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[PMID]:28692662
[Au] Autor:Cao S; Shen D; Wang Y; Li L; Zhou L; Wang Y
[Ad] Endereço:The Second Affiliated Hospital and Yuying Children's Hospital of Wenzhou Medical University, Wenzhou, Zhejiang, China.
[Ti] Título:Potential malignant transformation in the gastric mucosa of immunodeficient mice with persistent Mycoplasma penetrans infection.
[So] Source:PLoS One;12(7):e0180514, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Mycoplasma infection has been reported in immunocompromised cancer patients; nevertheless, it is not clear if persistent Mycoplasma infection could facilitate the proliferation of cancer cells in immunocompromised organisms. The aim of this study was to examine the relationship between persistent Mycoplasma infection and malignant transformation in an immunodeficient host model. Immunodeficient mouse model was established using cyclophosphamide and mice gastric mucosal cells were infected with Mycoplasma penetrans (Mpe). After 18 weeks, mice were sacrificed and gastric mucosal Mpe infected cells were identified by fluorescence in situ hybridization (FISH). Moreover, pathological and ultrastructural changes in mice gastric mucosa were evaluated and the expression of multiple proto-oncogenes was examined by Western blot. Our data show that Mpe infection was detected in the blood of immunodeficient mice and Mpe persistent infection in mice gastric mucosa was confirmed by FISH. There were pathological and ultrastructural malignant transformation occurred in the gastric mucosa of infected mice compared to control mice. Mpe infected mice showed lower expression of p53 and p21 and higher H-ras expression compared to the control group. Moreover, expression of NF-κB p65 subunit increased in Mpe infected mice, similar to the TNF-α expression. Bax expression in gastric mucosa of Mpe infected mice was lower while Bcl-2 expression was higher than in the uninfected control group. Collectively these data demonstrate that persistent Mpe infection is associated with aberrant expression of multiple proto-oncogenes in gastric mucosa of immunodeficient mice which potentially facilitate the malignant transformation.
[Mh] Termos MeSH primário: Transformação Celular Neoplásica/patologia
Mucosa Gástrica/microbiologia
Mucosa Gástrica/patologia
Infecções por Mycoplasma/microbiologia
Infecções por Mycoplasma/patologia
Mycoplasma penetrans/fisiologia
[Mh] Termos MeSH secundário: Animais
Apoptose
Inibidor de Quinase Dependente de Ciclina p21/metabolismo
Feminino
Mucosa Gástrica/ultraestrutura
Camundongos Endogâmicos C57BL
Camundongos SCID
Infecções por Mycoplasma/diagnóstico
Mycoplasma penetrans/ultraestrutura
NF-kappa B/metabolismo
Transdução de Sinais
Fator de Necrose Tumoral alfa/metabolismo
Proteína Supressora de Tumor p53/metabolismo
Proteína X Associada a bcl-2/metabolismo
Proteínas ras/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cyclin-Dependent Kinase Inhibitor p21); 0 (NF-kappa B); 0 (Tumor Necrosis Factor-alpha); 0 (Tumor Suppressor Protein p53); 0 (bcl-2-Associated X Protein); EC 3.6.5.2 (ras Proteins)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170925
[Lr] Data última revisão:
170925
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170711
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0180514


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[PMID]:28373274
[Au] Autor:Distelhorst SL; Jurkovic DA; Shi J; Jensen GJ; Balish MF
[Ad] Endereço:Department of Microbiology, Miami University, Oxford, Ohio, USA.
[Ti] Título:The Variable Internal Structure of the Mycoplasma penetrans Attachment Organelle Revealed by Biochemical and Microscopic Analyses: Implications for Attachment Organelle Mechanism and Evolution.
[So] Source:J Bacteriol;199(12), 2017 Jun 15.
[Is] ISSN:1098-5530
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Although mycoplasmas have small genomes, many of them, including the HIV-associated opportunist , construct a polar attachment organelle (AO) that is used for both adherence to host cells and gliding motility. However, the irregular phylogenetic distribution of similar structures within the mycoplasmas, as well as compositional and ultrastructural differences among these AOs, suggests that AOs have arisen several times through convergent evolution. We investigated the ultrastructure and protein composition of the cytoskeleton-like material of the AO with several forms of microscopy and biochemical analysis, to determine whether the AO was constructed at the molecular level on principles similar to those of other mycoplasmas, such as and We found that the AO interior was generally dissimilar from that of other mycoplasmas, in that it exhibited considerable heterogeneity in size and shape, suggesting a gel-like nature. In contrast, several of the 12 potential protein components identified by mass spectrometry of detergent-insoluble proteins shared certain distinctive biochemical characteristics with AO proteins, although not with proteins. We conclude that convergence between and AOs extends to the molecular level, leading to the possibility that the less organized material in both and is the substance principally responsible for the organization and function of the AO. is a bacterium that infects HIV-positive patients and may contribute to the progression of AIDS. It attaches to host cells through a structure called an AO, but it is not clear how it builds this structure. Our research is significant not only because it identifies the novel protein components that make up the material within the AO that give it its structure but also because we find that the AO is organized unlike AOs from other mycoplasmas, suggesting that similar structures have evolved multiple times. From this work, we derive some basic principles by which mycoplasmas, and potentially all organisms, build structures at the subcellular level.
[Mh] Termos MeSH primário: Estruturas Bacterianas/química
Estruturas Bacterianas/ultraestrutura
Mycoplasma penetrans/química
Mycoplasma penetrans/ultraestrutura
Organelas/química
Organelas/ultraestrutura
[Mh] Termos MeSH secundário: Evolução Biológica
Espectrometria de Massas
Mycoplasma pneumoniae/química
Mycoplasma pneumoniae/fisiologia
Mycoplasma pneumoniae/ultraestrutura
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171126
[Lr] Data última revisão:
171126
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170405
[St] Status:MEDLINE


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[PMID]:27087524
[Au] Autor:Han RZ; Xu GC; Dong JJ; Ni Y
[Ad] Endereço:Key Laboratory of Carbohydrate Chemistry and Biotechnology, Ministry of Education, School of Biotechnology, Jiangnan University, Wuxi, 214122, China.
[Ti] Título:Arginine deiminase: recent advances in discovery, crystal structure, and protein engineering for improved properties as an anti-tumor drug.
[So] Source:Appl Microbiol Biotechnol;100(11):4747-60, 2016 Jun.
[Is] ISSN:1432-0614
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Arginine deiminase (ADI) is an important arginine-degrading enzyme with wide applications, in particular as an anti-cancer agent for the therapy of arginine-auxotrophic tumors. In recent years, novel ADIs with excellent properties have been identified from various organisms, and crystal structures of ADI were investigated. To satisfy the requirements of potential therapeutic applications, protein engineering has been performed to improve the activity and properties of ADIs. In this mini-review, we systematically summarized the latest progress on identification and crystal structure of ADIs, and protein engineering strategies for improved enzymatic properties, such as pH optimum, K m and k cat values, and thermostability. We also outlined the PEGylation of ADI for improved circulating half-life and immunogenicity, as well as their performance in clinical trials. Finally, perspectives on extracellular secretion and property improvement of ADI were discussed.
[Mh] Termos MeSH primário: Antineoplásicos/química
Hidrolases/química
Engenharia de Proteínas
[Mh] Termos MeSH secundário: Animais
Antineoplásicos/farmacologia
Linhagem Celular Tumoral
Ensaios Clínicos como Assunto
Modelos Animais de Doenças
Sinergismo Farmacológico
Seres Humanos
Concentração de Íons de Hidrogênio
Hidrolases/farmacologia
Mycoplasma/classificação
Mycoplasma/enzimologia
Mycoplasma penetrans/enzimologia
Neoplasias/tratamento farmacológico
Conformação Proteica
Pseudomonas aeruginosa/enzimologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Antineoplastic Agents); EC 3.- (Hydrolases); EC 3.5.3.6 (arginine deiminase)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:170207
[Lr] Data última revisão:
170207
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160419
[St] Status:MEDLINE
[do] DOI:10.1007/s00253-016-7490-z


  4 / 66 MEDLINE  
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[PMID]:25792346
[Au] Autor:Chen LS; Wu JR; Wang B; Yang T; Yuan R; Zhao YY; Xu JS; Guo HX; Huan XP
[Ad] Endereço:Key Laboratory of Environmental Medicine and Engineering, Ministry of Education;Department of Epidemiology and Statistics,School of Public Health, Southeast University,Nanjing,Jiangsu,People's Republic of China.
[Ti] Título:Epidemiology of Mycoplasma acquisition in male HIV-1 infected patients: a multistage cross-sectional survey in Jiangsu, China.
[So] Source:Epidemiol Infect;143(15):3327-34, 2015 Nov.
[Is] ISSN:1469-4409
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Mycoplasma infections are most frequently associated with disease in the urogenital or respiratory tracts and, in most cases, mycoplasmas infect the host persistently. In HIV-infected individuals the prevalence and role of genital mycoplasmas has not been well studied. To investigate the six species of Mycoplasma and the risk factors for infection in Jiangsu province, first-void urine and venous blood samples were collected and epidemiological questionnaires were administered after informed consent. A total of 1541 HIV/AIDS patients were recruited in this study. The overall infection rates of six Mycoplasma species were: Ureaplasma urealyticum (26·7%), Mycoplasma hominis (25·3%), M. fermentans (5·1%), M. genitalium (20·1%), M. penetrans (1·6%) and M. pirum (15·4%). The Mycoplasma infection rate in the unmarried group was lower than that of the married, divorced and widowed groups [adjusted odds ratio (aOR) 1·432, 95% confidence interval (CI) 1·077-1·904, P < 0·05]. The patients who refused highly active antiretroviral therapy (HAART) had a much higher risk of Mucoplasma infection (aOR 1·357, 95% CI 1·097-1·679, P < 0·05). Otherwise, a high CD4+ T cell count was a protective factor against Mycoplasma infection (aOR 0·576, 95% CI 0·460-0·719, P < 0·05). Further research will be required to confirm a causal relationship and to identify risk factors for Mycoplasma infection in HIV/AIDS populations.
[Mh] Termos MeSH primário: Terapia Antirretroviral de Alta Atividade/estatística & dados numéricos
Infecções por HIV/epidemiologia
Estado Civil/estatística & dados numéricos
Infecções por Mycoplasma/epidemiologia
Infecções por Ureaplasma/epidemiologia
[Mh] Termos MeSH secundário: Adolescente
Adulto
Idoso
China/epidemiologia
Coinfecção/epidemiologia
Estudos Transversais
Infecções por HIV/tratamento farmacológico
HIV-1
Seres Humanos
Masculino
Meia-Idade
Mycoplasma/genética
Mycoplasma/isolamento & purificação
Infecções por Mycoplasma/microbiologia
Mycoplasma fermentans/genética
Mycoplasma fermentans/isolamento & purificação
Mycoplasma genitalium/genética
Mycoplasma genitalium/isolamento & purificação
Mycoplasma hominis/genética
Mycoplasma hominis/isolamento & purificação
Mycoplasma penetrans/genética
Mycoplasma penetrans/isolamento & purificação
Reação em Cadeia da Polimerase
Prevalência
Fatores de Risco
Ureaplasma urealyticum/genética
Ureaplasma urealyticum/isolamento & purificação
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Em] Mês de entrada:1512
[Cu] Atualização por classe:150930
[Lr] Data última revisão:
150930
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150321
[St] Status:MEDLINE
[do] DOI:10.1017/S0950268815000461


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[PMID]:23248272
[Au] Autor:Wojciechowski M; Czapinska H; Bochtler M
[Ad] Endereço:Laboratory of Structural Biology, International Institute of Molecular and Cell Biology, 02-109, Warsaw, Poland.
[Ti] Título:CpG underrepresentation and the bacterial CpG-specific DNA methyltransferase M.MpeI.
[So] Source:Proc Natl Acad Sci U S A;110(1):105-10, 2013 Jan 02.
[Is] ISSN:1091-6490
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Cytosine methylation promotes deamination. In eukaryotes, CpG methylation is thought to account for CpG underrepresentation. Whether scarcity of CpGs in prokaryotic genomes is diagnostic for methylation is not clear. Here, we report that Mycoplasms tend to be CpG depleted and to harbor a family of constitutively expressed or phase variable CpG-specific DNA methyltransferases. The very CpG poor Mycoplasma penetrans and its constitutively active CpG-specific methyltransferase M.MpeI were chosen for further characterization. Genome-wide sequencing of bisulfite-converted DNA indicated that M.MpeI methylated CpG target sites both in vivo and in vitro in a locus-nonselective manner. A crystal structure of M.MpeI with DNA at 2.15-Å resolution showed that the substrate base was flipped and that its place in the DNA stack was taken by a glutamine residue. A phenylalanine residue was intercalated into the "weak" CpG step of the nonsubstrate strand, indicating mechanistic similarities in the recognition of the short CpG target sequence by prokaryotic and eukaryotic DNA methyltransferases.
[Mh] Termos MeSH primário: Ilhas de CpG/genética
DNA (Citosina-5-)-Metiltransferases/química
DNA (Citosina-5-)-Metiltransferases/metabolismo
DNA/química
Modelos Moleculares
Mycoplasma penetrans/enzimologia
Mycoplasma penetrans/genética
[Mh] Termos MeSH secundário: Sequência de Bases
Clonagem Molecular
Cristalização
DNA/metabolismo
Desaminação
Sequenciamento de Nucleotídeos em Larga Escala
Dados de Sequência Molecular
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
9007-49-2 (DNA); EC 2.1.1.37 (DNA (Cytosine-5-)-Methyltransferases)
[Em] Mês de entrada:1302
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:121219
[St] Status:MEDLINE
[do] DOI:10.1073/pnas.1207986110


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[PMID]:23066969
[Au] Autor:Jurkovic DA; Hughes MR; Balish MF
[Ad] Endereço:Department of Microbiology, Miami University, Oxford, OH 45056, USA.
[Ti] Título:Analysis of energy sources for Mycoplasma penetrans gliding motility.
[So] Source:FEMS Microbiol Lett;338(1):39-45, 2013 Jan.
[Is] ISSN:1574-6968
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Mycoplasma penetrans, a potential human pathogen found mainly in HIV-infected individuals, uses a tip structure for both adherence and gliding motility. To improve our understanding of the molecular mechanism of M. penetrans gliding motility, we used chemical inhibitors of energy sources associated with motility of other organisms to determine which of these is used by M. penetrans and also tested whether gliding speed responded to temperature and pH. Mycoplasma penetrans gliding motility was not eliminated in the presence of a proton motive force inhibitor, a sodium motive force inhibitor, or an agent that depletes cellular ATP. At near-neutral pH, gliding speed increased as temperature increased. The absence of a clear chemical energy source for gliding motility and a positive correlation between speed and temperature suggest that energy derived from heat provides the major source of power for the gliding motor of M. penetrans.
[Mh] Termos MeSH primário: Metabolismo Energético
Temperatura Alta
Mycoplasma penetrans/fisiologia
[Mh] Termos MeSH secundário: Fenômenos Fisiológicos Bacterianos
Seres Humanos
Concentração de Íons de Hidrogênio
Microscopia de Fluorescência
Microscopia de Contraste de Fase
Mycoplasma penetrans/metabolismo
Temperatura Ambiente
Imagem com Lapso de Tempo
[Pt] Tipo de publicação:LETTER; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Em] Mês de entrada:1306
[Cu] Atualização por classe:161025
[Lr] Data última revisão:
161025
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:121017
[St] Status:MEDLINE
[do] DOI:10.1111/1574-6968.12026


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[PMID]:22782329
[Au] Autor:Jiang X; Lv YQ; Zhang JN; Shi YL; Xu FF
[Ad] Endereço:Department of Nephrology, Hangzhou Traditional Chinese Medical Hospital, Hangzhou, ZheJiang Province, PR China.
[Ti] Título:Mycoplasma penetrans infection is a potential cause of immunoglobulin A nephropathy: a new animal model.
[So] Source:J Nephrol;26(3):470-5, 2013 May-Jun.
[Is] ISSN:1724-6059
[Cp] País de publicação:Italy
[La] Idioma:eng
[Ab] Resumo:AIM: A new animal model of immunoglobulin A nephropathy (IgAN) was made by infecting mice with Mycoplasma penetrans (Mpe). To examine the pathogenesis of IgAN induced by Mpe infection, tumour necrosis factor-alpha (TNF-alpha), interleukin-6 (IL-6) and nuclear factor-kB (NF-kB) protein levels were compared among study groups. METHODS: To make an experimental IgAN animal model, mice were infected with Mpe, SP-4 medium or phosphate-buffered saline (PBS) via the urinary tract. To compare changes in the classical IgAN model, TNF-alpha and IL-6 RNA expression levels were measured using RT-PCR, and NF-kB protein was measured using EMSA. RESULTS: By producing a urinary tract infection with Mpe, we developed a new animal model of IgAN with a 100% success rate. There was no difference with the classical animal model. We also observed IgG deposition in 66.67% of the Mpe-infection group. Glomerular cell and mesangial matrix proliferation was greater in the Mpe-infection group than in the control groups (p<0.05). In the Mpe-infection and classical groups, TNF-alpha and IL-6 expression levels were much higher than in the control groups (p<0.01). NF-kB expression was much higher in the Mpe-infection group (p<0.05). CONCLUSIONS: We made a new IgAN animal model that will offer a new direction for IgAN research. The activation of inflammation factors was associated with the Mpe induction of IgAN.
[Mh] Termos MeSH primário: Modelos Animais de Doenças
Glomerulonefrite por IGA/microbiologia
Infecções por Mycoplasma/complicações
Mycoplasma penetrans
[Mh] Termos MeSH secundário: Animais
Feminino
Camundongos
Camundongos Endogâmicos BALB C
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Em] Mês de entrada:1311
[Cu] Atualização por classe:130517
[Lr] Data última revisão:
130517
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:120712
[St] Status:MEDLINE
[do] DOI:10.5301/jn.5000180


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[PMID]:23082227
[Au] Autor:Gallego P; Planell R; Benach J; Querol E; Perez-Pons JA; Reverter D
[Ad] Endereço:Institut de Biotecnologia i de Biomedicina and Departament de Bioquímica i de Biologia Molecular, Universitat Autònoma de Barcelona, Barcelona, Spain.
[Ti] Título:Structural characterization of the enzymes composing the arginine deiminase pathway in Mycoplasma penetrans.
[So] Source:PLoS One;7(10):e47886, 2012.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The metabolism of arginine towards ATP synthesis has been considered a major source of energy for microorganisms such as Mycoplasma penetrans in anaerobic conditions. Additionally, this pathway has also been implicated in pathogenic and virulence mechanism of certain microorganisms, i.e. protection from acidic stress during infection. In this work we present the crystal structures of the three enzymes composing the gene cluster of the arginine deiminase pathway from M. penetrans: arginine deiminase (ADI), ornithine carbamoyltransferase (OTC) and carbamate kinase (CK). The arginine deiminase (ADI) structure has been refined to 2.3 Å resolution in its apo-form, displaying an "open" conformation of the active site of the enzyme in comparison to previous complex structures with substrate intermediates. The active site pocket of ADI is empty, with some of the catalytic and binding residues far from their active positions, suggesting major conformational changes upon substrate binding. Ornithine carbamoyltransferase (OTC) has been refined in two crystal forms at 2.5 Å and 2.6 Å resolution, respectively, both displaying an identical dodecameric structure with a 23-point symmetry. The dodecameric structure of OTC represents the highest level of organization in this protein family and in M.penetrans it is constituted by a novel interface between the four catalytic homotrimers. Carbamate kinase (CK) has been refined to 2.5 Å resolution and its structure is characterized by the presence of two ion sulfates in the active site, one in the carbamoyl phosphate binding site and the other in the ß-phosphate ADP binding pocket of the enzyme. The CK structure also shows variations in some of the elements that regulate the catalytic activity of the enzyme. The relatively low number of metabolic pathways and the relevance in human pathogenesis of Mycoplasma penetrans places the arginine deiminase pathway enzymes as potential targets to design specific inhibitors against this human parasite.
[Mh] Termos MeSH primário: Hidrolases/química
Redes e Vias Metabólicas
Mycoplasma penetrans/enzimologia
Ornitina Carbamoiltransferase/química
Fosfotransferases (Aceptor do Grupo Carboxila)/química
[Mh] Termos MeSH secundário: Cristalografia por Raios X
Seres Humanos
Modelos Moleculares
Multimerização Proteica
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
EC 2.1.3.3 (Ornithine Carbamoyltransferase); EC 2.7.2.- (Phosphotransferases (Carboxyl Group Acceptor)); EC 2.7.2.2 (carbamate kinase); EC 3.- (Hydrolases); EC 3.5.3.6 (arginine deiminase)
[Em] Mês de entrada:1304
[Cu] Atualização por classe:150222
[Lr] Data última revisão:
150222
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:121020
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0047886


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[PMID]:22930310
[Au] Autor:Wang B; Wu JR; Guo HJ; Yang HT; Ai J; Hui M; Chan CY
[Ad] Endereço:School of Public Health, Southeast University, Nanjing, Jiangsu 210009, People's Republic of China. wangbeilxb@seu.edu.cn
[Ti] Título:The prevalence of six species of Mycoplasmataceae in an HIV/AIDS population in Jiangsu Province, China.
[So] Source:Int J STD AIDS;23(8):e7-10, 2012 Aug.
[Is] ISSN:1758-1052
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:This study employed culture and polymerase chain reaction (PCR) to examine the prevalence of Ureaplasma urealyticum, Mycoplasma hominis, Mycoplasma genitalium, Mycoplasma fermentans, Mycoplasma penetrans and Mycoplasma pirum in 210 HIV/AIDS patients, 455 sexually transmitted infection (STI) clinic attendees and 245 healthy volunteers from first-void urine specimens for men and endocervical swabs for women. U. urealyticum and M. hominis were detected in 107 (51.0%) and 69 (32.9%) patients in the HIV/AIDS group. At least one of the other four organisms was detected in 34 (16.2%) HIV/AIDS patients, 29 (6.4%) STI clinic attendees and six (2.5%) healthy volunteers. This study showed that U. urealyticum, M. hominis and M. fermentans were significantly more prevalent in HIV/AIDS patients, as were other mycoplasmas. Our results suggest a possible role for co-infection.
[Mh] Termos MeSH primário: Infecções Oportunistas Relacionadas com a AIDS/epidemiologia
Mycoplasmataceae
Infecções por Mycoplasmatales/epidemiologia
[Mh] Termos MeSH secundário: Adolescente
Adulto
Idoso
Criança
Pré-Escolar
China/epidemiologia
Feminino
Seres Humanos
Masculino
Meia-Idade
Mycoplasma
Infecções por Mycoplasma/epidemiologia
Infecções por Mycoplasma/microbiologia
Mycoplasma fermentans
Mycoplasma genitalium
Mycoplasma hominis
Mycoplasma penetrans
Infecções por Mycoplasmatales/microbiologia
Reação em Cadeia da Polimerase
Prevalência
Infecções por Ureaplasma/epidemiologia
Infecções por Ureaplasma/microbiologia
Ureaplasma urealyticum
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Em] Mês de entrada:1211
[Cu] Atualização por classe:120829
[Lr] Data última revisão:
120829
[Sb] Subgrupo de revista:IM; X
[Da] Data de entrada para processamento:120830
[St] Status:MEDLINE
[do] DOI:10.1258/ijsa.2009.009396


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[PMID]:22447904
[Au] Autor:Jurkovic DA; Newman JT; Balish MF
[Ad] Endereço:Department of Microbiology, Miami University, Oxford, OH, USA.
[Ti] Título:Conserved terminal organelle morphology and function in Mycoplasma penetrans and Mycoplasma iowae.
[So] Source:J Bacteriol;194(11):2877-83, 2012 Jun.
[Is] ISSN:1098-5530
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Within the genus Mycoplasma are species whose cells have terminal organelles, polarized structures associated with cytadherence and gliding motility. Mycoplasma penetrans, found mostly in HIV-infected patients, and Mycoplasma iowae, an economically significant poultry pathogen, are members of the Mycoplasma muris phylogenetic cluster. Both species have terminal organelles that interact with host cells, yet the structures in these species, or any in the M. muris cluster, remain uncharacterized. Time-lapse microcinematography of two strains of M. penetrans, GTU-54-6A1 and HF-2, and two serovars of M. iowae, K and N, show that the terminal organelles of both species play a role in gliding motility, with differences in speed within and between the two species. The strains and serovars also differed in their hemadsorption abilities that positively correlated with differences in motility speeds. No morphological differences were observed between M. penetrans and M. iowae by scanning electron microscopy (SEM). SEM and light microscopy of M. penetrans and M. iowae showed the presence of membranous filaments connecting pairs of dividing cells. Breaking of this filament during cell division was observed for M. penetrans by microcinematography, and this suggests a role for motility during division. The Triton X-100-insoluble fractions of M. penetrans and M. iowae consisted of similar structures that were unique compared to those identified in other mycoplasma species. Like other polarized mycoplasmas, M. penetrans and M. iowae have terminal organelles with cytadherence and gliding functions. The difference in function and morphology of the terminal organelles suggests that mycoplasmas have evolved terminal organelles independently of one another.
[Mh] Termos MeSH primário: Mycoplasma iowae/fisiologia
Mycoplasma penetrans/fisiologia
Organelas/fisiologia
[Mh] Termos MeSH secundário: Microscopia Eletrônica de Varredura
Mycoplasma iowae/citologia
Mycoplasma iowae/crescimento & desenvolvimento
Mycoplasma iowae/ultraestrutura
Mycoplasma penetrans/citologia
Mycoplasma penetrans/crescimento & desenvolvimento
Mycoplasma penetrans/ultraestrutura
Organelas/ultraestrutura
Imagem com Lapso de Tempo
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Em] Mês de entrada:1208
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:120327
[St] Status:MEDLINE
[do] DOI:10.1128/JB.00060-12



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