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1.
J Clin Microbiol ; 52(7): 2702-5, 2014 Jul.
Artículo en Inglés | MEDLINE | ID: mdl-24759725

RESUMEN

We describe two cases of bacteremic infections caused by a multidrug-resistant Klebsiella pneumoniae isolate producing the OXA-48 carbapenemase that occurred in two solid organ transplant (liver and kidney) recipients, which was apparently transmitted with the allografts. This finding underscores the risk of donor-derived infections by multidrug-resistant Gram-negative pathogens in solid organ transplant recipients and emphasizes the need for rapid screening of organ donors for carriage of similar pathogens.


Asunto(s)
Bacteriemia/diagnóstico , Infección Hospitalaria/diagnóstico , Farmacorresistencia Bacteriana Múltiple , Infecciones por Klebsiella/diagnóstico , Klebsiella pneumoniae/efectos de los fármacos , Klebsiella pneumoniae/enzimología , beta-Lactamasas/metabolismo , Adulto , Humanos , Klebsiella pneumoniae/aislamiento & purificación , Persona de Mediana Edad , Receptores de Trasplantes , Trasplante/efectos adversos , Trasplantes
2.
Plant Physiol ; 152(3): 1186-96, 2010 Mar.
Artículo en Inglés | MEDLINE | ID: mdl-20023146

RESUMEN

Histidine (His) plays a critical role in plant growth and development, both as one of the standard amino acids in proteins, and as a metal-binding ligand. While genes encoding seven of the eight enzymes in the pathway of His biosynthesis have been characterized from a number of plant species, the identity of the enzyme catalyzing the dephosphorylation of histidinol-phosphate to histidinol has remained elusive. Recently, members of a novel family of histidinol-phosphate phosphatase proteins, displaying significant sequence similarity to known myoinositol monophosphatases (IMPs) have been identified from several Actinobacteria. Here we demonstrate that a member of the IMP family from Arabidopsis (Arabidopsis thaliana), myoinositol monophosphatase-like2 (IMPL2; encoded by At4g39120), has histidinol-phosphate phosphatase activity. Heterologous expression of IMPL2, but not the related IMPL1 protein, was sufficient to rescue the His auxotrophy of a Streptomyces coelicolor hisN mutant. Homozygous null impl2 Arabidopsis mutants displayed embryonic lethality, which could be rescued by supplying plants heterozygous for null impl2 alleles with His. In common with the previously characterized HISN genes from Arabidopsis, IMPL2 was expressed in all plant tissues and throughout development, and an IMPL2:green fluorescent protein fusion protein was targeted to the plastid, where His biosynthesis occurs in plants. Our data demonstrate that IMPL2 is the HISN7 gene product, and suggest a lack of genetic redundancy at this metabolic step in Arabidopsis, which is characteristic of the His biosynthetic pathway.


Asunto(s)
Proteínas de Arabidopsis/metabolismo , Arabidopsis/enzimología , Histidina/biosíntesis , Histidinol-Fosfatasa/metabolismo , Arabidopsis/genética , Proteínas de Arabidopsis/genética , ADN Bacteriano/genética , ADN de Plantas/genética , Regulación de la Expresión Génica de las Plantas , Prueba de Complementación Genética , Histidinol/metabolismo , Histidinol-Fosfatasa/genética , Modelos Moleculares , Mutagénesis Insercional , Mutación , Fosforilación , Filogenia , Estructura Terciaria de Proteína , Proteínas Recombinantes de Fusión/genética , Proteínas Recombinantes de Fusión/metabolismo
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