Base de dados : MEDLINE Pesquisa : B01.650.940.800.575.912.250.618.875.625 [Categoria DeCS] Referências encontradas : 7 [refinar] Mostrando: 1 .. 7   no formato [Detalhado]

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[PMID]: 29188364 [Au] Autor: Lan P; Zhao J; Zhou Y; Li Y; Shen D; Liao Q; Li R; Li F [Ad] Endereço: State Key Laboratory for Conservation and Utilization of Bio-Resources in Yunnan, Yunnan Agricultural University, Kunming, 650201, China. [Ti] Título: Complete genome sequence of Paris mosaic necrosis virus, a distinct member of the genus Potyvirus. [So] Source: Arch Virol;163(3):787-790, 2018 Mar. [Is] ISSN: 1432-8798 [Cp] País de publicação: Austria [La] Idioma: eng [Ab] Resumo: The complete genomic sequence of a novel potyvirus was determined from Paris polyphylla var. yunnanensis. Its genomic RNA consists of 9,660 nucleotides (nt) excluding the 3'-terminal poly (A) tail, containing the typical open reading frame (ORF) of potyviruses and encoding a putative large polyprotein of 3030 amino acids. The virus shares 53.9-70.1% nt sequence identity and 43.9-73.2% amino acid sequence identity with other viruses classified within the genus Potyvirus. Proteolytic cleavage sites and conserved motifs of the potyviruses were identified in the polyprotein and within individual proteins. Phylogenetic analysis indicated that the virus is most closely related to members of the BCMV subgroup. The results suggest that the virus should be classified as a novel species within the genus Potyvirus, which we tentatively name "Paris mosaic necrosis virus". [Mh] Termos MeSH primário: Genoma Viral Melanthiaceae/virologia Filogenia Potyvirus/genética RNA Viral/genética [Mh] Termos MeSH secundário: Sequência de Aminoácidos Tamanho do Genoma Sequenciamento de Nucleotídeos em Larga Escala Fases de Leitura Aberta Doenças das Plantas/virologia Poliproteínas Potyvirus/classificação Potyvirus/isolamento & purificação Homologia de Sequência de Aminoácidos [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: 0 (Polyproteins); 0 (RNA, Viral) [Em] Mês de entrada: 1802 [Cu] Atualização por classe: 180220 [Lr] Data última revisão: 180220 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 171201 [St] Status: MEDLINE [do] DOI: 10.1007/s00705-017-3649-x

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[PMID]: 27823618 [Au] Autor: Hsieh MJ; Chien SY; Lin JT; Yang SF; Chen MK [Ad] Endereço: Cancer Research Center, Changhua Christian Hospital, Changhua, 50006, Taiwan; School of Optometry, Chung Shan Medical University, Taichung, 40201, Taiwan; Graduate Institute of Biomedical Sciences, China Medical University, Taichung, 404, Taiwan. Electronic address: 170780@cch.org.tw. [Ti] Título: Polyphyllin G induces apoptosis and autophagy cell death in human oral cancer cells. [So] Source: Phytomedicine;23(13):1545-1554, 2016 Dec 01. [Is] ISSN: 1618-095X [Cp] País de publicação: Germany [La] Idioma: eng [Ab] Resumo: BACKGROUND: Polyphyllin G (also called polyphyllin VII), extract from rhizomes of Paris yunnanensis Franch, has been shown to have strong anticancer activities in a wide variety of human cancer cell lines. However, the underlying influences of autophagy in human oral squamous cell carcinoma (OSCC) remain unclear. METHODS: In this study, the roles of apoptosis and autophagy in polyphyllin G-induced death in human oral cancer cells were investigated. Moreover, the molecular mechanism of the anticancer effects of polyphyllin G in human oral cancer cells was investigated. RESULTS: The results revealed that polyphyllin G significantly inhibited cell proliferation in human oral cancer cells; it dose-dependently induced apoptosis in SAS and OECM-1 cells through caspase-3, -8, and -9 activation and poly (ADP-ribose) polymerase cleavage. In addition, changes were observed in Bcl-2 and proapoptosis-related protein expression in different human oral cancer cell lines. The expression of both LC3-II and beclin-1 was markedly increased, suggesting the induction of autophagy in polyphyllin G-treated oral cells. To further clarify whether polyphyllin G-induced apoptosis and autophagy depended on Akt/extracellular signal-regulated kinases (ERK)/c-Jun N-terminal kinases (JNK)/p38 mitogen-activated protein kinases (MAPK) signaling pathways, the cells were cotreated with inhibitors. The results demonstrated polyphyllin G-induced apoptosis in oral cells through the activation of ERK, Akt, p38 MAPK, and JNK, whereas ERK and JNK accounted for polyphyllin G-induced autophagy. CONCLUSION: This study is the first to demonstrate apoptosis and autophagy during polyphyllin G-induced cell death in human oral cancer cell lines. These results suggest that polyphyllin G is a promising candidate for developing antitumor drugs targeting human oral squamous cell carcinoma. [Mh] Termos MeSH primário: Antineoplásicos Fitogênicos/farmacologia Apoptose/efeitos dos fármacos Autofagia/efeitos dos fármacos Melanthiaceae/química Neoplasias Bucais/tratamento farmacológico Saponinas/farmacologia [Mh] Termos MeSH secundário: Caspases/metabolismo Linhagem Celular Tumoral Proliferação Celular/efeitos dos fármacos Relação Dose-Resposta a Droga MAP Quinases Reguladas por Sinal Extracelular/metabolismo Seres Humanos Proteínas Quinases JNK Ativadas por Mitógeno/metabolismo Neoplasias Bucais/patologia Extratos Vegetais/farmacologia Poli(ADP-Ribose) Polimerases/metabolismo Proteínas Quinases p38 Ativadas por Mitógeno/metabolismo [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: 0 (Antineoplastic Agents, Phytogenic); 0 (Plant Extracts); 0 (Saponins); 0 (polyphyllin VII); EC 2.4.2.30 (Poly(ADP-ribose) Polymerases); EC 2.7.11.24 (Extracellular Signal-Regulated MAP Kinases); EC 2.7.11.24 (JNK Mitogen-Activated Protein Kinases); EC 2.7.11.24 (p38 Mitogen-Activated Protein Kinases); EC 3.4.22.- (Caspases) [Em] Mês de entrada: 1706 [Cu] Atualização por classe: 170817 [Lr] Data última revisão: 170817 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 161109 [St] Status: MEDLINE

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[PMID]: 27644244 [Au] Autor: Ke JY; Zhang W; Gong RS; Cen WJ; Huang HQ; Li YR; Kong WD; Jiang JW [Ad] Endereço: Department of Stomatology, The First Affiliated Hospital of Jinan University, Guangzhou, 510630, China. [Ti] Título: A monomer purified from Paris polyphylla (PP-22) triggers S and G2/M phase arrest and apoptosis in human tongue squamous cell carcinoma SCC-15 by activating the p38/cdc25/cdc2 and caspase 8/caspase 3 pathways. [So] Source: Tumour Biol;37(11):14863-14872, 2016 Nov. [Is] ISSN: 1423-0380 [Cp] País de publicação: United States [La] Idioma: eng [Ab] Resumo: Recent studies have shown that the aqueous, ethanolic extracts and a monomer compound of Paris polyphylla exhibit anticancer activity toward several types of cancer cell lines, but the anticancer activity of (3ß,17α,25R)-spirost-5-ene-3,17-diol 3-O-α-L-rhamnopyranosyl-(1 â†’ 2)-ß-D-glucopyranoside, a monomer isolated from P. polyphylla (PP), named PP-22, has not been reported previously. In this study, we investigated the effect of PP-22 on human tongue squamous cell carcinoma SCC-15 cells in vitro. MTT assays showed that PP-22 inhibited the growth of SCC-15 cells and had no obvious inhibitory effects on human liver L02 cells. Flow cytometry assays showed that the percentages of apoptotic cells were increased. In addition, cleaved caspase-8, cleaved caspase-3 and cleaved poly (ADP-ribose) polymerase (PARP) could be detected by Western blotting. Flow cytometry also showed that PP-22 triggered S and G2/M phases arrest in SCC-15 cells, and on the other hand, the expression of cyclin A, cyclin E2, cyclin B1, phospho-cell division cycle2 (p-cdc2)(Tyr15), p-Wee1, Myt1, and p53 was upregulated. Moreover, p-p38 levels increased, p-extracellular signal-regulated kinase (ERK) levels decreased, and cdc25B expression was inhibited. Furthermore, the p38/mitogen-activated protein kinase (MAPK) inhibitor SB203580 reversed the increase of the expression level of p38, p-cdc2 (Tyr15), cleaved caspase 3, cleaved PARP, p-p53, and p53 and reversed the decrease in cdc25B expression. In conclusion, these results demonstrated that PP-22 activated p38, inhibited cdc25B, increased p-cdc2 (Tyr15), and triggered S and G2/M phase arrest, as well as activated p53 through the p38-p53 pathway, inhibited the MAPK/ERK pathway, activated the caspase 8/caspase 3 pathway, and triggered the extrinsic apoptotic pathway in SCC-15 cells. [Mh] Termos MeSH primário: Caspase 3/metabolismo Caspase 8/metabolismo Quinases Ciclina-Dependentes/metabolismo Pontos de Checagem da Fase G2 do Ciclo Celular/efeitos dos fármacos Pontos de Checagem da Fase S do Ciclo Celular/efeitos dos fármacos Saponinas/farmacologia Fosfatases cdc25/metabolismo Proteínas Quinases p38 Ativadas por Mitógeno/metabolismo [Mh] Termos MeSH secundário: Antineoplásicos Fitogênicos/farmacologia Apoptose/efeitos dos fármacos Proteína Quinase CDC2 Carcinoma de Células Escamosas/tratamento farmacológico Proteínas de Ciclo Celular Linhagem Celular Tumoral Proliferação Celular/efeitos dos fármacos Ciclina A1/biossíntese Ciclina B1/biossíntese Ciclinas/biossíntese Proteínas de Ligação a DNA/biossíntese Seres Humanos Imidazóis/farmacologia Melanthiaceae/metabolismo Proteínas Nucleares Extratos Vegetais/farmacologia Poli(ADP-Ribose) Polimerases/metabolismo Proteínas Tirosina Quinases Piridinas/farmacologia Neoplasias da Língua/tratamento farmacológico Fatores de Transcrição/biossíntese Proteína Supressora de Tumor p53/biossíntese Proteínas Quinases p38 Ativadas por Mitógeno/antagonistas & inibidores [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: 0 (Antineoplastic Agents, Phytogenic); 0 (CCNA1 protein, human); 0 (CCNB1 protein, human); 0 (CCNE2 protein, human); 0 (Cell Cycle Proteins); 0 (Cyclin A1); 0 (Cyclin B1); 0 (Cyclins); 0 (DNA-Binding Proteins); 0 (Imidazoles); 0 (MYT1 protein, human); 0 (Nuclear Proteins); 0 (Plant Extracts); 0 (Pyridines); 0 (Saponins); 0 (Transcription Factors); 0 (Tumor Suppressor Protein p53); 0 (spirost-5-ene-3,17-diol 3-O-rhamnopyranosyl-(1-2)-glucopyranoside); EC 2.4.2.30 (Poly(ADP-ribose) Polymerases); EC 2.7.10.1 (Protein-Tyrosine Kinases); EC 2.7.10.2 (WEE1 protein, human); EC 2.7.11.22 (CDC2 Protein Kinase); EC 2.7.11.22 (CDK1 protein, human); EC 2.7.11.22 (Cyclin-Dependent Kinases); EC 2.7.11.24 (p38 Mitogen-Activated Protein Kinases); EC 3.1.3.48 (CDC25A protein, human); EC 3.1.3.48 (CDC25B protein, human); EC 3.1.3.48 (cdc25 Phosphatases); EC 3.4.22.- (Caspase 3); EC 3.4.22.- (Caspase 8); OU13V1EYWQ (SB 203580) [Em] Mês de entrada: 1702 [Cu] Atualização por classe: 171116 [Lr] Data última revisão: 171116 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 160921 [St] Status: MEDLINE

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[PMID]: 27469463 [Au] Autor: Yang LL; Jiang Z; Tang SK; Chu X; Xu LH; Zhi XY [Ad] Endereço: 1​The Key Laboratory for Microbial Resources of Ministry of Education, and Laboratory for Conservation and Utilization of Bio-Resources, Yunnan Institute of Microbiology, Yunnan University, Kunming 650091, PR China. [Ti] Título: Yimella radicis sp. nov., an endophytic actinobacterium isolated from the root of Paris polyphylla Smith var. yunnanensis. [So] Source: Int J Syst Evol Microbiol;66(10):4191-4196, 2016 Oct. [Is] ISSN: 1466-5034 [Cp] País de publicação: England [La] Idioma: eng [Ab] Resumo: An endophytic actinobacterial strain, designated py1292T, was isolated from the root of Paris polyphylla Smith var. yunnanensis collected from Yunnan province, China, and subjected to a polyphasic taxonomic characterization. Phylogenetic analysis based on 16S rRNA gene sequences placed the isolate in the family Dermacoccaceae and clustered with Yimella lutea (showing the highest similarity of 99.1 %). DNA-DNA relatedness between strain py1292T and Y. lutea YIM 45900T was 45.6±3.2 % (reciprocal 47.8±3.6 %). The novel isolate was found to be a Gram-staining-positive rod, catalase- and oxidase-positive. It grew at pH 6.0-8.0, with 0-9 % NaCl and at 20-45 ºC, optimally at pH 7.0, with 0-3 % NaCl and at 28 ºC. The predominant menaquinone was MK-8(H4), while the polar lipids were diphosphatidylglycerol, phosphatidylglycerol, phosphatidylinositol, phosphatidylinositol mannoside, two unknown phospholipids and two unknown polar lipids. The major cellular fatty acids were iso-C15 : 0, iso-C16 : 0, iso-C17 : 0 and anteiso-C17 : 0. The whole-cell hydrolysates contained mannose, ribose, rhamnose, glucose and galactose. The peptidoglycan contained alanine, glycine, serine, aspartic acid, glutamic acid and lysine. The genomic DNA G+C content was determined to be 65.6 mol%. Phylogenetic, phenotypic and chemotaxonomic data (especially the same peptidoglycan type) showed that strain py1292T should be classified as a representative of a novel species of the genus Yimella, for which the name Yimella radicis sp. nov. is proposed. The type strain is py1292T (=KCTC 39612T=LMG 29070T). [Mh] Termos MeSH primário: Actinomycetales/classificação Melanthiaceae/microbiologia Filogenia Raízes de Plantas/microbiologia [Mh] Termos MeSH secundário: Actinomycetales/genética Actinomycetales/isolamento & purificação Técnicas de Tipagem Bacteriana Composição de Bases Parede Celular/química China DNA Bacteriano/genética DNA Ribossômico/genética Ácidos Graxos/química Hibridização de Ácido Nucleico Peptidoglicano/química Fosfolipídeos/química RNA Ribossômico 16S/genética Análise de Sequência de DNA Vitamina K 2/análogos & derivados Vitamina K 2/química [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: 0 (DNA, Bacterial); 0 (DNA, Ribosomal); 0 (Fatty Acids); 0 (Peptidoglycan); 0 (Phospholipids); 0 (RNA, Ribosomal, 16S); 11032-49-8 (Vitamin K 2); 523-38-6 (vitamin MK 8) [Em] Mês de entrada: 1708 [Cu] Atualização por classe: 170817 [Lr] Data última revisão: 170817 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 160730 [St] Status: MEDLINE [do] DOI: 10.1099/ijsem.0.001334

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[PMID]: 27396351 [Au] Autor: Hong Y; Han YQ; Wang YZ; Gao JR; Li YX; Liu Q; Xia LZ [Ad] Endereço: Anhui University of Chinese Medicine, Hefei, Anhui 230031, China. Electronic address: hyan2003@163.com. [Ti] Título: Paridis Rhizoma Sapoinins attenuates liver fibrosis in rats by regulating the expression of RASAL1/ERK1/2 signal pathway. [So] Source: J Ethnopharmacol;192:114-122, 2016 Nov 04. [Is] ISSN: 1872-7573 [Cp] País de publicação: Ireland [La] Idioma: eng [Ab] Resumo: ETHNO-PHARMACOLOGICAL RELEVANCE: Paridis Rhizoma is a Chinese medicinal herb that has been used in liver disease treatment for thousands of years. Our previous studies found that Paridis Rhizoma saponins (PRS) are the critical components of Paridis Rhizoma which has good liver protection effect. However, the anti-hepatic fibrosis effect and the mechanism of PRS have seldom been reported. AIM OF THE STUDY: To investigate the potential of PRS in the treatment of experimental liver fibrosis and the underlying mechanism. MATERIALS AND METHODS: The chemical feature fingerprint of PRS was analyzed by UPLC-PDA. A total of 40 Male Sprague-Dawley (SD) rats were randomly divided into the control group, the model group, the PRS high dose group (PRS H) and the PRS low dose group (PRS L) with 10 rats in each group. The model, PRS H and L groups as liver fibrosis models were established with carbon tetrachloride (CCl ) method. PRS H and L groups were adopted PRS (300 and 150mg/kgd ) treatment since the twelfth week of modeling till the sixteenth week. Pathological changes in hepatic tissue were examined using hematoxylin and eosin (H&E) and MASSON trichrome staining. Immunohistochemical analysis was performed to determine the protein expression of the RASAL1. RT-PCR and western blotting were used to detect the expression of ERK1/2 mRNA and protein. RESULTS: Four saponins in PRS were identified from 19 detected chromatographic peaks on UPLC-PDA by comparing to the standard compounds. PRS can improve the degeneration and necrosis of hepatic tissue, reduce the extent of its fibrous hyperplasia according to H&E and MASSON staining detection. As was detected in PRS H and L groups, PRS down-regulated p-ERK1/2 mRNA and RASAL1 protein, and up-regulated the level of p-ERK1/2 mRNA and RASAL1 protein. CONCLUSION: These results demonstrated that PRS can attenuate CCl -induced liver fibrosis through the regulation of RAS/ERK1/2 signal pathway. [Mh] Termos MeSH primário: Doença Hepática Induzida por Substâncias e Drogas/prevenção & controle Proteínas Ativadoras de GTPase/metabolismo Cirrose Hepática Experimental/prevenção & controle Fígado/efeitos dos fármacos Melanthiaceae/química Proteína Quinase 1 Ativada por Mitógeno/metabolismo Proteína Quinase 3 Ativada por Mitógeno/metabolismo Extratos Vegetais/farmacologia Saponinas/farmacologia [Mh] Termos MeSH secundário: Animais Western Blotting Tetracloreto de Carbono Doença Hepática Induzida por Substâncias e Drogas/enzimologia Doença Hepática Induzida por Substâncias e Drogas/patologia Cromatografia Líquida de Alta Pressão Citoproteção Proteínas Ativadoras de GTPase/genética Regulação Enzimológica da Expressão Gênica Hiperplasia Imuno-Histoquímica Fígado/enzimologia Fígado/patologia Cirrose Hepática Experimental/induzido quimicamente Cirrose Hepática Experimental/enzimologia Cirrose Hepática Experimental/patologia Masculino Proteína Quinase 1 Ativada por Mitógeno/genética Proteína Quinase 3 Ativada por Mitógeno/genética Necrose Fosforilação Fitoterapia Extratos Vegetais/isolamento & purificação Plantas Medicinais RNA Mensageiro/genética RNA Mensageiro/metabolismo Ratos Sprague-Dawley Reação em Cadeia da Polimerase Via Transcriptase Reversa Saponinas/isolamento & purificação Transdução de Sinais/efeitos dos fármacos [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: 0 (GTPase-Activating Proteins); 0 (Plant Extracts); 0 (RASAL1 protein, rat); 0 (RNA, Messenger); 0 (Saponins); CL2T97X0V0 (Carbon Tetrachloride); EC 2.7.11.24 (Mapk1 protein, rat); EC 2.7.11.24 (Mitogen-Activated Protein Kinase 1); EC 2.7.11.24 (Mitogen-Activated Protein Kinase 3) [Em] Mês de entrada: 1704 [Cu] Atualização por classe: 170912 [Lr] Data última revisão: 170912 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 160712 [St] Status: MEDLINE

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[PMID]: 27271583 [Au] Autor: Wang CW; Tai CJ; Choong CY; Lin YC; Lee BH; Shi YC; Tai CJ [Ad] Endereço: Department of Obstetrics and Gynecology, School of Medicine, College of Medicine, Taipei Medical University, Taipei 11042, Taiwan. cwwang@ms4.hinet.net. [Ti] Título: Aqueous Extract of Paris polyphylla (AEPP) Inhibits Ovarian Cancer via Suppression of Peroxisome Proliferator-Activated Receptor-Gamma Coactivator (PGC)-1alpha. [So] Source: Molecules;21(6), 2016 Jun 03. [Is] ISSN: 1420-3049 [Cp] País de publicação: Switzerland [La] Idioma: eng [Ab] Resumo: Chemotherapy, a major approach was used in carcinoma treatment, always involves the development of drug resistance as well as side-effects that affect the quality of patients' lives. An association between epithelial-mesenchymal transition (EMT) and chemotherapy resistance was established recently. We demonstrate in this paper that the aqueous extract of Paris polyphylla (AEPP)-a traditional Chinese medicine-can be used in various cancer types for suppression of carcinogenesis. We evaluated the suppressions of EMT and mitochondrial activity by AEPP treatment in a high-glucose (HG) induced-human ovarian carcinoma cell line (OVCAR-3 cells). The mitochondrial morphology was investigated using MitoTracker Deep Red FM staining. Our results indicated that AEPP reduced the viability of OVCAR-3 cells considerably through induction of apoptosis. However, this inhibitory potential of AEPP was attenuated by HG induction in OVCAR-3 cells. The levels of estrogen-related receptor (ERR)-alpha activator and peroxisome proliferator-activated receptor-gamma coactivator (PGC)-1alpha were elevated by HG induction, but were suppressed by AEPP treatment. Down-regulations of cell survival and EMT were oberved in OVCAR-3 cells through suppression of PGC-1alpha by AEPP treatment. These results were confirmed through PGC-1alpha knockdown and overexpression in OVCAR-3 cells. Thus, AEPP can be beneficial for treating ovarian cancer and has potential for development of an integrative cancer therapy against ovarian cancer proliferation, metastasis, and migration. [Mh] Termos MeSH primário: Melanthiaceae/química Neoplasias Ovarianas/tratamento farmacológico Coativador 1-alfa do Receptor gama Ativado por Proliferador de Peroxissomo/biossíntese Extratos Vegetais/administração & dosagem [Mh] Termos MeSH secundário: Apoptose/efeitos dos fármacos Proliferação Celular/efeitos dos fármacos Sobrevivência Celular/efeitos dos fármacos Feminino Regulação Neoplásica da Expressão Gênica/efeitos dos fármacos Seres Humanos Medicina Tradicional Chinesa Neoplasias Ovarianas/patologia Coativador 1-alfa do Receptor gama Ativado por Proliferador de Peroxissomo/genética Extratos Vegetais/química [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: 0 (PPARGC1A protein, human); 0 (Peroxisome Proliferator-Activated Receptor Gamma Coactivator 1-alpha); 0 (Plant Extracts) [Em] Mês de entrada: 1704 [Cu] Atualização por classe: 170424 [Lr] Data última revisão: 170424 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 160609 [St] Status: MEDLINE

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[PMID]: 27059624 [Au] Autor: Yang LL; Tang SK; Chu X; Jiang Z; Xu LH; Zhi XY [Ad] Endereço: Key Laboratory of Microbial Diversity in Southwest China, Ministry of Education and the Laboratory for Conservation and Utilization of Bio-Resources, Yunnan Institute of Microbiology, Yunnan University, Kunming, China. [Ti] Título: Oceanobacillus endoradicis sp. nov., an endophytic bacterial species isolated from the root of Paris polyphylla Smith var. yunnanensis. [So] Source: Antonie Van Leeuwenhoek;109(7):957-64, 2016 Jul. [Is] ISSN: 1572-9699 [Cp] País de publicação: Netherlands [La] Idioma: eng [Ab] Resumo: A bacterial strain, py1294(T), isolated from a root of Paris polyphylla Smith var. yunnanensis collected from Yunnan province, southwest China, was characterised by using a polyphasic approach to clarify its taxonomic position. Strain py1294(T) was found to be Gram-positive, aerobic, spore-forming, peritrichous flagella and rod shaped. Growth was found to occur in the presence of 0-8 % (w/v) NaCl (optimum 1-3 %), at pH 6.5-9.5 (optimum 8.0) and at 10-42 °C (optimum 30 °C). The major cellular fatty acids were identified as anteiso-C15:0, anteiso-C17:0, iso-C16:0 and iso-C14:0. The predominant quinone was identified as MK-7 and a minor amount of MK-6 was detected. The diagnostic polar lipids were diphosphatidylglycerol, phosphatidylglycerol and phosphatidylethanolamine. The cell wall peptidoglycan was found to contain meso-diaminopimelic acid. Phylogenetic analysis of the 16S rRNA gene sequence showed that strain py1294(T) forms a well-supported clade with Oceanobacillus damuensis PT-20(T) (97.9 % sequence similarity) within the genus Oceanobacillus, although it also shares a high sequence similarity with Ornithinibacillus contaminans (97.5 %). Crucially, the DNA-DNA relatedness value between strain py1294(T) and O. damuensis PT-20(T) was 29.7 ± 3.2 %. The G+C content was determined to be 42.3 mol%. On the basis of the phylogenetic and phenotypic data, a novel species Oceanobacillus endoradicis sp. nov. is proposed, with py1294(T) (=DSM 100726(T) = KCTC 33731(T)) as the type strain. [Mh] Termos MeSH primário: Bacillaceae/classificação Bacillaceae/isolamento & purificação Melanthiaceae/microbiologia Raízes de Plantas/microbiologia [Mh] Termos MeSH secundário: Bacillaceae/genética Bacillaceae/metabolismo China Ácido Diaminopimélico/metabolismo Ácidos Graxos/metabolismo Hibridização de Ácido Nucleico Peptidoglicano/metabolismo Fenótipo Fosfolipídeos/metabolismo Filogenia RNA Ribossômico 16S/genética Análise de Sequência de DNA Cloreto de Sódio/metabolismo Microbiologia do Solo Vitamina K 2/análogos & derivados Vitamina K 2/metabolismo [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: 0 (Fatty Acids); 0 (Peptidoglycan); 0 (Phospholipids); 0 (RNA, Ribosomal, 16S); 11032-49-8 (Vitamin K 2); 451W47IQ8X (Sodium Chloride); 583-93-7 (Diaminopimelic Acid); 71ANL51TLA (menaquinone 6); 8427BML8NY (vitamin MK 7) [Em] Mês de entrada: 1703 [Cu] Atualização por classe: 170302 [Lr] Data última revisão: 170302 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 160410 [St] Status: MEDLINE [do] DOI: 10.1007/s10482-016-0695-4

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3	and or and not		PalavrasDescritor de assuntoDescritor de assunto primárioLimitesAutorPalavras do títuloPalavras do resumoIdiomaPaís de publicaçãoNome de substânciaNome de pessoa como assuntoRevistaAssunto de RevistaISSNTipo de publicaçãoIdentificador únicoMês de entradaAno de publicaçãoTexto completoAtualização por classeCategoria DeCSCategoria DeCS explodidaCategoria CID-10SubSetsPais de AfiliaçãoAfiliaçãoAfiliação 2

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BIREME/OPAS/OMS - Centro Latino-Americano e do Caribe de Informação em Ciências da Saúde