English   español  
Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/143039
logo share SHARE logo core CORE   Add this article to your Mendeley library MendeleyBASE

Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL
Exportar a otros formatos:


Is256 abolishes gelatinase activity and biofilm formation in a mutant of the nosocomial pathogen enterococcus faecalis v583

AuthorsPérez, Marta M.; Calles-Enríquez, Marina ; Río Lagar, Beatriz del ; Ladero Losada, Víctor Manuel ; Martín, M. Cruz ; Fernández García, María ; Álvarez González, Miguel Ángel
Insertion sequence
Enterococcus faecalis
Issue Date22-Apr-2015
PublisherCanadian Science Publishing
CitationCanadian Journal of Microbiology 61(7): 517-519 (2015)
AbstractEnterococcus faecalis is one of the most controversial species of lactic acid bacteria. Some strains are used as probiotics, while others are associated with severe and life-threatening nosocomial infections. Their pathogenicity depends on the acqui-sition of multidrug resistance and virulence factors. Gelatinase, which is required in the first steps of biofilm formation, is an important virulence determinant involved in E. faecalis pathogenesis, including endocarditis and peritonitis. The gene that codes for gelatinase (gelE) is controlled by the Fsr quorum-sensing system, whose encoding genes (fsrA, fsrB, fsrC, and fsrD) are located immediately upstream of gelE. The integration of a DNA fragment into the fsr locus of a derived mutant of E. faecalis V583 suppressed the gelatinase activity and prevented biofilm formation. Sequence analysis indicated the presence of IS256 integrated into the fsrC gene at nucleotide position 321. Interestingly, IS256 is also associated with biofilm formation in Staphylococcus epidermidis and Staphylococcus aureus. This is the first description of an insertion sequence that prevents biofilm formation in E. faecalis. Copyright de NRC Research Press
Publisher version (URL)https://doi.org/10.1139/cjm-2015-0090
Identifiersissn: 1480-3275
Appears in Collections:(IPLA) Artículos
Files in This Item:
File Description SizeFormat 
Abolishes Gelatinase Activity-Perez et al.pdf482,03 kBAdobe PDFThumbnail
Show full item record
Review this work

Related articles:

WARNING: Items in Digital.CSIC are protected by copyright, with all rights reserved, unless otherwise indicated.