetic elements associated with carbapenemase genes in South American Enterobacterales. Braz J Infect Dis. 2020; 24(3): 231-238. doi: 10.1016/j.bjid.2020.03.002</mixed-citation><mixed-citation xml:lang="en">Reyes JA, Melano R, Cardenas PA, Trueba G. Mobile genetic elements associated with carbapenemase genes in South American Enterobacterales. Braz J Infect Dis. 2020; 24(3): 231-238. doi: 10.1016/j.bjid.2020.03.002</mixed-citation></citation-alternatives></ref><ref id="cit14"><label>14</label><citation-alternatives><mixed-citation xml:lang="ru">Partridge SR, Kwong SM, Firth N, Jensen SO. Mobile genetic elements associated with antimicrobial resistance. Clin Microbiol Rev. 2018; 31(4): e00088-17. doi: 10.1128/CMR.00088-17</mixed-citation><mixed-citation xml:lang="en">Partridge SR, Kwong SM, Firth N, Jensen SO. Mobile genetic elements associated with antimicrobial resistance. Clin Microbiol Rev. 2018; 31(4): e00088-17. doi: 10.1128/CMR.00088-17</mixed-citation></citation-alternatives></ref><ref id="cit15"><label>15</label><citation-alternatives><mixed-citation xml:lang="ru">Diene SM, Rolain J-M. Carbapenemase genes and genetic platforms in Gram-negative bacilli: Enterobacteriaceae, Pseudomonas and Acinetobacter species. Clin Microbiol Infect. 2014; 20(9): 831-838. doi: 10.1111/1469-0691.12655</mixed-citation><mixed-citation xml:lang="en">Diene SM, Rolain J-M. Carbapenemase genes and genetic platforms in Gram-negative bacilli: Enterobacteriaceae, Pseudomonas and Acinetobacter species. Clin Microbiol Infect. 2014; 20(9): 831-838. doi: 10.1111/1469-0691.12655</mixed-citation></citation-alternatives></ref><ref id="cit16"><label>16</label><citation-alternatives><mixed-citation xml:lang="ru">Brouwer MSM, Tehrani KHME, Rapallini M, et al. Novel carbapenemases FLC-1 and IMI-2 encoded by an Enterobacter cloacae complex isolated from food products. Antimicrob Agents Chemother. 2019; 63(6): e02338-18. doi: 10.1128/AAC.02338-18</mixed-citation><mixed-citation xml:lang="en">Brouwer MSM, Tehrani KHME, Rapallini M, et al. Novel carbapenemases FLC-1 and IMI-2 encoded by an Enterobacter cloacae complex isolated from food products. Antimicrob Agents Chemother. 2019; 63(6): e02338-18. doi: 10.1128/AAC.02338-18</mixed-citation></citation-alternatives></ref><ref id="cit17"><label>17</label><citation-alternatives><mixed-citation xml:lang="ru">Aires-de-Sousa M, Ortiz de la Rosa J, Gonçalves M, Pereira A, Nordmann P, Poirel L. Epidemiology of carbapenemaseproducing Klebsiella pneumoniae in a hospital, Portugal. Emerg Infect Dis. 2019; 25(9): 1632-1638. doi: 10.3201/eid2509.190656</mixed-citation><mixed-citation xml:lang="en">Aires-de-Sousa M, Ortiz de la Rosa J, Gonçalves M, Pereira A, Nordmann P, Poirel L. Epidemiology of carbapenemaseproducing Klebsiella pneumoniae in a hospital, Portugal. Emerg Infect Dis. 2019; 25(9): 1632-1638. doi: 10.3201/eid2509.190656</mixed-citation></citation-alternatives></ref><ref id="cit18"><label>18</label><citation-alternatives><mixed-citation xml:lang="ru">Piccirilli A, Mercuri PS, Galleni M, et al. P174E substitution in GES-1 and GES-5 β-lactamases improves catalytic efficiency toward carbapenems. Antimicrob Agents Chemother. 2018; 62(5): e01851-17. doi: 10.1128/AAC.01851-17</mixed-citation><mixed-citation xml:lang="en">Piccirilli A, Mercuri PS, Galleni M, et al. P174E substitution in GES-1 and GES-5 β-lactamases improves catalytic efficiency toward carbapenems. Antimicrob Agents Chemother. 2018; 62(5): e01851-17. doi: 10.1128/AAC.01851-17</mixed-citation></citation-alternatives></ref><ref id="cit19"><label>19</label><citation-alternatives><mixed-citation xml:lang="ru">Chihi H, Bonnin RA, Bourouis A, Mahrouki S, Besbes S, Moussa MB, et al. GES-11-producing Acinetobacter baumannii clinical isolates from Tunisian hospitals: Long-term dissemination of GES-type carbapenemases in North Africa. J Glob Antimicrob Resist. 2016; 5: 47-50. doi: 10.1016/j.jgar.2016.03.005</mixed-citation><mixed-citation xml:lang="en">Chihi H, Bonnin RA, Bourouis A, Mahrouki S, Besbes S, Moussa MB, et al. GES-11-producing Acinetobacter baumannii clinical isolates from Tunisian hospitals: Long-term dissemination of GES-type carbapenemases in North Africa. J Glob Antimicrob Resist. 2016; 5: 47-50. doi: 10.1016/j.jgar.2016.03.005</mixed-citation></citation-alternatives></ref><ref id="cit20"><label>20</label><citation-alternatives><mixed-citation xml:lang="ru">Hopkins KL, Findlay J, Meunier D, Cummins M, Curtis S, Kustos I, et al. Serratia marcescens producing SME carbapenemases: An emerging resistance problem in the UK? J Antimicrob Chemother. 2017; 72(5): 1535-1537. doi: 10.1093/jac/dkw567</mixed-citation><mixed-citation xml:lang="en">Hopkins KL, Findlay J, Meunier D, Cummins M, Curtis S, Kustos I, et al. Serratia marcescens producing SME carbapenemases: An emerging resistance problem in the UK? J Antimicrob Chemother. 2017; 72(5): 1535-1537. doi: 10.1093/jac/dkw567</mixed-citation></citation-alternatives></ref><ref id="cit21"><label>21</label><citation-alternatives><mixed-citation xml:lang="ru">Iovene MR, Pota V, Galdiero M, et al. First Italian outbreak of VIM-producing Serratia marcescens in an adult polyvalent intensive care unit, August-October 2018: A case report and literature review. World J Clin Cases. 2019; 7(21): 3535-3548. doi: 10.12998/wjcc.v7.i21.3535</mixed-citation><mixed-citation xml:lang="en">Iovene MR, Pota V, Galdiero M, et al. First Italian outbreak of VIM-producing Serratia marcescens in an adult polyvalent intensive care unit, August-October 2018: A case report and literature review. World J Clin Cases. 2019; 7(21): 3535-3548. doi: 10.12998/wjcc.v7.i21.3535</mixed-citation></citation-alternatives></ref><ref id="cit22"><label>22</label><citation-alternatives><mixed-citation xml:lang="ru">Sahuquillo-Arce JM, Hernandez-Cabezas A, Yarad-Auad F, Ibanez-Martínez E, Falomir-Salcedo P, Ruiz-Gaitán A. Carbapenemases: A worldwide threat to antimicrobial therapy. World J Pharmacol. 2015; 4(1): 75-95. doi: 10.5497/wjp.v4.i1.75</mixed-citation><mixed-citation xml:lang="en">Sahuquillo-Arce JM, Hernandez-Cabezas A, Yarad-Auad F, Ibanez-Martínez E, Falomir-Salcedo P, Ruiz-Gaitán A. Carbapenemases: A worldwide threat to antimicrobial therapy. World J Pharmacol. 2015; 4(1): 75-95. doi: 10.5497/wjp.v4.i1.75</mixed-citation></citation-alternatives></ref><ref id="cit23"><label>23</label><citation-alternatives><mixed-citation xml:lang="ru">Liakopoulos A, Mevius D, Ceccarelli D. A review of SHV extended-spectrum β-lactamases: Neglected yet ubiquitous. Front Microbiol. 2016; 7: 1374. doi: 10.3389/fmicb.2016.01374</mixed-citation><mixed-citation xml:lang="en">Liakopoulos A, Mevius D, Ceccarelli D. A review of SHV extended-spectrum β-lactamases: Neglected yet ubiquitous. Front Microbiol. 2016; 7: 1374. doi: 10.3389/fmicb.2016.01374</mixed-citation></citation-alternatives></ref><ref id="cit24"><label>24</label><citation-alternatives><mixed-citation xml:lang="ru">Naas T, Dortet L, Iorga BI. Structural and functional aspects of class A carbapenemases. Current Drug Targets. 2016; 17(9): 1006-1028. doi: 10.2174/1389450117666160310144501</mixed-citation><mixed-citation xml:lang="en">Naas T, Dortet L, Iorga BI. Structural and functional aspects of class A carbapenemases. Current Drug Targets. 2016; 17(9): 1006-1028. doi: 10.2174/1389450117666160310144501</mixed-citation></citation-alternatives></ref><ref id="cit25"><label>25</label><citation-alternatives><mixed-citation xml:lang="ru">Cui X, Zhang H, Du H. Carbapenemases in Enterobacteriaceae: Detection and antimicrobial therapy. Front Microbiol. 2019; 10: 1823. doi: 10.3389/fmicb.2019.01823</mixed-citation><mixed-citation xml:lang="en">Cui X, Zhang H, Du H. Carbapenemases in Enterobacteriaceae: Detection and antimicrobial therapy. Front Microbiol. 2019; 10: 1823. doi: 10.3389/fmicb.2019.01823</mixed-citation></citation-alternatives></ref><ref id="cit26"><label>26</label><citation-alternatives><mixed-citation xml:lang="ru">Niu S, Chavda KD, Wei J, et al. A ceftazidime- avibactamresistant and carbapenem-susceptible Klebsiella pneumoniae strain harboring blaKPC-14 isolated in New York City. mSphere. 2020; 5(4): e00775-20. doi: 10.1128/mSphere.00775-20</mixed-citation><mixed-citation xml:lang="en">Niu S, Chavda KD, Wei J, et al. A ceftazidime-avibactamresistant and carbapenem-susceptible Klebsiella pneumoniae strain harboring blaKPC-14 isolated in New York City. mSphere. 2020; 5(4): e00775-20. doi: 10.1128/mSphere.00775-20</mixed-citation></citation-alternatives></ref><ref id="cit27"><label>27</label><citation-alternatives><mixed-citation xml:lang="ru">Bonnin RA, Jousset AB, Urvoy N, Gauthier L, Tlili L,</mixed-citation><mixed-citation xml:lang="en">Bonnin RA, Jousset AB, Urvoy N, Gauthier L, Tlili L, Creton E, et al. Detection of GES-5 carbapenemase in Klebsiella pneumoniae, a newcomer in France. Antimicrob Agents Chemother. 2017; 61(3): e02263-16. doi: 10.1128/AAC.02263-16</mixed-citation></citation-alternatives></ref><ref id="cit28"><label>28</label><citation-alternatives><mixed-citation xml:lang="ru">Creton E, et al. Detection of GES-5 carbapenemase in Klebsiella pneumoniae, a newcomer in France. Antimicrob Agents Chemother. 2017; 61(3): e02263-16. doi: 10.1128/AAC.02263-16</mixed-citation><mixed-citation xml:lang="en">Marsh JW, Mustapha MM, Griffith MP, Evans DR, Ezeonwuka C, Pasculle AW, et al. Evolution of outbreak-causing carbapenem-resistant Klebsiella pneumoniae ST258 at a tertiary care hospital over 8 years. MBio. 2019; 10(5): e01945-19. doi: 10.1128/mBio.01945-19</mixed-citation></citation-alternatives></ref><ref id="cit29"><label>29</label><citation-alternatives><mixed-citation xml:lang="ru">Marsh JW, Mustapha MM, Griffith MP, Evans DR, Ezeonwuka C, Pasculle AW, et al. Evolution of outbreak- causing carbapenem-resistant Klebsiella pneumoniae ST258 at a tertiary care hospital over 8 years. MBio. 2019; 10(5): e01945-19. doi: 10.1128/mBio.01945-19</mixed-citation><mixed-citation xml:lang="en">Duin D van, Doi Y. The global epidemiology of carbapenemase-producing Enterobacteriaceae. Virulence. 2017; 8(4): 460-469. doi: 10.1080/21505594.2016.1222343</mixed-citation></citation-alternatives></ref><ref id="cit30"><label>30</label><citation-alternatives><mixed-citation xml:lang="ru">Duin D van, Doi Y. The global epidemiology of carbapenemase-producing Enterobacteriaceae. Virulence. 2017; 8(4): 460-469. doi: 10.1080/21505594.2016.1222343</mixed-citation><mixed-citation xml:lang="en">Antonelli A, D’Andrea MM, Di Pilato V, et al. Characterization of a novel putative Xer-dependent integrative mobile element carrying the bla(NMC-A) carbapenemase gene, inserted into the chromosome of members of the Enterobacter cloacae complex. Antimicrob Agents Chemother. 2015; 59(10): 6620-6624. doi: 10.1128/aac.01452-15</mixed-citation></citation-alternatives></ref><ref id="cit31"><label>31</label><citation-alternatives><mixed-citation xml:lang="ru">Antonelli A, D›Andrea MM, Di Pilato V, et al. Characterization of a novel putative Xer-dependent integrative mobile element carrying the bla(NMC-A) carbapenemase gene, inserted into the chromosome of members of the Enterobacter cloacae complex. Antimicrob Agents Chemother. 2015; 59(10): 6620-6624. doi: 10.1128/aac.01452-15</mixed-citation><mixed-citation xml:lang="en">Boyd DA, Mataseje LF, Davidson R, Delport JA, Fuller J, Hoang L, et al. Enterobacter cloacae complex isolates harboring bla NMC-A or blaIMI-type class A carbapenemase genes on novel chromosomal integrative elements and plasmids. Antimicrob Agents Chemother. 2017; 61(5): e02578-16. doi: 10.1128/AAC.02578-16</mixed-citation></citation-alternatives></ref><ref id="cit32"><label>32</label><citation-alternatives><mixed-citation xml:lang="ru">Boyd DA, Mataseje LF, Davidson R, Delport JA, Fuller J, Hoang L, et al. Enterobacter cloacae complex isolates harboring bla NMC-A or blaIMI-type class A carbapenemase genes on novel chromosomal integrative elements and plasmids. Antimicrob Agents Chemother. 2017; 61(5): e02578-16. doi: 10.1128/AAC.02578-16</mixed-citation><mixed-citation xml:lang="en">Hopkins KL, Findlay J, Doumith M, Mather B, Meunier D, D’Arcy S, et al. IMI-2 carbapenemase in a clinical Klebsiella variicola isolated in the UK. J Antimicrob Chemother. 2017; 72(7): 2129-2131. doi: 10.1093/jac/dkx103</mixed-citation></citation-alternatives></ref><ref id="cit33"><label>33</label><citation-alternatives><mixed-citation xml:lang="ru">Hopkins KL, Findlay J, Doumith M, Mather B, Meunier D, D’Arcy S, et al. IMI-2 carbapenemase in a clinical Klebsiella variicola isolated in the UK. J Antimicrob Chemother. 2017; 72(7): 2129-2131. doi: 10.1093/jac/dkx103</mixed-citation><mixed-citation xml:lang="en">Huang L, Wang X, Feng Y, Xie Y, Xie L, Zong Z. First identification of an IMI-1 carbapenemase-producing colistin-resistant Enterobacter cloacae in China. Ann Clin Microbiol Antimicrob. 2015; 14: 51. doi: 10.1186/s12941-015-0112-2</mixed-citation></citation-alternatives></ref><ref id="cit34"><label>34</label><citation-alternatives><mixed-citation xml:lang="ru">Huang L, Wang X, Feng Y, Xie Y, Xie L, Zong Z. First identification of an IMI-1 carbapenemase-producing colistin-resistant Enterobacter cloacae in China. Ann Clin Microbiol Antimicrob. 2015; 14: 51. doi: 10.1186/s12941-015-0112-2</mixed-citation><mixed-citation xml:lang="en">Fonseca F, Sarmento AC, Henriques I, Samyn B, Beeumen J van, Domingues P, et al. Biochemical characterization of SFC-1, a class A carbapenem-hydrolyzing β-lactamase. Antimicrob Agents Chemother. 2007; 51(12): 4512-4514. doi: 10.1128/AAC.00491-07</mixed-citation></citation-alternatives></ref><ref id="cit35"><label>35</label><citation-alternatives><mixed-citation xml:lang="ru">Fonseca F, Sarmento AC, Henriques I, Samyn B, Beeumen J van, Domingues P, et al. Biochemical characterization of SFC-1, a class A carbapenem-hydrolyzing β-lactamase. Antimicrob Agents Chemother. 2007; 51(12): 4512-4514. doi: 10.1128/AAC.00491-07</mixed-citation><mixed-citation xml:lang="en">Henriques I, Moura A, Alves A, Saavedra MJ, Correia A. Molecular characterization of a carbapenem-hydrolyzing class A β-lactamase, SFC-1, from Serratia fonticola UTAD54. Antimicrob Agents Chemother. 2004; 48(6): 2321-2324; doi: 10.1128/AAC.48.6.2321-2324.2004</mixed-citation></citation-alternatives></ref><ref id="cit36"><label>36</label><citation-alternatives><mixed-citation xml:lang="ru">Henriques I, Moura A, Alves A, Saavedra MJ, Correia A. Molecular characterization of a carbapenem-hydrolyzing class A β-lactamase, SFC-1, from Serratia fonticola UTAD54. Antimicrob Agents Chemother. 2004; 48(6): 2321-2324; doi: 10.1128/AAC.48.6.2321-2324.2004</mixed-citation><mixed-citation xml:lang="en">Becka SA, Zeiser ET, Marshall SH, et al. Sequence heterogeneity of the PenA carbapenemase in clinical isolates of Burkholderia multivorans. Diagn Microbiol Infect Dis. 2018; 92(3): 253-258. doi: 10.1016/j.diagmicrobio.2018.06.005</mixed-citation></citation-alternatives></ref><ref id="cit37"><label>37</label><citation-alternatives><mixed-citation xml:lang="ru">Becka SA, Zeiser ET, Marshall SH, et al. Sequence heterogeneity of the PenA carbapenemase in clinical isolates of Burkholderia multivorans. Diagn Microbiol Infect Dis. 2018; 92(3): 253-258. doi: 10.1016/j.diagmicrobio.2018.06.005</mixed-citation><mixed-citation xml:lang="en">Juan C, Torrens G, Gonzalez-Nicolau M, Oliver A. Diversity and regulation of intrinsic β-lactamases from non-fermenting and other Gram-negative opportunistic pathogens. FEMS Microbiol Rev. 2017; 41(6): 781-815. doi: 10.1093/femsre/fux043</mixed-citation></citation-alternatives></ref><ref id="cit38"><label>38</label><citation-alternatives><mixed-citation xml:lang="ru">Juan C, Torrens G, Gonzalez-Nicolau M, Oliver A. Diversity and regulation of intrinsic β-lactamases from non-fermenting and other Gram-negative opportunistic pathogens. FEMS Microbiol Rev. 2017; 41(6): 781-815. doi: 10.1093/femsre/fux043</mixed-citation><mixed-citation xml:lang="en">Papp-Wallace KM., Scott AB, Zeiser ET, et al. Overcoming an extremely drug resistant (XDR) pathogen: Avibactam restores susceptibility to ceftazidime for Burkholderia cepacia complex isolates from cystic fibrosis patients. ACS Infect Dis. 2017; 3(7): 502-511. doi: 10.1021/acsinfecdis.7b00020</mixed-citation></citation-alternatives></ref><ref id="cit39"><label>39</label><citation-alternatives><mixed-citation xml:lang="ru">Papp-Wallace KM., Scott AB, Zeiser ET, et al. Overcoming an extremely drug resistant (XDR) pathogen: Avibactam restores susceptibility to ceftazidime for Burkholderia cepacia complex isolates from cystic fibrosis patients. ACS Infect Dis. 2017; 3(7): 502-511. doi: 10.1021/acsinfecdis.7b00020</mixed-citation><mixed-citation xml:lang="en">Nicoletti AG, Marcondes MFM, Martins WMBS, Almeida LGP, Nicolás MF, Vasconcelos ATR, et al. Characterization of BKC-1 class A carbapenemase from Klebsiella pneumoniae clinical isolates in Brazil. Antimicrob Agents Chemother. 2015; 59(9): 5159-5164. doi: 10.1128/AAC.00158-15</mixed-citation></citation-alternatives></ref><ref id="cit40"><label>40</label><citation-alternatives><mixed-citation xml:lang="ru">Nicoletti AG, Marcondes MFM, Martins WMBS, Almeida LGP, Nicolás MF, Vasconcelos ATR, et al. Characterization of BKC-1 class A carbapenemase from Klebsiella pneumoniae clinical isolates in Brazil. Antimicrob Agents Chemother. 2015; 59(9): 5159-5164.</mixed-citation><mixed-citation xml:lang="en">Dortet L, Poirel L, Abbas S, Oueslati S, Nordmann P. Genetic and biochemical characterization of FRI-1, a carbapenem-hydrolyzing class A β-lactamase from Enterobacter cloacae. Antimicrob Agents Chemother. 2015; 59(12): 7420-7425. doi: 10.1128/AAC.01636-15</mixed-citation></citation-alternatives></ref><ref id="cit41"><label>41</label><citation-alternatives><mixed-citation xml:lang="ru">doi: 10.1128/AAC.00158-15</mixed-citation><mixed-citation xml:lang="en">Schauer J, Gatermann SG, Hoffmann D, Hupfeld L, Pfennigwerth N. GPC-1, a novel class A carbapenemase detected in a clinical Pseudomonas aeruginosa isolate. J Antimicrob Chemother. 2020; 75(4): 911-916. doi: 10.1093/jac/dkz536</mixed-citation></citation-alternatives></ref><ref id="cit42"><label>42</label><citation-alternatives><mixed-citation xml:lang="ru">Dortet L, Poirel L, Abbas S, Oueslati S, Nordmann P. Genetic and biochemical characterization of FRI-1, a carbapenemhydrolyzing class A β-lactamase from Enterobacter cloacae. Antimicrob Agents Chemother. 2015; 59(12): 7420-7425. doi: 10.1128/AAC.01636-15</mixed-citation><mixed-citation xml:lang="en">Lv R, Guo J, Yan Y, et al. Characterization of a novel class A carbapenemase PAD-1 from Paramesorhizobium desertii A-3-ET, a strain highly resistant to β-lactam antibiotics. Sci Rep. 2017; 7: 8370. doi: 10.1038/s41598-017-07841-1</mixed-citation></citation-alternatives></ref><ref id="cit43"><label>43</label><citation-alternatives><mixed-citation xml:lang="ru">Schauer J, Gatermann SG, Hoffmann D, Hupfeld L, Pfennigwerth N. GPC-1, a novel class A carbapenemase detected in a clinical Pseudomonas aeruginosa isolate. J Antimicrob Chemother. 2020; 75(4): 911-916. doi: 10.1093/jac/dkz536</mixed-citation><mixed-citation xml:lang="en">Tamma PD, Simner PJ. Phenotypic detection of carbapenemase-producing organisms from clinical isolates. J Clin Microbiol. 2018; 56(11): e01140-18. doi: 10.1128/JCM.01140-18</mixed-citation></citation-alternatives></ref><ref id="cit44"><label>44</label><citation-alternatives><mixed-citation xml:lang="ru">Lv R, Guo J, Yan Y, et al. Characterization of a novel class A carbapenemase PAD-1 from Paramesorhizobium desertii A-3-ET, a strain highly resistant to β-lactam antibiotics. Sci Rep. 2017; 7: 8370. doi: 10.1038/s41598-017-07841-1</mixed-citation><mixed-citation xml:lang="en">Mojica MF, Bonomo RA, Fast W. B1-metallo-β-lactamases: Where do we stand? Curr Drug Targets. 2016; 17(9): 1029-1050. doi: 10.2174/1389450116666151001105622</mixed-citation></citation-alternatives></ref><ref id="cit45"><label>45</label><citation-alternatives><mixed-citation xml:lang="ru">Tamma PD, Simner PJ. Phenotypic detection of carbapenemase-producing organisms from clinical isolates. J Clin Microbiol. 2018; 56(11): e01140-18. doi: 10.1128/JCM.01140-18</mixed-citation><mixed-citation xml:lang="en">Mercuri PS, Bouillenne F, Boschi L, et al. Biochemical characterization of the FEZ-1 metallo-beta-lactamase of Legionella gormanii ATCC 33297T produced in Escherichia coli. Antimicrob Agents Chemother. 2001; 45(4): 1254-1262. doi: 10.1128/AAC.45.4.1254-1262.2001</mixed-citation></citation-alternatives></ref><ref id="cit46"><label>46</label><citation-alternatives><mixed-citation xml:lang="ru">Mojica MF, Bonomo RA, Fast W. B1-metallo-β-lactamases: Where do we stand? Curr Drug Targets. 2016; 17(9): 1029-1050. doi: 10.2174/1389450116666151001105622</mixed-citation><mixed-citation xml:lang="en">Lowe CF, Matic N, Champagne S, Romney MG, Leung V, Ritchie G. The brief case: IMP, the uncommonly common carbapenemase. J Clin Microbiol. 2020; 58(4): e01094-19. doi: 10.1128/JCM.01094-19</mixed-citation></citation-alternatives></ref><ref id="cit47"><label>47</label><citation-alternatives><mixed-citation xml:lang="ru">Mercuri PS, Bouillenne F, Boschi L, et al. Biochemical characterization of the FEZ-1 metallo-beta-lactamase of Legionella gormanii ATCC 33297T produced in Escherichia coli. Antimicrob Agents Chemother. 2001; 45(4): 1254-1262. doi: 10.1128/AAC.45.4.1254-1262.2001</mixed-citation><mixed-citation xml:lang="en">Bonardi S, Pitino R. Carbapenemase-producing bacteria in food-producing animals, wildlife and environment: A challenge for human health. Ital J Food Saf. 2019; 8(2): 7956. doi: 10.4081/ijfs.2019.7956</mixed-citation></citation-alternatives></ref><ref id="cit48"><label>48</label><citation-alternatives><mixed-citation xml:lang="ru">Lowe CF, Matic N, Champagne S, Romney MG, Leung V, Ritchie G. The brief case: IMP, the uncommonly common carbapenemase. J Clin Microbiol. 2020; 58(4): e01094-19. doi: 10.1128/JCM.01094-19</mixed-citation><mixed-citation xml:lang="en">Makena A, Duzgun AO, Brem J, McDonough MA, Rydzik AM, Abboud MI, et al. Comparison of Verona integron-Borne metallo-β-lactamase (VIM) variants reveals differences in stability and inhibition profiles. Antimicrob Agents Chemother. 2016; 60(3): 1377-1384. doi: 10.1128/AAC.01768-15</mixed-citation></citation-alternatives></ref><ref id="cit49"><label>49</label><citation-alternatives><mixed-citation xml:lang="ru">Bonardi S, Pitino R. Carbapenemase-producing bacteria in food-producing animals, wildlife and environment: A challenge for human health. Ital J Food Saf. 2019; 8(2): 7956. doi: 10.4081/ijfs.2019.7956</mixed-citation><mixed-citation xml:lang="en">Zmarlicka M, Nailor M, Nicolau D. Impact of the New Delhi metallo-beta-lactamase on beta-lactam antibiotics. Infect Drug Resist. 2015; 8: 297-309. doi: 10.2147/IDR.S39186</mixed-citation></citation-alternatives></ref><ref id="cit50"><label>50</label><citation-alternatives><mixed-citation xml:lang="ru">Makena A, Duzgun AO, Brem J, McDonough MA, Rydzik AM, Abboud MI, et al. Comparison of Verona integron-Borne metallo-β-lactamase (VIM) variants reveals differences in stability and inhibition profiles. Antimicrob Agents Chemother. 2016; 60(3): 1377-1384. doi: 10.1128/AAC.01768-15</mixed-citation><mixed-citation xml:lang="en">Bahr G, Vitor-Horen L, Bethel ChR, Bonomo RA, Gonzalez LJ, Vila AJ. Clinical evolution of New Delhi metallo-β-lactamase (NDM) optimizes resistance under Zn(II) deprivation. Antimicrob Agents Chemother. 2017; 62(1): e01849-17. doi: 10.1128/AAC.01849-17</mixed-citation></citation-alternatives></ref><ref id="cit51"><label>51</label><citation-alternatives><mixed-citation xml:lang="ru">Zmarlicka M, Nailor M, Nicolau D. Impact of the New Delhi metallo-beta-lactamase on beta-lactam antibiotics. Infect Drug Resist. 2015; 8: 297-309. doi: 10.2147/IDR.S39186</mixed-citation><mixed-citation xml:lang="en">Weber RE, Pietsch M, Frühauf A, Pfeifer Y, Martin M, Luft D, et al. IS26-mediated transfer of blaNDM-1 as the main route of resistance transmission during a polyclonal, multispecies outbreak in a German hospital. Front Microbiol. 2019; 10: 2817. doi: 10.3389/fmicb.2019.02817</mixed-citation></citation-alternatives></ref><ref id="cit52"><label>52</label><citation-alternatives><mixed-citation xml:lang="ru">Bahr G, Vitor-Horen L, Bethel ChR, Bonomo RA, Gonzalez LJ, Vila AJ. Clinical evolution of New Delhi metallo-β-lactamase (NDM) optimizes resistance under Zn(II) deprivation. Antimicrob Agents Chemother. 2017; 62(1): e01849-17. doi: 10.1128/AAC.01849-17</mixed-citation><mixed-citation xml:lang="en">Adams MD, Pasteran F, Traglia GM, Martinez J, Huang F, Liu C, et al. Distinct mechanisms of dissemination of NDM-1 metallo-β-lactamase in Acinetobacter species in Argentina. Antimicrob Agents Chemother. 2020; 64(5): e00324-20. doi: 10.1128/AAC.00324-20</mixed-citation></citation-alternatives></ref><ref id="cit53"><label>53</label><citation-alternatives><mixed-citation xml:lang="ru">Weber RE, Pietsch M, Frühauf A, Pfeifer Y, Martin M, Luft D, et al. IS26-mediated transfer of blaNDM-1 as the main route of resistance transmission during a polyclonal, multispecies outbreak in a German hospital. Front Microbiol. 2019; 10: 2817. doi: 10.3389/fmicb.2019.02817</mixed-citation><mixed-citation xml:lang="en">Wendel AF, MacKenzie CR. Characterization of a novel metallo-β-lactamase variant, GIM-2, from a clinical isolate of Enterobacter cloacae in Germany. Antimicrob Agents Chemother. 2015; 59(3): 1824-1825. doi: 10.1128/AAC.05062-14</mixed-citation></citation-alternatives></ref><ref id="cit54"><label>54</label><citation-alternatives><mixed-citation xml:lang="ru">Adams MD, Pasteran F, Traglia GM, Martinez J, Huang F, Liu C, et al. Distinct mechanisms of dissemination of NDM-1 metallo-β-lactamase in Acinetobacter species in Argentina. Antimicrob Agents Chemother. 2020; 64(5): e00324-20. doi: 10.1128/AAC.00324-20</mixed-citation><mixed-citation xml:lang="en">Lu Y, Zhao S, Liang H, Zhang W, Liu J, Hu H. The first report of a novel IncHI1B blaSIM-1-carrying megaplasmid pSIM-1-BJ01 from a clinical Klebsiella pneumoniae isolate. Infect Drug Resist. 2019; 12: 2103-2112. doi: 10.2147/IDR.S212333</mixed-citation></citation-alternatives></ref><ref id="cit55"><label>55</label><citation-alternatives><mixed-citation xml:lang="ru">Wendel AF, MacKenzie CR. Characterization of a novel metallo-β-lactamase variant, GIM-2, from a clinical isolate of Enterobacter cloacae in Germany. Antimicrob Agents Chemother. 2015; 59(3): 1824-1825. doi: 10.1128/AAC.05062-14</mixed-citation><mixed-citation xml:lang="en">Zheng Z, Cheng Q, Chan EW‐C, Chen S. Genetic and biochemical characterization of VMB‐1, a novel metallo‐β‐lactamase encoded by a conjugative, broad‐host range IncC plasmid from Vibrio spp. Adv. Biosys. 2020; 4: 1900221. doi: 10.1002/adbi.201900221</mixed-citation></citation-alternatives></ref><ref id="cit56"><label>56</label><citation-alternatives><mixed-citation xml:lang="ru">Lu Y, Zhao S, Liang H, Zhang W, Liu J, Hu H. The first report of a novel IncHI1B blaSIM-1-carrying megaplasmid pSIM-1-BJ01 from a clinical Klebsiella pneumoniae isolate. Infect Drug Resist. 2019; 12: 2103-2112. doi: 10.2147/IDR.S212333</mixed-citation><mixed-citation xml:lang="en">Poirel L, Palmieri M, Brilhante M, Masseron A, Perreten V, Nordmann P. PFM-like enzymes are a novel family of subclass B2 metallo-β-lactamases fromPseudomonas synxanthabelonging to the Pseudomonas fluorescens complex Nordmann. Antimicrob Agents Chemother. 2020; 64(2): e01700-19. doi: 10.1128/AAC.01700-19</mixed-citation></citation-alternatives></ref><ref id="cit57"><label>57</label><citation-alternatives><mixed-citation xml:lang="ru">Zheng Z, Cheng Q, Chan EW‐C, Chen S. Genetic and biochemical characterization of VMB‐1, a novel metallo‐β‐ lactamase encoded by a conjugative, broad‐host range IncC plasmid from Vibrio spp. Adv. Biosys. 2020; 4: 1900221. doi: 10.1002/adbi.201900221</mixed-citation><mixed-citation xml:lang="en">Brem J, Struwe WB, Rydzik AM, et al. Studying the activesite loop movement of the São Paolo metallo-β-lactamase-1. Chem Sci. 2015; 6(2): 956-963. doi: 10.1039/c4sc01752h</mixed-citation></citation-alternatives></ref><ref id="cit58"><label>58</label><citation-alternatives><mixed-citation xml:lang="ru">Poirel L, Palmieri M, Brilhante M, Masseron A, Perreten V, Nordmann P. PFM-like enzymes are a novel family of subclass B2 metallo-β-lactamases from Pseudomonas synxantha belonging to the Pseudomonas fluorescens complex Nordmann. Antimicrob Agents Chemother. 2020; 64(2): e01700-19. doi: 10.1128/AAC.01700-19</mixed-citation><mixed-citation xml:lang="en">Lopez C, Ayala JA, Bonomo RA, et al. Protein determinants of dissemination and host specificity of metallo-β-lactamases. Nat Commun. 2019; 10: 3617. doi: 10.1038/s41467-019-11615-w</mixed-citation></citation-alternatives></ref><ref id="cit59"><label>59</label><citation-alternatives><mixed-citation xml:lang="ru">Brem J, Struwe WB, Rydzik AM, et al. Studying the activesite loop movement of the São Paolo metallo-β- lactamase-1. Chem Sci. 2015; 6(2): 956-963. doi: 10.1039/c4sc01752h</mixed-citation><mixed-citation xml:lang="en">Jabalameli F, Taki E, Emaneini M, Beigverdi R. Prevalence of metallo-β-lactamase-encoding genes among carbapenemresistant Pseudomonas aeruginosa strains isolated from burn patients in Iran. Rev Soc Bras Med Trop. 2018; 51(3): 270-276. doi: 10.1590/0037-8682-0044-2018</mixed-citation></citation-alternatives></ref><ref id="cit60"><label>60</label><citation-alternatives><mixed-citation xml:lang="ru">Lopez C, Ayala JA, Bonomo RA, et al. Protein determinants of dissemination and host specificity of metallo-β-lactamases. Nat Commun. 2019; 10: 3617. doi: 10.1038/s41467-019-11615-w</mixed-citation><mixed-citation xml:lang="en">Smith CA, Stewart NK, Toth M, Vakulenko SB. Structural insights into the mechanism of carbapenemase activity of the OXA-48 β-lactamase. Antimicrob Agents Chemother. 2019; 63(10): e01202-19. doi: 10.1128/AAC.01202-19</mixed-citation></citation-alternatives></ref><ref id="cit61"><label>61</label><citation-alternatives><mixed-citation xml:lang="ru">Jabalameli F, Taki E, Emaneini M, Beigverdi R. Prevalence of metallo-β-lactamase-encoding genes among carbapenemresistant Pseudomonas aeruginosa strains isolated from burn patients in Iran. Rev Soc Bras Med Trop. 2018; 51(3): 270-276. doi: 10.1590/0037-8682-0044-2018</mixed-citation><mixed-citation xml:lang="en">Pasteran F, Denorme L, Ote I, et al. Rapid identification of OXA-48 and OXA-163 subfamilies in carbapenem-resistant gram-negative Bacilli with a novel immunochromatographic lateral flow assay. J Clin Microbiol. 2016; 54(11): 2832-2836. doi: 10.1128/JCM.01175-16</mixed-citation></citation-alternatives></ref><ref id="cit62"><label>62</label><citation-alternatives><mixed-citation xml:lang="ru">Smith CA, Stewart NK, Toth M, Vakulenko SB. Structural insights into the mechanism of carbapenemase activity of the OXA-48 β-lactamase. Antimicrob Agents Chemother. 2019; 63(10): e01202-19. doi: 10.1128/AAC.01202-19</mixed-citation><mixed-citation xml:lang="en">Doi Y. Treatment options for carbapenem-resistant gramnegative bacterial infections. Clin Infect Dis. 2019; 69(7): S565-S575. doi: 10.1093/cid/ciz830</mixed-citation></citation-alternatives></ref><ref id="cit63"><label>63</label><citation-alternatives><mixed-citation xml:lang="ru">Pasteran F, Denorme L, Ote I, et al. Rapid identification of OXA-48 and OXA-163 subfamilies in carbapenem-resistant gram-negative Bacilli with a novel immunochromatographic lateral flow assay. J Clin Microbiol. 2016; 54(11): 2832-2836. doi: 10.1128/JCM.01175-16</mixed-citation><mixed-citation xml:lang="en">Joshi PR, Acharya M, Kakshapati T, et al. Co-existence of bla OXA-23 and blaNDM-1 genes of Acinetobacter baumannii isolated from Nepal: Antimicrobial resistance and clinical significance. Antimicrob Resist Infect Control. 2017; 6(21). doi: 10.1186/s13756-017-0180-5</mixed-citation></citation-alternatives></ref><ref id="cit64"><label>64</label><citation-alternatives><mixed-citation xml:lang="ru">Doi Y. Treatment options for carbapenem-resistant gramnegative bacterial infections. Clin Infect Dis. 2019; 69(7): S565-S575. doi: 10.1093/cid/ciz830</mixed-citation><mixed-citation xml:lang="en">Kuzmenkov AYu, Trushin IV, Avramenko AA, Eidelshtein MV, Dekhnich AV, Kozlov RS. Amrmap: online platform for monitoring antibiotic resistance. КМАХ. 2017. 19(2): 84-90. (In Russ.)</mixed-citation></citation-alternatives></ref><ref id="cit65"><label>65</label><citation-alternatives><mixed-citation xml:lang="ru">Joshi PR, Acharya M, Kakshapati T, et al. Co-existence of bla OXA-23 and blaNDM-1 genes of Acinetobacter baumannii isolated from Nepal: Antimicrobial resistance and clinical significance. Antimicrob Resist Infect Control. 2017; 6(21). doi: 10.1186/s13756-017-0180-5</mixed-citation><mixed-citation xml:lang="en">Baeza LL, Pfennigwerth N, Greissl C, Gottig S, Saleh A, Stelzer Y, et al. Comparison of five methods for detection of carbapenemases in Enterobacterales with proposal of a new algorithm. Clin Microbiol Infect. 2019; 25(10): 1286.e9-1286.e15. doi: 10.1016/j.cmi.2019.03.003</mixed-citation></citation-alternatives></ref><ref id="cit66"><label>66</label><citation-alternatives><mixed-citation xml:lang="ru">Кузьменков А.Ю., Трушин И.В., Авраменко А.А., Эйдельштейн М.В., Дехнич А.В., Козлов Р.С. Amrmap: интернетплатформа мониторинга антибиотикорезистентности. КМАХ. 2017. 19(2): 84-90.</mixed-citation><mixed-citation xml:lang="en">Zhivich A. Fighting bacterial resistance: Approaches, challenges, and opportunities in the search for new antibiotics. Part 1. Antibiotics used in clinical practice: mechanisms of action and the development of bacterial resistance. The Microbiology Independent Research (MIR) journal. 2017; 4(1): 31-51. doi: 10.18527/2500-2236-2017-4-1-31-51</mixed-citation></citation-alternatives></ref><ref id="cit67"><label>67</label><citation-alternatives><mixed-citation xml:lang="ru">Baeza LL, Pfennigwerth N, Greissl C, Gottig S, Saleh A, Stelzer Y, et al. Comparison of five methods for detection of carbapenemases in Enterobacterales with proposal of a new algorithm. Clin Microbiol Infect. 2019; 25(10): 1286.e9-1286.e15. doi: 10.1016/j.cmi.2019.03.003</mixed-citation><mixed-citation xml:lang="en">Lohans CT, Groesen E van, Kumar K, Tooke CL, Spencer J, Paton RS, et al. A new mechanism for β‐ lactamases: Class D enzymes degrade 1β‐methyl carbapenems through lactone formation. Angew Chem Int Ed Engl. 2018; 57: 1282. doi: 10.1002/anie.201711308</mixed-citation></citation-alternatives></ref><ref id="cit68"><label>68</label><citation-alternatives><mixed-citation xml:lang="ru">Zhivich A. Fighting bacterial resistance: Approaches, challenges, and opportunities in the search for new antibiotics. Part 1. Antibiotics used in clinical practice: mechanisms of action and the development of bacterial resistance. The Microbiology Independent Research (MIR) journal. 2017; 4(1): 31-51. doi: 10.18527/2500-2236-2017-4-1-31-51</mixed-citation><mixed-citation xml:lang="en">Shurygina IA, Prozorova GF, Trukhan IS, Korzhova SA, Fadeeva TV, Pozdnyakov AS, et al. NonToxic Silver/Poly-1-Vinyl-1,2,4-Triazole. Nanomaterials. 2020; 10(8): 1477. doi: 10.3390/nano10081477/</mixed-citation></citation-alternatives></ref><ref id="cit69"><label>69</label><citation-alternatives><mixed-citation xml:lang="ru">Lohans CT, Groesen E van, Kumar K, Tooke CL, Spencer J, Paton RS, et al. A new mechanism for β‐ lactamases: Class D enzymes degrade 1β‐methyl carbapenems through lactone formation. Angew Chem Int Ed Engl. 2018; 57: 1282. doi: 10.1002/anie.201711308</mixed-citation><mixed-citation xml:lang="en">Williamson DA, Carter GP, Howden BP. Current and emerging topical antibacterials and antiseptics: Agents, action, and resistance patterns. Clin Microbiol Rev. 2017; 30(3): 827-860. doi: 10.1128/CMR.00112-16</mixed-citation></citation-alternatives></ref><ref id="cit70"><label>70</label><citation-alternatives><mixed-citation xml:lang="ru">Shurygina IA, Prozorova GF, Trukhan IS, Korzhova SA, Fadeeva TV, Pozdnyakov AS, et al. NonToxic Silver/Poly-1-Vinyl-1,2,4-Triazole. Nanomaterials. 2020; 10(8): 1477. doi: 10.3390/nano10081477/</mixed-citation><mixed-citation xml:lang="en">Belete TM. Novel targets to develop new antibacterial agents and novel alternatives to antibacterial agents. Hum Microb J. 2019; 11: 100052. doi: 10.1016/j.humic.2019.01.001</mixed-citation></citation-alternatives></ref><ref id="cit71"><label>71</label><citation-alternatives><mixed-citation xml:lang="ru">Williamson DA, Carter GP, Howden BP. Current and emerging topical antibacterials and antiseptics: Agents, action, and resistance patterns. Clin Microbiol Rev. 2017; 30(3): 827-860. doi: 10.1128/CMR.00112-16</mixed-citation><mixed-citation xml:lang="en">Beloborodov VB, Gusarov VG, Dekhnich AV, Zamiatin MN, Zubareva NA, Zyrianov SK, et al. Diagnostics and antimicrobial therapy of infections caused by multidrug-resistant microorganisms: Guidelines of the Russian non-profit public organization «Association of Anesthesiologists and Resuscitators», Interregional Public Organization «Alliance of Clinical Chemotherapists and Microbiologists», Interregional Association for Clinical Microbiology and Antimicrobial Organization (МАКМАХ) Sepsis Forum». Messenger of Anesthesiology and Resuscitaion. 2020; 17(1): 52-83. (In Russ.)</mixed-citation></citation-alternatives></ref><ref id="cit72"><label>72</label><citation-alternatives><mixed-citation xml:lang="ru">Belete TM. Novel targets to develop new antibacterial agents and novel alternatives to antibacterial agents. Hum Microb J. 2019; 11: 100052. doi: 10.1016/j.humic.2019.01.001</mixed-citation><mixed-citation xml:lang="en">Lazareva IV, Ageevets VA, Ershova TA, Zueva LP, Goncharov AE, Daryina MG, et al. Distribution and antibacterial resistance of gram-negative bacteria, producers of carbapenemases, in St. Petersburg and some other regions of the Russian Federation. Antibiotics and Chemotherapy. 2016; 61(11-12): 28-38. (In Russ.)</mixed-citation></citation-alternatives></ref><ref id="cit73"><label>73</label><citation-alternatives><mixed-citation xml:lang="ru">Белобородов В.Б., Гусаров В.Г., Дехнич А.В., Замятин М.Н., Зубарева Н.А., Зырянов С.К. и др. Диагностика и антимикробная терапия инфекций, вызванных полирезистентными микроорганизмами: методические рекомендации Российской некоммерческой общественной организации «Ассоциация анестезиологов-реаниматологов», Межрегиональной общественной организации «Альянс клинических химиотерапевтов и микробиологов», Межрегиональной ассоциации по клинической микробиологии и антимикробной химиотерапии (МАКМАХ), Общественной организации «Российский Сепсис Форум». Вестник анестезиологии и реаниматологии. 2020; 17 (1): 52-83.</mixed-citation><mixed-citation xml:lang="en">Pagano M, Martins AF, Barth AL. Mobile genetic elements related to carbapenem resistance in Acinetobacter baumannii. Braz J Microbiol. 2016; 47(4): 785-792. doi: 10.1016/j.bjm.2016.06.005</mixed-citation></citation-alternatives></ref><ref id="cit74"><label>74</label><citation-alternatives><mixed-citation xml:lang="ru">Лазарева И.В., Агеевец В.А., Ершова Т.А., Зуева Л.П., Гончаров А.Е., Дарьина М.Г. и др. Распространение и антибактериальная резистентность грамотрицательных бактерий, продуцентов карбапенемаз, в Санкт-Петербурге и некоторых других регионах Российской Федерации. Антибиотики и химиотерапия. 2016; 61 (11-12): 28-38.</mixed-citation><mixed-citation xml:lang="en">Shek EA, Sukhorukova MV, Edelstein MV, Skleenova EYu, Ivanchik NV, Shajdullina ER, et al. Antimicrobial resistance, carbapenemase production, and genotypes of nosocomial Pseudomonas aeruginosa isolates in Russia: Results of multicenter epidemiological study “MARATHON 2015–2016”. Clinical Microbiology and Antimicrobial Chemotherapy. 2019; 21(2): 160-170. doi: 10.36488/cmac.2019.2.160-170</mixed-citation></citation-alternatives></ref><ref id="cit75"><label>75</label><citation-alternatives><mixed-citation xml:lang="ru">Pagano M, Martins AF, Barth AL. Mobile genetic elements related to carbapenem resistance in Acinetobacter baumannii. Braz J Microbiol. 2016; 47(4): 785-792. doi: 10.1016/j.bjm.2016.06.005</mixed-citation><mixed-citation xml:lang="en">Bonomo RA, Burd EM, Conly J, Limbago BM, Poirel L, Segre JA, et al. Carbapenemase-producing organisms: A global scourge. Clin Infect Dis. 2018; 66(8): 1290-1297. doi: 10.1093/cid/cix893</mixed-citation></citation-alternatives></ref><ref id="cit76"><label>76</label><citation-alternatives><mixed-citation xml:lang="ru">Shek EA, Sukhorukova MV, Edelstein MV, Skleenova EYu, Ivanchik NV, Shajdullina ER, et al. Antimicrobial resistance, carbapenemase production, and genotypes of nosocomial Pseudomonas aeruginosa isolates in Russia: Results of multicenter epidemiological study “MARATHON 2015–2016”. Clinical Microbiology and Antimicrobial Chemotherapy. 2019; 21(2): 160-170. doi: 10.36488/cmac.2019.2.160-170</mixed-citation><mixed-citation xml:lang="en">Shek EA, Sukhorukova MV, Edelstein MV, Skleenova EYu, Ivanchik NV, Shajdullina ER, et al. Antimicrobial resistance, carbapenemase production, and genotypes of nosocomial Pseudomonas aeruginosa isolates in Russia: Results of multicenter epidemiological study “MARATHON 2015–2016”. Clinical Microbiology and Antimicrobial Chemotherapy. 2019; 21(2): 160-170. doi: 10.36488/cmac.2019.2.160-170</mixed-citation></citation-alternatives></ref><ref id="cit77"><label>77</label><citation-alternatives><mixed-citation xml:lang="ru">Bonomo RA, Burd EM, Conly J, Limbago BM, Poirel L, Segre JA, et al. Carbapenemase-producing organisms: A global scourge. Clin Infect Dis. 2018; 66(8): 1290-1297. doi: 10.1093/cid/cix893</mixed-citation><mixed-citation xml:lang="en">Bonomo RA, Burd EM, Conly J, Limbago BM, Poirel L, Segre JA, et al. Carbapenemase-producing organisms: A global scourge. Clin Infect Dis. 2018; 66(8): 1290-1297. doi: 10.1093/cid/cix893</mixed-citation></citation-alternatives></ref></ref-list><fn-group><fn fn-type="conflict"><p>The authors declare that there are no conflicts of interest present.</p></fn></fn-group></back></article>
