Relevant bibliographies by topics / Metallo-B-lactamase genes

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Academic literature on the topic 'Metallo-B-lactamase genes'

Author: Grafiati
Published: 18 May 2024

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Journal articles on the topic "Metallo-B-lactamase genes"

1

Garau, Gianpiero, Anne Marie Di Guilmi, and Barry G. Hall. "Structure-Based Phylogeny of the Metallo-β-Lactamases." Antimicrobial Agents and Chemotherapy 49, no. 7 (July 2005): 2778–84. http://dx.doi.org/10.1128/aac.49.7.2778-2784.2005.

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ABSTRACTThe metallo-β-lactamases fall into two groups: Ambler class B subgroups B1 and B2 and Ambler class B subgroup B3. The two groups are so distantly related that there is no detectable sequence homology between members of the two different groups, but homology is clearly detectable at the protein structure level. The multiple structure alignment program MAPS has been used to align the structures of eight metallo-β-lactamases and five structurally homologous proteins from the metallo-β-lactamase superfamily, and that alignment has been used to construct a phylogenetic tree of the metallo-β-lactamases. The presence of genes fromEubacteria,Archaebacteria, andEukaryotaon that tree is consistent with a very ancient origin of the metallo-β-lactamase family.
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2

Matsumoto, Takehisa, Mika Nagata, Nau Ishimine, Kenji Kawasaki, Kazuyoshi Yamauchi, Eiko Hidaka, Eriko Kasuga, et al. "Characterization of CIA-1, an Ambler Class A Extended-Spectrum β-Lactamase from Chryseobacterium indologenes." Antimicrobial Agents and Chemotherapy 56, no. 1 (November 14, 2011): 588–90. http://dx.doi.org/10.1128/aac.05165-11.

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ABSTRACTAn Ambler class A β-lactamase gene,blaCIA-1, was cloned from the reference strainChryseobacterium indologenesATCC 29897 and expressed inEscherichia coliBL21. TheblaCIA-1gene encodes a novel extended-spectrum β-lactamase (ESBL) that shared 68% and 60% identities with the CGA-1 and CME-1 β-lactamases, respectively.blaCIA-1-like genes were detected from clinical isolates. In addition to the metallo-β-lactamase IND of Ambler class B,C. indologeneshas a class A ESBL gene,blaCIA-1, located on the chromosome.
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Biedenbach, Douglas J., Krystyna Kazmierczak, Samuel K. Bouchillon, Daniel F. Sahm, and Patricia A. Bradford. "In VitroActivity of Aztreonam-Avibactam against a Global Collection of Gram-Negative Pathogens from 2012 and 2013." Antimicrobial Agents and Chemotherapy 59, no. 7 (May 11, 2015): 4239–48. http://dx.doi.org/10.1128/aac.00206-15.

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ABSTRACTThe combination of aztreonam plus avibactam is being developed for use in infections caused by metallo-β-lactamase-producingEnterobacteriaceaestrains that also produce serine β-lactamases. Thein vitroactivities of aztreonam-avibactam and comparator antimicrobials were determined against year 2012 and 2013 clinical isolates ofEnterobacteriaceae,Pseudomonas aeruginosa, andAcinetobacter baumanniiusing the broth microdilution methodology recommended by the Clinical and Laboratory Standards Institute (CLSI). A total of 28,501 unique clinical isolates were obtained from patients in 190 medical centers within 39 countries. MIC90values of aztreonam and aztreonam-avibactam against all collected isolates ofEnterobacteriaceae(n= 23,516) were 64 and 0.12 μg/ml, respectively, with 76.2% of the isolates inhibited by ≤4 μg/ml of aztreonam (the CLSI breakpoint) and 99.9% of the isolates inhibited by ≤4 μg/ml of aztreonam-avibactam using a fixed concentration of 4 μg/ml of avibactam. The MIC90was 32 μg/ml for both aztreonam and aztreonam-avibactam againstP. aeruginosa(n= 3,766). Aztreonam alone or in combination with avibactam had noin vitroactivity against isolates ofA. baumannii. PCR and sequencing were used to characterize 5,076 isolates for β-lactamase genes. Aztreonam was not active against mostEnterobacteriaceaeisolates producing class A or class C enzymes alone or in combination with class B metallo-β-lactamases. In contrast, >99% ofEnterobacteriaceaeisolates producing all observed Ambler classes of β-lactamase enzymes were inhibited by ≤4 μg/ml aztreonam in combination with avibactam, including isolates that produced IMP-, VIM-, and NDM-type metallo-β-lactamases in combination with multiple serine β-lactamases.
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Abaza, Amani F., Soraya A. El Shazly, Heba S. A. Selim, and Gehan S. A. Aly. "Metallo-Beta-Lactamase Producing Pseudomonas aeruginosa in a Healthcare Setting in Alexandria, Egypt." Polish Journal of Microbiology 66, no. 3 (September 27, 2017): 297–308. http://dx.doi.org/10.5604/01.3001.0010.4855.

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Pseudomonas aeruginosa has emerged as a major healthcare associated pathogen that creates a serious public health disaster in both developing and developed countries. In this work we aimed at studying the occurrence of metallo-beta-lactamase (MBL) producing P. aeruginosa in a healthcare setting in Alexandria, Egypt. This cross sectional study included 1583 clinical samples that were collected from patients admitted to Alexandria University Students’ Hospital. P. aeruginosa isolates were identified using standard microbiological methods and were tested for their antimicrobial susceptibility patterns using single disc diffusion method according to the Clinical and Laboratory Standards Institute recommendations. Thirty P. aeruginosa isolates were randomly selected and tested for their MBL production by both phenotypic and genotypic methods. Diagnostic Epsilometer test was done to detect metallo-beta-lactamase enzyme producers and polymerase chain reaction test was done to detect imipenemase (IMP), Verona integron-encoded (VIM) and Sao Paulo metallo-beta-lactamase (IMP) encoding genes. Of the 1583 clinical samples, 175 (11.3%) P. aeruginosa isolates were identified. All the 30 (100%) selected P. aeruginosa isolates that were tested for MBL production by Epsilometer test were found to be positive; where 19 (63.3%) revealed blaSPM gene and 11 (36.7%) had blaIMP gene. blaVIM gene was not detected in any of the tested isolates. Isolates of MBL producing P. aeruginosa were highly susceptible to polymyxin B 26 (86.7%) and highly resistant to amikacin 26 (86.7%). MBL producers were detected phenotypically by Epsilometer test in both carbapenem susceptible and resistant P. aeruginosa isolates. blaSPM was the most commonly detected MBL gene in P. aeruginosa isolates.
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Bagheri Josheghani, Sareh, Rezvan Moniri, Farzaneh Firoozeh, Mojtaba Sehat, and Yasaman Dasteh Goli. "Susceptibility Pattern and Distribution of Oxacillinases andblaPER-1Genes among Multidrug ResistantAcinetobacter baumanniiin a Teaching Hospital in Iran." Journal of Pathogens 2015 (2015): 1–7. http://dx.doi.org/10.1155/2015/957259.

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Acinetobacter baumannii (A. baumannii)is an important nosocomial pathogen in healthcare institutions.β-Lactamase-mediated resistance is the most common mechanism for carbapenem resistance inA. baumannii. The aim of this study was to determine the antibiotic resistance pattern, to detectOXAencoding genes, class A,blaPER-1, and to detect the presence of ISAba1. A total of 124A. baumanniiisolates were collected from hospitalized patients in a teaching hospital in Kashan, Iran. The susceptibility of isolates to different antibiotics was determined by disk-diffusion method. PCR was used to detectblaPER-1,blaOXA-23,blaOXA-24,blaOXA-51,blaOXA-58, and ISAba1 genes. All isolates were resistant to ceftazidime, ceftriaxone, and cefotaxime. All of the isolates revealed susceptibility to polymyxin B and colistin. Ninety-six percent of the isolates were extensive drug resistance (XDR), 5.6% extended spectrum beta-lactamase (ESBL), and 54.8% metallo-beta-lactamase (MBL). All isolates were positive forblaOXA-51and ISAba1.blaOXA-23, blaOXA-24, andblaOXA-58were found in 79.8%, 25%, and 3.2%, respectively. The frequency rate ofblaPER-1gene was 52.4%. Multidrug resistantA. baumanniiisolates are increasing in our setting and extensively limit therapeutic options. The high rate presence of class D carbapenemase-encoding genes, mainlyblaOXA-23carbapenemases, is worrying and alarming as an emerging threat in our hospital.
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Vivan, Ana Carolina Polano, Juliana Ferraz Rosa, Camila Fonseca Rizek, Marsileni Pelisson, Silvia Figueiredo Costa, Mariangela Hungria, Renata Kobayashi, and Eliana Carolina Vespero. "Molecular characterization of carbapenem-resistant Klebsiella pneumoniae isolates from a university hospital in Brazil." Journal of Infection in Developing Countries 11, no. 05 (June 1, 2017): 379–86. http://dx.doi.org/10.3855/jidc.8614.

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Introduction: The emergence of Klebsiella pneumoniae carbapenemase (KPC)-producing K. pneumoniae (KPC-Kpn) isolates is attracting significant attention in nosocomial infection settings. K. pneumoniae is the main pathogen that harbours blaKPC genes. Methodology: This study evaluated 54 K. pneumoniae carbapenem-resistant isolates from patients hospitalized at the University Hospital of Londrina, between July 2009 and July 2010. The isolates were phenotypically screened for carbapenemase production and submitted for genotypic confirmation by polymerase chain reaction (PCR) for KPC, metallo-β-lactamases, OXA-48, and extended-spectrum beta-lactamase genes. The absence of outer membrane proteins (OMP) was investigated by SDS-PAGE. The susceptibility profile was determined by broth microdilution, according to Clinical and Laboratory Standards Institute protocol. Results: All isolates were phenotypically positive for class A carbapenemase production, but negative for metallo-β-lactamase activity. PCR analysis demonstrated that all isolates carried blaKPC genes and sequencing showed that all strains belonged to KPC-2 subtype. Four strains did not show porin expression, and all isolates were resistant to ertapenem, meropenem, and imipenem. Susceptibility rates reached 35.2% for gentamicin, 85.2% for polymixyn B, 87% for colistin, and 98.1% for both tigecycline and fosfomycin. Pulsed-field gel electrophoresis showed six clones, and three of them predominated among the isolates. Conclusions: KPC-2-producing K. pneumoniae is becoming predominant among carbapenem-resistant K. pneumoniae isolates at the hospital. The association of the enzyme KPC with other resistance determinants, such as loss of porins, may increase the severity of the situation of nosocomial infections. There is an urgent need to develop strategies for infection control and prevention.
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Woodford, Neil, Marie-France I. Palepou, Gioia S. Babini, Barry Holmes, and David M. Livermore. "Carbapenemases of Chryseobacterium(Flavobacterium) meningosepticum: Distribution ofblaB and Characterization of a Novel Metallo-β-Lactamase Gene, blaB3, in the Type Strain, NCTC 10016." Antimicrobial Agents and Chemotherapy 44, no. 6 (June 1, 2000): 1448–52. http://dx.doi.org/10.1128/aac.44.6.1448-1452.2000.

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ABSTRACT Genes encoding carbapenemases in 15 reference strains ofChryseobacterium (Flavobacterium)meningosepticum from the United Kingdom National Collection of Type Cultures and in one recent clinical isolate were investigated. All the strains hydrolyzed imipenem, but their levels of resistance to carbapenems varied, with imipenem and meropenem MICs ranging from 2 to >32 μg/ml. The blaB gene, which encodes a molecular-class B carbapenemase, was detected in only six reference strains and in clinical isolate 97/P/5448. The gene from 97/P/5448 had 98% nucleotide identity with the published sequence ofblaB (from strain NCTC 10585) and was designatedblaB2. A distinct carbapenemase gene, designatedblaB3, was cloned from the type strain of C. meningosepticum, NCTC 10016. blaB3 had an open reading frame of 750 bp with 82% nucleotide identity toblaB and blaB2 and encoded a β-lactamase of 249 amino acids, including the putative signal peptide. This β-lactamase showed 87.6 and 86.7% amino acid homology with BlaB and BlaB2, respectively. blaB3 was detected in one other reference strain besides NCTC 10016, but the genetic basis of the carbapenemase activity detected in the other seven reference strains was not defined. Thus, neither blaB nor blaB3was ubiquitous in the strains of C. meningosepticumstudied, indicating that the reference strains may represent more than one bacterial species, each with its own intrinsic metallo-β-lactamase. Further taxonomic studies of C. meningosepticum are necessary to resolve this topic.Chryseobacterium spp. are environmental organisms and occasional opportunist pathogens. They apparently represent a reservoir of diverse metallo-β-lactamases, which potentially spread to gram-negative bacteria of greater clinical significance.
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8

Lee, Kyungwon, Jong Back Lim, Jong Hwa Yum, Dongeun Yong, Yunsop Chong, June Myung Kim, and David M. Livermore. "bla VIM-2 Cassette-Containing Novel Integrons in Metallo-β-Lactamase-Producing Pseudomonas aeruginosa and Pseudomonas putida Isolates Disseminated in a Korean Hospital." Antimicrobial Agents and Chemotherapy 46, no. 4 (April 2002): 1053–58. http://dx.doi.org/10.1128/aac.46.4.1053-1058.2002.

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ABSTRACT We investigated the phenotypic and genetic properties of metallo-β-lactamase-producing Pseudomonas isolates collected at a tertiary-care hospital in Korea since 1995. The prevalence of imipenem resistance among Pseudomonas aeruginosa isolates reached 16% in 1997, when 9% of the resistant organisms were found to produce VIM-2 β-lactamase, a class B enzyme previously found only in P. aeruginosa isolates from Europe. VIM-2-producing isolates of Pseudomonas putida were also detected. Resistance was transferable from both these species to P. aeruginosa PAO4089Rp by filter mating, although the resistance determinant could not be found on any detectable plasmid. Serotyping showed that many of the VIM-2-producing P. aeruginosa isolates belonged to serotypes O:11 and O:12, and pulsed-field gel electrophoresis of XbaI-digested genomic DNA revealed that many had identical profiles, whereas the P. putida isolates were diverse. Sequencing showed that the bla VIM-2 genes resided as cassettes in class 1 integrons. In contrast to previous VIM-encoding integrons, the integron sequenced from a P. aeruginosa isolate had bla VIM located downstream of a variant of aacA4. bla VIM also lay in a class 1 integron in a representative P. putida strain, but the organization of this integron was different from that sequenced from the P. aeruginosa strain. In conclusion, the metallo-β-lactamase produced by these imipenem-resistant Pseudomonas isolates was VIM-2, and the accumulation of producers reflected clonal dissemination as well as horizontal spread. Strict measures are required in order to control a further spread of resistance.
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Aghamiri, Samira, Nour Amirmozafari, Jalil Fallah Mehrabadi, Babak Fouladtan, and Hossein Samadi Kafil. "Antibiotic Resistance Pattern and Evaluation of Metallo-Beta Lactamase Genes Including bla-IMP and bla-VIM Types in Pseudomonas aeruginosa Isolated from Patients in Tehran Hospitals." ISRN Microbiology 2014 (April 23, 2014): 1–6. http://dx.doi.org/10.1155/2014/941507.

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Beta-lactamase producing strains of Pseudomonas aeruginosa are important etiological agents of hospital infections. Carbapenems are among the most effective antibiotics used against Pseudomonas infections, but they can be rendered infective by group B β-lactamase, commonly called metallo-beta lactamase. In this study, the antimicrobial sensitivity patterns of P. aeruginosa strains isolated from 9 different hospitals in Tehran, Iran, as well as the prevalence of MBLs genes (bla-VIM and bla-IMP) were determined. A total of 212 strains of P. aeruginosa recovered from patients in hospitals in Tehran were confirmed by both biochemical methods and PCR. Their antimicrobial sensitivity patterns were determined by Kirby-Bauer disk diffusion method. Following MIC determination, imipenem resistant strains were selected by DDST method which was followed by PCR tests for determination of MBLs genes: bla-IMP and bla-VIM. The results indicated that, in the DDST phenotypic method, among the 100 imipenem resistant isolates, 75 strains were MBLs positive. The PCR test indicated that 70 strains (33%) carried bla-VIM gene and 20 strains (9%) harbored bla-IMP. The results indicated that the extent of antibiotic resistance among Pseudomonas aeruginosa is on the rise. This may be due to production of MBLs enzymes. Therefore, determination of antibiotic sensitivity patterns and MBLs production by these bacteria, can be important in control of clinical Pseudomonas infection.
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Toleman, Mark A., Kenneth Rolston, Ronald N. Jones, and Timothy R. Walsh. "Molecular and Biochemical Characterization of OXA-45, an Extended-Spectrum Class 2d′ β-Lactamase in Pseudomonas aeruginosa." Antimicrobial Agents and Chemotherapy 47, no. 9 (September 2003): 2859–63. http://dx.doi.org/10.1128/aac.47.9.2859-2863.2003.

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ABSTRACT As part of the CANCER Antimicrobial Surveillance Program in North America, a clinical strain of Pseudomonas aeruginosa, strain 07-406, isolated in Texas was found to be resistant to all antimicrobials except polymyxin B. Genetic analysis of this isolate identified two unique extended-spectrum β-lactamase genes. One, bla VIM-7, encoded a metallo-β-lactamase (unpublished data), and the other, bla OXA-45, described here, encoded a class D extended-spectrum β-lactamase. bla OXA-45 was isolated on a Sau3A1 genomic fragment of 1.8 kb and encodes a protein of 264 amino acids with the highest identities to OXA-18 (65.9%), OXA-9 (42.8%), OXA-22 (40.2%), OXA-12 (38.6%), and OXA-29 (35.2%) but weak identities with other class D β-lactamases. bla OXA-45 was found to be harbored on a 24-kb plasmid in a region that displays high identities with a section of the 43-kb genomic island of Salmonella enterica serovar Typhimurium DT104. Biochemically OXA-45 is most similar to OXA-18 in its substrate profile and inhibition by clavulanic acid and is a member of the 2d′ class of β-lactamases.
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Dissertations / Theses on the topic "Metallo-B-lactamase genes"

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Ranjan, Vivek Kumar. "Search for molecular diversity of metallo-B-lactamase genes in eubacterial isolates of Karala and Mahananda rivers of West Bengal." Thesis, University of North Bengal, 2021. http://ir.nbu.ac.in/handle/123456789/4663.

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