scholarly journals Molecular characterization of antimicrobial-resistant Enterococcus faecalis and Enterococcus faecium isolated from layer parent stock

2019 ◽  
Vol 98 (11) ◽  
pp. 5892-5899 ◽  
Author(s):  
Yeong Bin Kim ◽  
Kwang Won Seo ◽  
Jong Bo Shim ◽  
Se hyun Son ◽  
Eun Bi Noh ◽  
...  
Keyword(s):  
Molecular Characterization ◽  
Enterococcus Faecalis ◽  
Enterococcus Faecium ◽  
Parent Stock

scholarly journals Molecular Characterization of Glycopeptide-Resistant Enterococci from Hospitals of the Picardy Region (France)

2010 ◽  
Vol 2010 ◽  
pp. 1-8 ◽  
Author(s):  
M. Biendo ◽  
C. Adjidé ◽  
S. Castelain ◽  
M. Belmekki ◽  
F. Rousseau ◽  
...  
Keyword(s):  
Molecular Characterization ◽  
Enterococcus Faecalis ◽  
Genetic Relationship ◽  
Enterococcus Faecium ◽  
Gel Electrophoresis ◽  
Multilocus Sequence Typing ◽  
Pulsed Field Gel Electrophoresis ◽  
Pcr Products ◽  
Sequence Types

We studied 138 glycopeptide-resistant enterococci (GRE) strains, consisting of 131 glycopeptide-resistantEnterococcus faecium(GREfm) and 7 glycopeptide-resistantEnterococcus faecalis(GREfs). The GREfm strains were resistant to penicillin, ampicillin, vancomycin, and teicoplanin, while the GREfs strains were only resistant to vancomycin and teicoplanin. Thevan Agene was the only glycopeptide determinant present in all GRE isolates investigated. Genes coding for Hyl and Hyl+ Esp were detected in 39 (29.8%) and 92 (70.2%) of the 131 GREfm isolates, respectively. Three of the 7 GREfs were positive forgelE+asa 1genes, 3 forgel Egene, and 1 forasa 1gene. The genetic relationship between the 138 GRE was analyzed by pulsed-field gel electrophoresis (PFGE) and multilocus sequence typing (MLST). GREfm isolates were clustered in a single genogroup (pulsotype A), and GREfs were clustered in six genogroups (pulsotypes B-G). Among the isolates investigated by MLST, only 18 PCR products were sequenced (12E. faeciumand 6E. faecalis), and 9 sequence types (STs) were identified.

scholarly journals Molecular Characterization of Ampicillin-Resistant Enterococcus faecium Isolates from Hospitalized Patients in Norway

2003 ◽  
Vol 41 (6) ◽  
pp. 2330-2336 ◽  
Author(s):  
R. Jureen ◽  
J. Top ◽  
S. C. Mohn ◽  
S. Harthug ◽  
N. Langeland ◽  
...  
Keyword(s):  
Molecular Characterization ◽  
Enterococcus Faecium ◽  
Hospitalized Patients

scholarly journals Molecular characterization of the Enterococcus faecalis cytolysin activator.

1991 ◽  
Vol 59 (4) ◽  
pp. 1239-1246 ◽  
Author(s):  
R A Segarra ◽  
M C Booth ◽  
D A Morales ◽  
M M Huycke ◽  
M S Gilmore
Keyword(s):  
Molecular Characterization ◽  
Enterococcus Faecalis

scholarly journals Molecular Characterization of Vancomycin-Resistant Enterococcus faecium Isolates from Korea

2005 ◽  
Vol 43 (5) ◽  
pp. 2303-2306 ◽  
Author(s):  
K. S. Ko ◽  
J. Y. Baek ◽  
J.-Y. Lee ◽  
W. S. Oh ◽  
K. R. Peck ◽  
...  
Keyword(s):  
Molecular Characterization ◽  
Enterococcus Faecium ◽  
Vancomycin Resistant Enterococcus ◽  
Vancomycin Resistant

Heterologous Expression and Characterization of Tyrosine Decarboxylase from Enterococcus faecalis R612Z1 and Enterococcus faecium R615Z1

2014 ◽  
Vol 77 (4) ◽  
pp. 592-598 ◽  
Author(s):  
FANG LIU ◽  
WENJUAN XU ◽  
LIHUI DU ◽  
DAOYING WANG ◽  
YONGZHI ZHU ◽  
...  
Keyword(s):  
Amino Acid ◽  
Heterologous Expression ◽  
Molecular Mass ◽  
Enterococcus Faecalis ◽  
Enterococcus Faecium ◽  
Maximal Activity ◽  
Tyrosine Decarboxylase ◽  
Acid Protein ◽  
Amino Acid Protein

Tyrosine decarboxylase (TDC) is responsible for tyramine production and can catalyze phenylalanine to produce β-phenylethylamine. Enterococcus strains are a group of bacteria predominantly producing tyramine and β-phenylethylamine in water-boiled salted duck. In this study, the heterologous expression and characterization of two TDCs from Enterococcus faecalis R612Z1 (612TDC) and Enterococcus faecium R615Z1 (615TDC) were studied. The recombinant putative proteins of 612TDC and 615TDC were heterologously expressed in Escherichia coli. 612TDC is a 620-amino-acid protein with a molecular mass of 70.0 kDa, whereas 615TDC is a 625-amino-acid protein with a molecular mass of 70.3 kDa. Both 612TDC and 615TDC showed an optimum temperature of 25°C for the tyrosine and phenylalanine substrates. However, 612TDC revealed maximal activity at pH 5.5, whereas 615TDC revealed maximal activity at pH 6.0. Kinetic studies showed that 612TDC and 615TDC exhibited higher specificity for tyrosine than for phenylalanine. The catalysis abilities of both 612TDC and 615TDC for phenylalanine were restrained significantly with the increase in NaCl concentration, but this was not the case for tyrosine. This study revealed that the enzyme properties of the purified recombinant 612TDC and 615TDC were similar, although their amino acid sequences had 84% identity.

scholarly journals Molecular Characterization of Glycopeptide-Resistant Enterococcus faecium Isolates from Portuguese Hospitals

2005 ◽  
Vol 49 (7) ◽  
pp. 3073-3079 ◽  
Author(s):  
Carla Novais ◽  
João C. Sousa ◽  
Teresa M. Coque ◽  
Luísa V. Peixe
Keyword(s):  
Molecular Characterization ◽  
Enterococcus Faecium ◽  
Gel Electrophoresis ◽  
Pulsed Field Gel Electrophoresis ◽  
Pulsed Field ◽  
Vancomycin Resistant ◽  
Geographical Locations

ABSTRACT Fifty-one pulsed-field gel electrophoresis types and 17 Tn1546 variants were identified among 101 Enterococcus faecium isolates recovered in three distant Portuguese hospitals. Intra- and interhospital dissemination of specific strains and Tn1546 types was detected, which might largely contribute to the endemicity of vancomycin-resistant E. faecium in Portuguese hospitals, as happened previously in other geographical locations.

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