VIM-19, a metallo-beta-lactamase with increased carbapenemase activity from Escherichia coli and Klebsiella pneumoniae.

Abstract:

:Two carbapenem-resistant isolates, one Escherichia coli isolate and one Klebsiella pneumoniae isolate, recovered from an Algerian patient expressed a novel VIM-type metallo-beta-lactamase (MBL). The identified bla(VIM-19) gene was located on a ca. 160-kb plasmid and located inside a class 1 integron in both isolates. VIM-19 differed from VIM-1 by the Asn215Lys and Ser228Arg substitutions, increasing its hydrolytic activity toward carbapenems. Site-directed mutagenesis experiments showed that both substitutions were necessary for the increased carbapenemase activity of VIM-19. This study indicates that MBLs with enhanced activity toward carbapenems may be obtained as a result of very few amino acid substitutions.

authors

Rodriguez-Martinez JM,Nordmann P,Fortineau N,Poirel L

doi

10.1128/AAC.00458-09

subject

Has Abstract

pub_date

2010-01-01 00:00:00

pages

471-6

issue

1

eissn

0066-4804

issn

1098-6596

pii

AAC.00458-09

journal_volume

54

pub_type

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