Enterobacteria producing extended-spectrum β-lactamases and IMP-1 metallo-β-lactamases isolated from Brazilian hospitals

Lincopán, Nilton; Leis, Renato; Vianello, Marco A.; Araújo, Maria; Ruiz, Alice S.; Mamizuka, Elsa Masae

doi:10.1099/jmm.0.46771-0

Cited by 26 publications

(24 citation statements)

References 11 publications

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“…The work of Lincopan et al described the presence of IMP-1 in a K. pneumoniae strain detected in a patient from a university hospital from São Paulo, located at the Southeast of Brazil 49 . The same IMP-1-producing K. pneumoniae strain was detected in six distinct hospitals of the city of São Paulo between the years 2003 and 2005 50 . In one of these hospitals, it was responsible for causing an outbreak in an intensive care unit 51 .…”

Section: The Rise Of Carbapenemases In Brazilmentioning

confidence: 97%

Antimicrobial resistance in Enterobacteriaceae in Brazil: focus on β-lactams and polymyxins

Sampaio

Gales

2016

Brazilian Journal of Microbiology

111

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During the last 30 years there has been a dissemination of plasmid-mediated β-lactamases in Enterobacteriaceae in Brazil. Extended spectrum β-lactamases (ESBL) are widely disseminated in the hospital setting and are detected in a lower frequency in the community setting. Cefotaximases are the most frequently detected ESBL type and Klebsiella pneumoniae is the predominant species among ESBL producers. Klebsiella pneumoniae carbapenemase-producing Enterobacteriaceae became widely disseminated in Brazil during the last decade and KPC production is currently the most frequent resistance mechanism (96.2%) in carbapenem resistant K. pneumoniae. To date KPC-2 is the only variant reported in Brazil. Polymyxin B resistance in KPC-2-producing K. pneumoniae has come to an alarming rate of 27.1% in 2015 in São Paulo, the largest city in Brazil. New Delhi metallo-β-lactamase was detected in Brazil in 2013, has been reported in different Brazilian states but are not widely disseminated. Antimicrobial resistance in Enterobacteriaceae in Brazil is a very serious problem that needs urgent actions which includes both more strict adherence to infection control measures and more judicious use of antimicrobials.

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Section: The Rise Of Carbapenemases In Brazilmentioning

confidence: 97%

Antimicrobial resistance in Enterobacteriaceae in Brazil: focus on β-lactams and polymyxins

Sampaio

Gales

2016

Brazilian Journal of Microbiology

111

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“…P. stuartii produces a chromosomally encoded cephalosporinase, AmpC, which causes the natural resistance to aminopenicillins and narrow-spectrum cephalosporins (5). The productions of different extended-spectrum ␤-lactamases (6,7,8,9,10,11) and metallo-␤-lactamases (12,13,14) have been reported in association with resistance to carbapenems in Providencia spp. Other enzymatic mechanisms of antibiotic resistance identified in P. stuartii include acetyl aminotransferases targeting aminoglycoside antibiotics and an integronencoded erythromycin esterase involved in the resistance to macrolides (15,16).…”

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confidence: 99%

Implication of Porins in β-Lactam Resistance of Providencia stuartii

Tran

Mahendran

Hajjar

et al. 2010

Journal of Biological Chemistry

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An integrative approach combining biophysical and microbiological methods was used to characterize the antibiotic translocation through the outer membrane of Providencia stuartii. Two novel members of the General Bacterial Porin family of Enterobacteriaceae, named OmpPst1 and OmpPst2, were identified in P. stuartii. In the presence of ertapenem (ERT), cefepime (FEP), and cefoxitin (FOX) in growth media, several resistant derivatives of P. stuartii ATCC 29914 showed OmpPst1-deficiency. These porin-deficient strains showed significant decrease of susceptibility to ␤-lactam antibiotics. OmpPst1 and OmpPst2 were purified to homogeneity and reconstituted into planar lipid bilayers to study their biophysical characteristics and their interactions with ␤-lactam molecules. Determination of ␤-lactam translocation through OmpPst1 and OmpPst2 indicated that the strength of interaction decreased in the order of ertapenem Ͼ Ͼ cefepime > cefoxitin. Moreover, the translocation of these antibiotics through OmpPst1 was more efficient than through OmpPst2. Heterologous expression of OmpPst1 in the porin-deficient E. coli strain BL21(DE3)omp8 was associated with a higher antibiotic susceptibility of the E. coli cells to ␤-lactams compared with expression of OmpPst2. All our data enlighten the involvement of porins in the resistance of P. stuartii to ␤-lactam antibiotics.Providencia stuartii is an opportunistic pathogen involved in community-acquired as well as hospital-acquired infectious diseases. Clinical strains of P. stuartii are mostly isolated from urinary tract infections of patients with long-term indwelling urinary catheters and, in fewer cases, from respiratory and skin infections (1, 2). P. stuartii is reported as one of the most resistant species in the family of Enterobacteriaceae (3). P. stuartii strains show high levels of resistance to the majority of antibiotic classes but were found to remain susceptible to carbapenems (3, 4). P. stuartii produces a chromosomally encoded cephalosporinase, AmpC, which causes the natural resistance to aminopenicillins and narrow-spectrum cephalosporins (5). The productions of different extended-spectrum ␤-lactamases (6, 7, 8, 9, 10, 11) and metallo-␤-lactamases (12, 13, 14) have been reported in association with resistance to carbapenems in Providencia spp. Other enzymatic mechanisms of antibiotic resistance identified in P. stuartii include acetyl aminotransferases targeting aminoglycoside antibiotics and an integronencoded erythromycin esterase involved in the resistance to macrolides (15, 16). Moreover, mutations of the gyrA gene leading to a modification of target site were described in resistance to fluoroquinolones (17). In contrast, little is known about the involvement of membrane proteins in antibiotic resistance of P. stuartii. One study suggested a role of outer membrane porins in antibiotic permeability for Proteus, Morganella, and Providencia strains by selection of mutants resistant to cefoxitin, a cephalosporin of the second generation (18). However, the authors sugg...

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“…Desde então, nessa região, os membros da família Enterobactériaceae têm sido relacionados apenas com esta MBL e à presença da serino carbapenemase KPC-2 (Lincopan et al, 2005, Villegas et al, 2006e Pasteran et al 2008, Peirano et al, 2009, Monteiro et al, 2009 (Penteado, 2007, Lincopan et al, 2006Grimbaum, et al, 2004 ), no entanto, não foi confirmada a localização do gene no plasmideo, uma vez que a transformação de DH10B e o DNA plasmidial extraído das cepas produtoras de IMP-1 não foi realizada com êxito.…”

Section: Discussionunclassified

“…No Brasil, em abril de 2003, identificou-se o primeiro isolado de metalo-β-lactamase produzida por Klebsiella pneumoniae (Lincopan et al, 2005), sendo o primeiro relato de diversos isolados que apresentaram um padrão de resistência similar, mostrando, dessa forma, o surgimento de novos determinantes de resistência em hospitais brasileiros (Lincopan et al, 2006, Peirano et al, 2009, Zavazcki, et al, 2009). …”

Section: Hiperprodutor De Ampc Cromossomoal (Turner 2009) Em Relaçãounclassified

“…i) elementos que se movem de uma bactéria a outra, denominados plasmídios conjugativos ou elementos de transferência horizontal e ii) elementos que se mobilizam no genoma de uma mesma célula através de recombinação por meio dos transposons, denominados genes cassete (Bennett, 2008 (Lincopan et al, 2006).…”

Section: Contexto Genético De Aquisição E Disseminação De Determinantunclassified

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Caracterização molecular da resistência aos carbapenêmicos em enterobactérias isoladas em hospitais brasileiros

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Enterobacteria producing extended-spectrum β-lactamases and IMP-1 metallo-β-lactamases isolated from Brazilian hospitals

Cited by 26 publications

References 11 publications

Antimicrobial resistance in Enterobacteriaceae in Brazil: focus on β-lactams and polymyxins

Antimicrobial resistance in Enterobacteriaceae in Brazil: focus on β-lactams and polymyxins

Implication of Porins in β-Lactam Resistance of Providencia stuartii

Caracterização molecular da resistência aos carbapenêmicos em enterobactérias isoladas em hospitais brasileiros

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