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      High frequency of the exoU+/ exoS+ genotype associated with multidrug-resistant “high-risk clones” of Pseudomonas aeruginosa clinical isolates from Peruvian hospitals

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          Abstract

          The type III secretion system of Pseudomonas aeruginosa is an important virulence factor contributing to the cytotoxicity and the invasion process of this microorganism. The current study aimed to determine the presence of the exoU+/ exoS+ genotype in P. aeruginosa clinical isolates. The presence of exoS, exoT, exoU and exoY was determined in 189 P. aeruginosa by PCR, and the presence/absence of exoU was analysed according to source infection, clonal relationships, biofilm formation, motility and antimicrobial susceptibility. The gyrA, parC, oprD, efflux pump regulators and β-lactamases genes were also analysed by PCR/sequencing. The exoS, exoT and exoY genes were found in 100% of the isolates. Meanwhile, exoU was present in 43/189 (22.8%) of the isolates, being significantly associated with multidrug resistance, extensively drug resistance as well as with higher level quinolone resistance. However, the presence of β-lactamases, mutations in gyrA and parC, and relevant modifications in efflux pumps and OprD were not significantly associated with exoU+ isolates. MLST analysis of a subset of 25 isolates showed 8 different STs displaying the exoU+/ exoS+ genotype. The MDR basis of the exoU+ isolates remain to be elucidated. Furthermore, the clinical implications and spread of exoU+/ exoSP. aeruginosa isolates need to be established.

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          Carbapenemases: the versatile beta-lactamases.

          Carbapenemases are beta-lactamases with versatile hydrolytic capacities. They have the ability to hydrolyze penicillins, cephalosporins, monobactams, and carbapenems. Bacteria producing these beta-lactamases may cause serious infections in which the carbapenemase activity renders many beta-lactams ineffective. Carbapenemases are members of the molecular class A, B, and D beta-lactamases. Class A and D enzymes have a serine-based hydrolytic mechanism, while class B enzymes are metallo-beta-lactamases that contain zinc in the active site. The class A carbapenemase group includes members of the SME, IMI, NMC, GES, and KPC families. Of these, the KPC carbapenemases are the most prevalent, found mostly on plasmids in Klebsiella pneumoniae. The class D carbapenemases consist of OXA-type beta-lactamases frequently detected in Acinetobacter baumannii. The metallo-beta-lactamases belong to the IMP, VIM, SPM, GIM, and SIM families and have been detected primarily in Pseudomonas aeruginosa; however, there are increasing numbers of reports worldwide of this group of beta-lactamases in the Enterobacteriaceae. This review updates the characteristics, epidemiology, and detection of the carbapenemases found in pathogenic bacteria.
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            Multiplex PCR for rapid detection of genes encoding acquired metallo-beta-lactamases.

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              Imipenem-EDTA disk method for differentiation of metallo-beta-lactamase-producing clinical isolates of Pseudomonas spp. and Acinetobacter spp.

              Rapid detection of metallo-beta-lactamase (MBL)-producing gram-negative bacilli is necessary to prevent their dissemination. The method using a disk with imipenem plus 750 micro g of EDTA differentiated all MBL-producing pseudomonads, and the sensitivity and specificity for acinetobacters were 95.7 and 91.0%, respectively. The imipenem-EDTA disks were stable for 12 and 16 weeks at 4 and -20 degrees C, respectively.
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                Author and article information

                Contributors
                gertrudis.horna@isglobal.org
                joruiz.trabajo@gmail.com
                Journal
                Sci Rep
                Sci Rep
                Scientific Reports
                Nature Publishing Group UK (London )
                2045-2322
                26 July 2019
                26 July 2019
                2019
                : 9
                : 10874
                Affiliations
                [1 ]ISNI 0000 0000 9635 9413, GRID grid.410458.c, Barcelona Institute for Global Health, ISGlobal, Hospital Clinic - Universitat de Barcelona, ; Barcelona, Spain
                [2 ]GRID grid.441721.5, Universidad Catolica los Angeles de Chimbote, Instituto de Investigacion, ; Chimbote, Peru
                [3 ]ISNI 0000 0001 0673 9488, GRID grid.11100.31, Universidad Peruana Cayetano Heredia, Instituto de Medicina Tropical Alexander von Humboldt, ; Lima, Peru
                [4 ]GRID grid.414881.0, Hospital Nacional Cayetano Heredia, ; Lima, Peru
                [5 ]Universidad Continental, Lima, Peru
                Author information
                http://orcid.org/0000-0001-8974-7044
                http://orcid.org/0000-0002-2617-053X
                http://orcid.org/0000-0002-4431-2036
                Article
                47303
                10.1038/s41598-019-47303-4
                6659710
                31350412
                57cc4773-943f-4cc8-888e-260d674aaba2
                © The Author(s) 2019

                Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

                History
                : 18 January 2019
                : 15 July 2019
                Funding
                Funded by: FundRef https://doi.org/10.13039/100002322, Schlumberger Foundation;
                Funded by: FundRef https://doi.org/10.13039/501100004587, Ministry of Economy and Competitiveness | Instituto de Salud Carlos III (Institute of Health Carlos III);
                Award ID: CES11/012
                Award Recipient :
                Categories
                Article
                Custom metadata
                © The Author(s) 2019

                Uncategorized
                antimicrobial resistance,molecular biology
                Uncategorized
                antimicrobial resistance, molecular biology

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