VIM-39, a VIM-1-like metallo-β-lactamase variant (VIM-1 Thr33Ala His224Leu) was identified in a clinical isolate of Klebsiella pneumoniae belonging to sequence type 147. VIM-39 hydrolyzed ampicillin, cephalothin, and imipenem more efficiently than did VIM-1 and VIM-26 (a VIM-1 variant with the His224Leu substitution) because of higher turnover rates. © 2015 American Society for Microbiology. All Rights Reserved.

Papagiannitsis, C.C., Pollini, S., DE LUCA, F., Rossolini, G.M., Docquier, J.D., & Hrabák, J. (2015). Biochemical Characterization of VIM-39, a VIM-1-Like Metallo-β-Lactamase Variant from a Multidrug-Resistant Klebsiella pneumoniae Isolate from Greece. ANTIMICROBIAL AGENTS AND CHEMOTHERAPY, 59(12), 7811-7814 [10.1128/AAC.01935-15].

Biochemical Characterization of VIM-39, a VIM-1-Like Metallo-β-Lactamase Variant from a Multidrug-Resistant Klebsiella pneumoniae Isolate from Greece

POLLINI, SIMONA;DE LUCA, FILOMENA;ROSSOLINI, GIAN MARIA;DOCQUIER, JEAN DENIS;
2015

Abstract

VIM-39, a VIM-1-like metallo-β-lactamase variant (VIM-1 Thr33Ala His224Leu) was identified in a clinical isolate of Klebsiella pneumoniae belonging to sequence type 147. VIM-39 hydrolyzed ampicillin, cephalothin, and imipenem more efficiently than did VIM-1 and VIM-26 (a VIM-1 variant with the His224Leu substitution) because of higher turnover rates. © 2015 American Society for Microbiology. All Rights Reserved.
Papagiannitsis, C.C., Pollini, S., DE LUCA, F., Rossolini, G.M., Docquier, J.D., & Hrabák, J. (2015). Biochemical Characterization of VIM-39, a VIM-1-Like Metallo-β-Lactamase Variant from a Multidrug-Resistant Klebsiella pneumoniae Isolate from Greece. ANTIMICROBIAL AGENTS AND CHEMOTHERAPY, 59(12), 7811-7814 [10.1128/AAC.01935-15].
File in questo prodotto:
File Dimensione Formato  
Biochemical Characterization of VIM-39-Papagiannitis-2015.pdf

non disponibili

Tipologia: PDF editoriale
Licenza: NON PUBBLICO - Accesso privato/ristretto
Dimensione 188.46 kB
Formato Adobe PDF
188.46 kB Adobe PDF   Visualizza/Apri   Richiedi una copia

I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.

Utilizza questo identificativo per citare o creare un link a questo documento: http://hdl.handle.net/11365/982017