Journal
ANTIMICROBIAL AGENTS AND CHEMOTHERAPY
Volume 54, Issue 1, Pages 471-476Publisher
AMER SOC MICROBIOLOGY
DOI: 10.1128/AAC.00458-09
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Funding
- European Community [LSHM-CT-2005-018705, HEALTH-F3-2008-223031]
- INSERM
- Ministere de l'Education Nationale et de la Recherche [UPRES-EA3539]
- Universite Paris XI, Paris, France
- Ministerio de Educacion y Ciencia from Spain [2007/0292]
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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.
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