scholarly journals Identification and Characterization of a New Metallo-β-Lactamase, IND-5, from a Clinical Isolate of Chryseobacterium indologenes

2007 ◽  
Vol 51 (8) ◽  
pp. 2988-2990 ◽  
Author(s):  
Mariagrazia Perilli ◽  
Bibiana Caporale ◽  
Giuseppe Celenza ◽  
Cristina Pellegrini ◽  
Jean Denis Docquier ◽  
...  
Keyword(s):  
Amino Acid ◽  
Clinical Isolate ◽  
Amino Acid Homology ◽  
Chryseobacterium Indologenes ◽  
Identification And Characterization

ABSTRACT A new natural IND-type metallo-β-lactamase variant, IND-5, was identified in a clinical isolate of Chryseobacterium indologenes. IND-5 shared 92.8% and 92.4% amino acid homology with IND-1 and IND-3, respectively. Purified enzyme (pI = 8.8, M r = 25,000) was able to hydrolyze penicillins, some narrow- and expanded-spectrum cephalosporins, and carbapenems but not monobactams.

scholarly journals Isolation, identification and characterization of a novel elastase from Chryseobacterium indologenes

2018 ◽  
Vol 61 (3) ◽  
pp. 365-372 ◽  
Author(s):  
Yunlong Lei ◽  
Peipei Zhao ◽  
Chenglei Li ◽  
Haixia Zhao ◽  
Zhi Shan ◽  
...  
Keyword(s):  
Chryseobacterium Indologenes ◽  
Identification And Characterization

scholarly journals IND-6, a Highly Divergent IND-Type Metallo-β-Lactamase from Chryseobacterium indologenes Strain 597 Isolated in Burkina Faso

2009 ◽  
Vol 53 (10) ◽  
pp. 4320-4326 ◽  
Author(s):  
Boukaré Zeba ◽  
Filomena De Luca ◽  
Alain Dubus ◽  
Michael Delmarcelle ◽  
Jacques Simporé ◽  
...  
Keyword(s):  
Burkina Faso ◽  
Posttranslational Modification ◽  
Human Pathogens ◽  
Turnover Rates ◽  
Chryseobacterium Indologenes ◽  
Sequence Identity ◽  
New Variant ◽  
The Family ◽  
Identification And Characterization

ABSTRACT The genus Chryseobacterium and other genera belonging to the family Flavobacteriaceae include organisms that can behave as human pathogens and are known to cause different kinds of infections. Several species of Flavobacteriaceae, including Chryseobacterium indologenes, are naturally resistant to β-lactam antibiotics (including carbapenems), due to the production of a resident metallo-β-lactamase. Although C. indologenes presently constitutes a limited clinical threat, the incidence of infections caused by this organism is increasing in some settings, where isolates that exhibit multidrug resistance phenotypes (including resistance to aminoglycosides and quinolones) have been detected. Here, we report the identification and characterization of a new IND-type variant from a C. indologenes isolate from Burkina Faso that is resistant to β-lactams and aminoglycosides. The levels of sequence identity of the new variant to other IND-type metallo-β-lactamases range between 72 and 90% (for IND-4 and IND-5, respectively). The purified enzyme exhibited N-terminal heterogeneity and a posttranslational modification consisting of the presence of a pyroglutamate residue at the N terminus. IND-6 shows a broad substrate profile, with overall higher turnover rates than IND-5 and higher activities than IND-2 and IND-5 against ceftazidime and cefepime.

scholarly journals Characterization of an Enterococcus gallinarum Isolate Carrying a DualvanAandvanBCassette

2015 ◽  
Vol 53 (7) ◽  
pp. 2225-2229 ◽  
Author(s):  
Alireza Eshaghi ◽  
Dea Shahinas ◽  
Aimin Li ◽  
Ruwandi Kariyawasam ◽  
Philip Banh ◽  
...  
Keyword(s):  
Clinical Isolate ◽  
Resistance Mechanism ◽  
Vancomycin Resistance ◽  
Content Type ◽  
Enterococcal Species ◽  
Enterococcus Gallinarum ◽  
High Level ◽  
Identification And Characterization ◽  
Level Resistance

The ability of vancomycin resistance determinants to be horizontally transferred within enterococci species is a concern. Identification and characterization of vancomycin-resistant enterococci (VRE) in a clinical isolate have a significant impact on infection control practices. In this study, we describe a clinical isolate ofEnterococcus gallinarumexhibiting high-level resistance to vancomycin and teicoplanin. The genetic characterization of this isolate showed the presence ofvanAandvanBgenes in addition to the naturally carriedvanCgene.vanAwas identified on pA6981, a 35,608-bp circular plasmid with significant homology to plasmid pS177. ThevanBoperon was integrated into the bacterial chromosome and showed a high level of homology to previously reported Tn1549and Tn5382. To the best of our knowledge, this is the first report ofE. gallinarumcarrying bothvanAandvanBoperons, indicating the importance of identifying the vancomycin resistance mechanism in non-E. faeciumand non-E. faecalisenterococcal species.

scholarly journals First Identification and Characterization of an AdeABC-Like Efflux Pump inAcinetobacterGenomospecies 13TU

2011 ◽  
Vol 55 (3) ◽  
pp. 1285-1286 ◽  
Author(s):  
Ignasi Roca ◽  
Paula Espinal ◽  
Sara Martí ◽  
Jordi Vila
Keyword(s):  
Multidrug Resistance ◽  
Acinetobacter Baumannii ◽  
Clinical Isolate ◽  
Nosocomial Infections ◽  
Efflux Pump ◽  
Hospital Setting ◽  
Multidrug Resistant ◽  
Identification Techniques ◽  
Identification And Characterization

ABSTRACTNon-Acinetobacter baumanniispp. are emerging among clinicalAcinetobacterisolates causing nosocomial infections, and some (such as genomospecies 13TU) appear to be multidrug resistant. The prevalence of non-Acinetobacter baumanniispp. in the hospital setting is likely understated due to poor identification techniques. We report the first identification of an AdeABC-type efflux pump in anAcinetobactergenomospecies 13TU clinical isolate, its contribution to multidrug resistance, and the coexistence of three Ade-type efflux pumps in this strain.

scholarly journals Characterization of TEM-56, a Novel β-Lactamase Produced by a Klebsiella pneumoniae Clinical Isolate

2000 ◽  
Vol 44 (2) ◽  
pp. 453-455 ◽  
Author(s):  
Catherine Neuwirth ◽  
Roger Labia ◽  
Eliane Siebor ◽  
Andre Pechinot ◽  
Stephanie Madec ◽  
...  
Keyword(s):  
Amino Acid ◽  
Klebsiella Pneumoniae ◽  
Amino Acid Sequence ◽  
Clinical Isolate ◽  
Isoelectric Point ◽  
Catalytic Properties ◽  
Resistance Level ◽  
Extended Spectrum ◽  
Moderate Resistance

ABSTRACT TEM-56 produced by a Klebsiella pneumoniae clinical isolate is a novel β-lactamase of isoelectric point 6.4 that confers a moderate resistance level to expanded-spectrum cephalosporins. The amino acid sequence deduced from the corresponding bla gene showed two amino acid replacements with respect to the TEM-2 sequence: Glu-104 to Lys and His-153 to Arg. This enzyme showed catalytic properties close to those of TEM-18. Thus, TEM-56 appears as a new TEM mutant, an intermediary between TEM-18 and the extended-spectrum β-lactamase TEM-21.

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