RESUMEN
BACKGROUND: Although Faecalibacterium prausnitzii is a major bacterium in the intestine of adults, which is known to have anti-inflammatory effects, the development in infants or the response to prebiotics remains unclear. METHODS: The counts of F. prausnitzii in the feces were examined by real-time polymerase chain reaction (PCR). Fecal samples were obtained from 65 atopic dermatitis (AD) infants who participated in a randomized controlled clinical trial to investigate the therapeutic effect of kestose, the smallest fructooligosaccharide. RESULTS: Although the F. prausnitzii count was undetectable level in most 0- to 1-y-old infants, the count reached a level comparable to that in adults in 2- to 5-y-old infants. The bacterial number increased about 10-fold by oral administration of kestose every day for 12 wk in the younger infants, but not so much in the older infants. This bacterial increase was significantly correlated with an improvement in the AD symptoms in the older infants. CONCLUSION: The F. prausnitzii population in the intestine reaches a level comparable to that in adult at approximately 2 y of age. Kestose efficiently stimulates the growth of this bacterium in the intestine, which might lead to an improvement in AD symptoms in infants.
Asunto(s)
Dermatitis Atópica/tratamiento farmacológico , Dermatitis Atópica/microbiología , Faecalibacterium prausnitzii/efectos de los fármacos , Oligosacáridos/uso terapéutico , Prebióticos/administración & dosificación , Factores de Edad , Carga Bacteriana , Bifidobacterium/efectos de los fármacos , Bifidobacterium/genética , Bifidobacterium/aislamiento & purificación , Preescolar , Faecalibacterium prausnitzii/genética , Faecalibacterium prausnitzii/aislamiento & purificación , Femenino , Microbioma Gastrointestinal/efectos de los fármacos , Humanos , Lactante , Recién Nacido , Masculino , Reacción en Cadena en Tiempo Real de la PolimerasaRESUMEN
The LBP-1 family consists of four proteins, which act as transcription factors in the formation of dimers with a member of this family. LBP-1a and LBP-1b are splicing variants from one gene, and LBP-1c and LBP-1d also arise from the alternative splicing of another gene. Investigation of subcellular localization of LBP-1 proteins fused to YFP revealed that the LBP-1b was localized in the nucleus, whereas LBP-1a and LBP-1c were exclusively localized in the cytosol. The peptide of 36 amino acids encoded by exon 6, a specific exon used only for LBP-1b, possessed the function of a nuclear localization signal (NLS). Nuclear localization of LBP-1a and LBP-1c occurred when LBP-1b was co-expressed, suggesting that heterodimerization of LBP-1a and LBP-1c with LBP-1b is important for their nuclear transport. Transiently expressed LBP-1 proteins in COS-7 cells formed speckles in the nucleus. Most speckles overlapped with the PML body. The activity of LBP-1a for accumulation in the PML body was mapped in the N-terminal region.
