scholarly journals Characterization of blaKPC-2-Carrying Plasmid pR31-KPC from a Pseudomonasaeruginosa Strain Isolated in China

Antibiotics ◽  
2021 ◽  
Vol 10 (10) ◽  
pp. 1234
Author(s):  
Min Yuan ◽  
Hongxia Guan ◽  
Dan Sha ◽  
Wenting Cao ◽  
Xiaofeng Song ◽  
...  

This work aimed to characterize a 29-kb blaKPC-2-carrying plasmid, pR31-KPC, from a multidrug resistant strain of Pseudomonas aeruginosa isolated from the sputum of an elderly patient with multiple chronic conditions in China. The backbone of pR31-KPC is closely related to four other blaKPC-2-carrying plasmids, YLH6_p3, p1011-KPC2, p14057A, and pP23-KPC, none of which have been assigned to any of the known incompatibility groups. Two accessory modules, the IS26-blaKPC-2-IS26 unit and IS26-ΔTn6376-IS26 region, separated by a 5.9-kb backbone region, were identified in pR31-KPC, which was also shown to carry the unique resistance marker blaKPC-2. A comparative study of the above five plasmids showed that p1011-KPC2 may be the most complete plasmid of this group to be reported, while pR31-KPC is the smallest plasmid having lost most of its conjugative region. Regions between the iterons and orf207 in the backbone may be hot spots for the acquisition of exogenous resistance entities. The accessory regions of these plasmids have all undergone several biological events when compared with Tn6296. The further transfer of blaKPC-2 in these plasmids may be initiated by either the Tn3 family or IS26-associated transposition or homologous recombination. The data presented here will contribute to a deeper understanding of blaKPC-2 carrying plasmids in Pseudomonas.

2020 ◽  
Vol 27 (11) ◽  
pp. 2955-2960
Author(s):  
Xiaojuan Wu ◽  
Dunia A. Al Farraj ◽  
Jayarajapazham Rajaselvam ◽  
Roua M. Alkufeidy ◽  
Ponnuswamy Vijayaraghavan ◽  
...  

Biologicals ◽  
2020 ◽  
Vol 63 ◽  
pp. 89-96 ◽  
Author(s):  
Muhammad Adnan ◽  
Muhammad Rahman Ali Shah ◽  
Muhsin Jamal ◽  
Fazal Jalil ◽  
Saadia Andleeb ◽  
...  

PLoS ONE ◽  
2013 ◽  
Vol 8 (8) ◽  
pp. e70557 ◽  
Author(s):  
Kanao Kobayashi ◽  
Ikue Hayashi ◽  
Syuntaro Kouda ◽  
Fuminori Kato ◽  
Tamaki Fujiwara ◽  
...  

2012 ◽  
Vol 2 (1) ◽  
Author(s):  
C. Formosa ◽  
M. Grare ◽  
E. Jauvert ◽  
A. Coutable ◽  
J. B. Regnouf-de-Vains ◽  
...  

2021 ◽  
Author(s):  
Nathan B Pincus ◽  
Monica Rosas-Lemus ◽  
Samuel WM Gatesy ◽  
Ludmilla A. Shuvalova ◽  
Joseph Brunzelle ◽  
...  

Resistance to antipseudomonal penicillins and cephalosporins is often driven by the overproduction of the intrinsic β-lactamase AmpC. However, OXA-10-family β-lactamases are a rich source of resistance in Pseudomonas aeruginosa. OXA β-lactamases have a propensity for mutation leading to extended spectrum cephalosporinase and carbapenemase activity. In this study, we identified isolates from a subclade of the multidrug-resistant (MDR) high risk clonal complex CC446 with resistance to ceftazidime. Genomic analysis revealed that these isolates harbored a plasmid containing a novel allele of blaOXA-10, named blaOXA-935, which was predicted to produce an OXA-10 variant with two amino acid substitutions: an aspartic acid instead of glycine at position 157 and a serine instead of phenylalanine at position 153. The G157D mutation, present in OXA-14, is associated with resistance to ceftazidime. Deletion of blaOXA-935 restored sensitivity to ceftazidime and susceptibility profiling of P. aeruginosa laboratory strains expressing blaOXA-935 revealed that OXA-935 conferred ceftazidime resistance. To better understand the impact of the variant amino acids, we determined the crystal structures of OXA-14 and OXA-935. In contrast, both monomers of OXA-935 were decarbamylated at K70, and the F153S mutation conferred increased flexibility to the omega (Ω) loop. Compared to OXA-14, the catalytic efficiency of OXA-935 for nitrocefin was significantly reduced. Amino acid changes that confer extended spectrum cephalosporinase activity to OXA-10-family β-lactamases are concerning given rising reliance on novel β-lactam/β-lactamase inhibitor combinations such as ceftolozane-tazobactam and ceftazidime-avibactam to treat MDR P. aeruginosa infections.


2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Sonika Sharma ◽  
Sibnarayan Datta ◽  
Soumya Chatterjee ◽  
Moumita Dutta ◽  
Jhuma Samanta ◽  
...  

AbstractIn recent years, the use of bacteriophages (or 'phages') against multidrug-resistant (MDR) bacteria including Pseudomonas aeruginosa has drawn considerable attention, globally. In this work, we report the isolation and detailed characterization of a highly lytic Pseudomonasphage DRL-P1 isolated from wastewater. Under TEM, DRL-P1 appeared as a member of the phage family Myoviridae. DRL-P1 featured rapid adsorption (~ 5 min), short-latency (~ 30 min), and large burst size (~ 100 PFU per infected cell). DRL-P1 can withstand a wide temperature range (4 °C to 40 °C) and pH (5.0 to 10.0) conditions. The 66,243 bp DRL-P1 genome (MN564818) encodes at least 93 ORFs, of which 36 were functionally annotated based on homology with similar phage proteins available in the databases. Comparative analyses of related genomes suggest an independent evolutionary history and discrete taxonomic position of DRL-P1 within genus Pbunavirus. No toxin or antibiotic resistance genes was identified. DRL-P1 is tolerant to lyophilization and encapsulation techniques and retained lytic activity even after 18 months of storage. We also demonstrated decontaminating potentials of DRL-P1 in vitro, on an artificially contaminated cover-slip model. To the best of our knowledge, this is the first Pbunavirus to be reported from India. Our study suggests DRL-P1 as a potential candidate for various applications.


2021 ◽  
Vol 10 (32) ◽  
Author(s):  
Baha Abdalhamid ◽  
Itidal Reslane ◽  
Emily Mccutchen ◽  
Peter C. Iwen

Multidrug-resistant Pseudomonas aeruginosa is a serious threat worldwide causing health care-acquired infections and is associated with significant morbidity and mortality. This report describes the draft genome sequences of five multidrug-resistant Pseudomonas aeruginosa strains isolated from human infections.


2015 ◽  
Vol 172 ◽  
pp. 68-78 ◽  
Author(s):  
Sara A. Ochoa ◽  
Ariadnna Cruz-Córdova ◽  
Gerardo E. Rodea ◽  
Vicenta Cázares-Domínguez ◽  
Gerardo Escalona ◽  
...  

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