Base de dados : LILACS
Pesquisa : D02.241.223.200.380 [Categoria DeCS]
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Id: lil-751349
Autor: Cavalcante, F.S.; Abad, E.D.; Lyra, Y.C.; Saintive, S.B.; Ribeiro, M.; Ferreira, D.C.; Santos, K.R.N. dos.
Título: High prevalence of methicillin resistance and PVL genes among Staphylococcus aureus isolates from the nares and skin lesions of pediatric patients with atopic dermatitis
Fonte: Braz. j. med. biol. res = Rev. bras. pesqui. méd. biol;48(7):588-594, 07/2015. tab.
Idioma: en.
Projeto: FAPERJ; . CNPq; . CAPES; . FUJB; . PRONEX.
Resumo: Staphylococcus aureus is highly prevalent among patients with atopic dermatitis (AD), and this pathogen may trigger and aggravate AD lesions. The aim of this study was to determine the prevalence of S. aureus in the nares of pediatric subjects and verify the phenotypic and molecular characteristics of the isolates in pediatric patients with AD. Isolates were tested for antimicrobial susceptibility, SCCmec typing, and Panton-Valentine Leukocidin (PVL) genes. Lineages were determined by pulsed-field gel electrophoresis and multilocus sequence typing (MLST). AD severity was assessed with the Scoring Atopic Dermatitis (SCORAD) index. Among 106 patients, 90 (85%) presented S. aureus isolates in their nares, and 8 also presented the pathogen in their skin infections. Two patients had two positive lesions, making a total of 10 S. aureus isolates from skin infections. Methicillin-resistant S. aureus (MRSA) was detected in 24 (26.6%) patients, and PVL genes were identified in 21 (23.3%), including 6 (75%) of the 8 patients with skin lesions but mainly in patients with severe and moderate SCORAD values (P=0.0095). All 24 MRSA isolates were susceptible to trimethoprim/sulfamethoxazole, while 8 isolates had a minimum inhibitory concentration (MIC) to mupirocin >1024 μg/mL. High lineage diversity was found among the isolates including USA1100/ST30, USA400/ST1, USA800/ST5, ST83, ST188, ST718, ST1635, and ST2791. There was a high prevalence of MRSA and PVL genes among the isolates recovered in this study. PVL genes were found mostly among patients with severe and moderate SCORAD values. These findings can help clinicians improve the therapies and strategies for the management of pediatric patients with AD.
Descritores: Nefropatias/metabolismo
Rim/metabolismo
Podócitos/metabolismo
Transdução de Sinais
-Células Cultivadas
Proteína de Ligação ao Elemento de Resposta ao AMP Cíclico/metabolismo
Proteínas Quinases Dependentes de AMP Cíclico/metabolismo
Expressão Gênica
Redes Reguladoras de Genes
Immunoblotting
Nefropatias/induzido quimicamente
Nefropatias/genética
Rim/patologia
Rim/fisiopatologia
Microscopia Eletrônica
Proteínas de Membrana/genética
Proteínas de Membrana/metabolismo
Proteínas dos Microfilamentos/genética
Proteínas dos Microfilamentos/metabolismo
Puromicina
Podócitos/patologia
Podócitos/ultraestrutura
Proteômica/métodos
Ratos Sprague-Dawley
Reação em Cadeia da Polimerase Via Transcriptase Reversa
Limites: Animais
Masculino
Camundongos
Ratos
Tipo de Publ: Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.
Responsável: BR1.1 - BIREME


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Id: lil-386684
Autor: Nóbrega, Otávio T; Santana, Jaime M; Sturm, Nancy R; Teixeira, Antônio R. L; Campbell, David A.
Título: HygR and PurR plasmid vectors for episomal transfection of Trypanosoma cruzi
Fonte: Mem. Inst. Oswaldo Cruz;99(5):513-516, Aug. 2004. ilus.
Idioma: en.
Projeto: CNPq; . Genbank.
Resumo: This work describes the development and functional testing of two episomes for stable transfection of Trypanosoma cruzi. pHygD contained the 5'- and 3'- flanking regions of the gene encoding the cathepsin B-like protease of T. cruzi as functional trans-splicing and polyadenylation signals for the hygR ORF. Evidence is presented to support extrachromosomal maintenance and organization as tandem repeats in transfected parasites. pPac was derived from pHygD by replacement of the entire hygR ORF with a purR coding region. The ability to modify pHygD and the availability of the complete DNA sequence make these plasmids useful tools for the genetic manipulation of T. cruzi.
Descritores: Vetores Genéticos
Transfecção
Trypanosoma cruzi
-Dados de Sequência Molecular
Puromicina
Limites: Animais
Responsável: BR1.1 - BIREME


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Id: lil-228602
Autor: Henriquez, Diana A; Perez, Norma; Pance, Alena; Bradley, Charles.
Título: Mechanisms of protein degradation in Trypanosoma cruzi
Fonte: Biol. Res;26(1/2):151-7, 1993.
Idioma: en.
Resumo: Proteolysis of endogenous proteins may play a key role in the adaptation of T. cruzi to the different host environments to which it is exposed during its complex life cycle. For this reason, we have attempted to study the intracellular pathways of protein degradation in the non infective epimastigotes form (EP strain) of T. cruzi. Following intracellular proteolysis by pulse chase experiments with 35 S methionine, we observed a significant inhibition (50 percent) of the degradation of endogenous proteins in log phase parasites in the presence of inhibitors of lysosomal functions, such as chloroquine and E 64. A significant increase in proteolysis was observed in stationary phase parasites which was reverted to log phase values by supplementing the chase medium with 0.5 percent glucose or 10 percent serum, or in the presence of chloroquine. Under this condition of nutritional stress, we could observe an increase in the activity of acid proteases. A significant increase in the degradation rates was observed when abnormal proteins were induced in the parasite by amino acid analogs and puromycin. This increase was not affected by E 64, suggesting the participation of non lysosomal mechanisms in the degradation of rapidly degradable abnormal proteins. Under these conditions, we could observe an increase in high molecular weight conjugates of ubiquitin with respect to endogenous proteins. These results suggest the importance of lysosomal mechanisms in the degradation of cellular proteins in nutritional optimal conditions and during nutritional deprivation, and the possible involvement of the ubiquitin system in the degradation of high turnover proteins
Descritores: Peptídeo Hidrolases/metabolismo
Proteínas de Protozoários/metabolismo
Trypanosoma cruzi/metabolismo
-Cloroquina/farmacologia
Cisteína Proteases/metabolismo
Concentração de Íons de Hidrogênio
Membranas Intracelulares/metabolismo
Leucina/análogos & derivados
Leucina/farmacologia
Peso Molecular
Inibidores de Proteases/farmacologia
Puromicina/farmacologia
Fatores de Tempo
Trypanosoma cruzi/enzimologia
Trypanosoma cruzi/crescimento & desenvolvimento
Ubiquitina/metabolismo
Limites: Animais
Tipo de Publ: Research Support, Non-U.S. Gov't
Responsável: BR1.1 - BIREME



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