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Pesquisa : D08.811.913.696.445.035 [Categoria DeCS]
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[PMID]:28395125
[Au] Autor:Noel M; Gilormini PA; Cogez V; Yamakawa N; Vicogne D; Lion C; Biot C; Guérardel Y; Harduin-Lepers A
[Ad] Endereço:Université de Lille, CNRS, UMR 8576, UGSF, Unité de Glycobiologie Structurale et Fonctionnelle, 59000, Lille, France.
[Ti] Título:Probing the CMP-Sialic Acid Donor Specificity of Two Human ß-d-Galactoside Sialyltransferases (ST3Gal I and ST6Gal I) Selectively Acting on O- and N-Glycosylproteins.
[So] Source:Chembiochem;18(13):1251-1259, 2017 Jul 04.
[Is] ISSN:1439-7633
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Sialylation of glycoproteins and glycolipids is catalyzed by sialyltransferases in the Golgi of mammalian cells, whereby sialic acid residues are added at the nonreducing ends of oligosaccharides. Because sialylated glycans play critical roles in a number of human physio-pathological processes, the past two decades have witnessed the development of modified sialic acid derivatives for a better understanding of sialic acid biology and for the development of new therapeutic targets. However, nothing is known about how individual mammalian sialyltransferases tolerate and behave towards these unnatural CMP-sialic acid donors. In this study, we devised several approaches to investigate the donor specificity of the human ß-d-galactoside sialyltransferases ST6Gal I and ST3Gal I by using two CMP-sialic acids: CMP-Neu5Ac, and CMP-Neu5N-(4pentynoyl)neuraminic acid (CMP-SiaNAl), an unnatural CMP-sialic acid donor with an extended and functionalized N-acyl moiety.
[Mh] Termos MeSH primário: Antígenos CD/metabolismo
Ácido N-Acetilneuramínico Citidina Monofosfato/metabolismo
Citidina Monofosfato/análogos & derivados
Glicolipídeos/metabolismo
Glicoproteínas/metabolismo
Polissacarídeos/metabolismo
Ácidos Siálicos/metabolismo
Sialiltransferases/metabolismo
[Mh] Termos MeSH secundário: Antígenos CD/química
Antígenos CD/genética
Proteínas de Bactérias/química
Proteínas de Bactérias/metabolismo
Clonagem Molecular
Citidina Monofosfato/química
Citidina Monofosfato/metabolismo
Ácido N-Acetilneuramínico Citidina Monofosfato/química
Expressão Gênica
Glicolipídeos/química
Glicoproteínas/química
Glicoproteínas/genética
Glicosilação
Células HEK293
Seres Humanos
Cinética
N-Acilneuraminato Citidililtransferase/genética
N-Acilneuraminato Citidililtransferase/metabolismo
Neisseria meningitidis/química
Neisseria meningitidis/enzimologia
Polissacarídeos/química
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Ácidos Siálicos/química
Sialiltransferases/química
Sialiltransferases/genética
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antigens, CD); 0 (Bacterial Proteins); 0 (Glycolipids); 0 (Glycoproteins); 0 (Polysaccharides); 0 (Recombinant Proteins); 0 (Sialic Acids); 0 (cytidine-5'-monophosphosialic acid); 3063-71-6 (Cytidine Monophosphate N-Acetylneuraminic Acid); EC 2.4.99.- (Sialyltransferases); EC 2.4.99.1 (ST6GAL1 protein, human); EC 2.4.99.4 (beta-galactoside alpha-2,3-sialyltransferase); EC 2.7.7.43 (N-Acylneuraminate Cytidylyltransferase); F469818O25 (Cytidine Monophosphate)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170723
[Lr] Data última revisão:
170723
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170411
[St] Status:MEDLINE
[do] DOI:10.1002/cbic.201700024


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[PMID]:28374933
[Au] Autor:Abeln M; Borst KM; Cajic S; Thiesler H; Kats E; Albers I; Kuhn M; Kaever V; Rapp E; Münster-Kühnel A; Weinhold B
[Ad] Endereço:Institute of Clinical Biochemistry, Hannover Medical School, Carl-Neuberg-Strasse 1, 30625, Hannover, Germany.
[Ti] Título:Sialylation Is Dispensable for Early Murine Embryonic Development in Vitro.
[So] Source:Chembiochem;18(13):1305-1316, 2017 Jul 04.
[Is] ISSN:1439-7633
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:The negatively charged nonulose sialic acid (Sia) is essential for murine development in vivo. In order to elucidate the impact of sialylation on differentiation processes in the absence of maternal influences, we generated mouse embryonic stem cell (mESC) lines that lack CMP-Sia synthetase (CMAS) and thereby the ability to activate Sia to CMP-Sia. Loss of CMAS activity resulted in an asialo cell surface accompanied by an increase in glycoconjugates with terminal galactosyl and oligo-LacNAc residues, as well as intracellular accumulation of free Sia. Remarkably, these changes did not impact intracellular metabolites or the morphology and transcriptome of pluripotent mESC lines. Moreover, the capacity of Cmas mESCs for undirected differentiation into embryoid bodies, germ layer formation and even the generation of beating cardiomyocytes provides first and conclusive evidence that pluripotency and differentiation of mESC in vitro can proceed in the absence of (poly)sialoglycans.
[Mh] Termos MeSH primário: Camadas Germinativas/metabolismo
Células-Tronco Embrionárias Murinas/metabolismo
Miócitos Cardíacos/metabolismo
N-Acilneuraminato Citidililtransferase/deficiência
Células-Tronco Pluripotentes/metabolismo
Ácidos Siálicos/metabolismo
[Mh] Termos MeSH secundário: Amino Açúcares/metabolismo
Animais
Diferenciação Celular
Linhagem Celular
Embrião de Mamíferos
Corpos Embrioides/citologia
Corpos Embrioides/metabolismo
Efeito Fundador
Galactose/metabolismo
Expressão Gênica
Camadas Germinativas/citologia
Glicoconjugados/metabolismo
Células HEK293
Seres Humanos
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Transgênicos
Células-Tronco Embrionárias Murinas/citologia
Miócitos Cardíacos/citologia
N-Acilneuraminato Citidililtransferase/genética
Células-Tronco Pluripotentes/citologia
Transcriptoma
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amino Sugars); 0 (Glycoconjugates); 0 (Sialic Acids); 3Y5B2K5OOK (N-acetyllactosamine); EC 2.7.7.43 (N-Acylneuraminate Cytidylyltransferase); X2RN3Q8DNE (Galactose)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170725
[Lr] Data última revisão:
170725
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170405
[St] Status:MEDLINE
[do] DOI:10.1002/cbic.201700083


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[PMID]:27380425
[Au] Autor:Kohnz RA; Roberts LS; DeTomaso D; Bideyan L; Yan P; Bandyopadhyay S; Goga A; Yosef N; Nomura DK
[Ad] Endereço:Departments of Chemistry, Molecular and Cell Biology, and Nutritional Sciences and Toxicology, University of California, Berkeley , Berkeley, California 94720, United States.
[Ti] Título:Protein Sialylation Regulates a Gene Expression Signature that Promotes Breast Cancer Cell Pathogenicity.
[So] Source:ACS Chem Biol;11(8):2131-9, 2016 Aug 19.
[Is] ISSN:1554-8937
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Many mechanisms have been proposed for how heightened aerobic glycolytic metabolism fuels cancer pathogenicity, but there are still many unexplored pathways. Here, we have performed metabolomic profiling to map glucose incorporation into metabolic pathways upon transformation of mammary epithelial cells by 11 commonly mutated human oncogenes. We show that transformation of mammary epithelial cells by oncogenic stimuli commonly shunts glucose-derived carbons into synthesis of sialic acid, a hexosamine pathway metabolite that is converted to CMP-sialic acid by cytidine monophosphate N-acetylneuraminic acid synthase (CMAS) as a precursor to glycoprotein and glycolipid sialylation. We show that CMAS knockdown leads to elevations in intracellular sialic acid levels, a depletion of cellular sialylation, and alterations in the expression of many cancer-relevant genes to impair breast cancer pathogenicity. Our study reveals the heretofore unrecognized role of sialic acid metabolism and protein sialylation in regulating the expression of genes that maintain breast cancer pathogenicity.
[Mh] Termos MeSH primário: Neoplasias da Mama/metabolismo
Regulação Neoplásica da Expressão Gênica
Ácido N-Acetilneuramínico/metabolismo
Proteínas de Neoplasias/metabolismo
[Mh] Termos MeSH secundário: Animais
Neoplasias da Mama/enzimologia
Neoplasias da Mama/patologia
Linhagem Celular Tumoral
Feminino
Técnicas de Silenciamento de Genes
Xenoenxertos
Seres Humanos
Metabolômica
Camundongos SCID
N-Acilneuraminato Citidililtransferase/genética
N-Acilneuraminato Citidililtransferase/metabolismo
Transcriptoma
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Neoplasm Proteins); EC 2.7.7.43 (N-Acylneuraminate Cytidylyltransferase); GZP2782OP0 (N-Acetylneuraminic Acid)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170619
[Lr] Data última revisão:
170619
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160706
[St] Status:MEDLINE
[do] DOI:10.1021/acschembio.6b00433


  4 / 143 MEDLINE  
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[PMID]:27357083
[Au] Autor:Ma Y; Tian S; Wang Z; Wang C; Chen X; Li W; Yang Y; He S
[Ad] Endereço:Department of Biochemistry & Biology, University of South China, Hengyang, Hunan 421001, P.R. China.
[Ti] Título:CMP­N­acetylneuraminic acid synthetase interacts with fragile X related protein 1.
[So] Source:Mol Med Rep;14(2):1501-8, 2016 Aug.
[Is] ISSN:1791-3004
[Cp] País de publicação:Greece
[La] Idioma:eng
[Ab] Resumo:Fragile X mental retardation protein (FMRP), fragile X related 1 protein (FXR1P) and FXR2P are the members of the FMR protein family. These proteins contain two KH domains and a RGG box, which are characteristic of RNA binding proteins. The absence of FMRP, causes fragile X syndrome (FXS), the leading cause of hereditary mental retardation. FXR1P is expressed throughout the body and important for normal muscle development, and its absence causes cardiac abnormality. To investigate the functions of FXR1P, a screen was performed to identify FXR1P­interacting proteins and determine the biological effect of the interaction. The current study identified CMP­N­acetylneuraminic acid synthetase (CMAS) as an interacting protein using the yeast two­hybrid system, and the interaction between FXR1P and CMAS was validated in yeast using a ß­galactosidase assay and growth studies with selective media. Furthermore, co­immunoprecipitation was used to analyze the FXR1P/CMAS association and immunofluorescence microscopy was performed to detect expression and intracellular localization of the proteins. The results of the current study indicated that FXR1P and CMAS interact, and colocalize in the cytoplasm and the nucleus of HEK293T and HeLa cells. Accordingly, a fragile X related 1 (FXR1) gene overexpression vector was constructed to investigate the effect of FXR1 overexpression on the level of monosialotetrahexosylganglioside 1 (GM1). The results of the current study suggested that FXR1P is a tissue­specific regulator of GM1 levels in SH­SY5Y cells, but not in HEK293T cells. Taken together, the results initially indicate that FXR1P interacts with CMAS, and that FXR1P may enhance the activation of sialic acid via interaction with CMAS, and increase GM1 levels to affect the development of the nervous system, thus providing evidence for further research into the pathogenesis of FXS.
[Mh] Termos MeSH primário: Proteína do X Frágil de Retardo Mental/metabolismo
Síndrome do Cromossomo X Frágil/metabolismo
N-Acilneuraminato Citidililtransferase/metabolismo
[Mh] Termos MeSH secundário: Proteína do X Frágil de Retardo Mental/química
Proteína do X Frágil de Retardo Mental/genética
Síndrome do Cromossomo X Frágil/genética
Expressão Gênica
Células HEK293
Células HeLa
Seres Humanos
Imunoprecipitação
Oligossacarídeos/metabolismo
Ligação Proteica
Domínios e Motivos de Interação entre Proteínas
Mapeamento de Interação de Proteínas
Transporte Proteico
Técnicas do Sistema de Duplo-Híbrido
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (FMR1 protein, human); 0 (GM1 pentasaccharide); 0 (Oligosaccharides); 139135-51-6 (Fragile X Mental Retardation Protein); EC 2.7.7.43 (N-Acylneuraminate Cytidylyltransferase)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170406
[Lr] Data última revisão:
170406
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160701
[St] Status:MEDLINE
[do] DOI:10.3892/mmr.2016.5438


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[PMID]:27114558
[Au] Autor:Mertsalov IB; Novikov BN; Scott H; Dangott L; Panin VM
[Ad] Endereço:Department of Biochemistry and Biophysics, Texas A&M University, College Station, TX 77843, U.S.A.
[Ti] Título:Characterization of Drosophila CMP-sialic acid synthetase activity reveals unusual enzymatic properties.
[So] Source:Biochem J;473(13):1905-16, 2016 Jul 01.
[Is] ISSN:1470-8728
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:CMP-sialic acid synthetase (CSAS) is a key enzyme of the sialylation pathway. CSAS produces the activated sugar donor, CMP-sialic acid, which serves as a substrate for sialyltransferases to modify glycan termini with sialic acid. Unlike other animal CSASs that normally localize in the nucleus, Drosophila melanogaster CSAS (DmCSAS) localizes in the cell secretory compartment, predominantly in the Golgi, which suggests that this enzyme has properties distinct from those of its vertebrate counterparts. To test this hypothesis, we purified recombinant DmCSAS and characterized its activity in vitro Our experiments revealed several unique features of this enzyme. DmCSAS displays specificity for N-acetylneuraminic acid as a substrate, shows preference for lower pH and can function with a broad range of metal cofactors. When tested at a pH corresponding to the Golgi compartment, the enzyme showed significant activity with several metal cations, including Zn(2+), Fe(2+), Co(2+) and Mn(2+), whereas the activity with Mg(2+) was found to be low. Protein sequence analysis and site-specific mutagenesis identified an aspartic acid residue that is necessary for enzymatic activity and predicted to be involved in co-ordinating a metal cofactor. DmCSAS enzymatic activity was found to be essential in vivo for rescuing the phenotype of DmCSAS mutants. Finally, our experiments revealed a steep dependence of the enzymatic activity on temperature. Taken together, our results indicate that DmCSAS underwent evolutionary adaptation to pH and ionic environment different from that of counterpart synthetases in vertebrates. Our data also suggest that environmental temperatures can regulate Drosophila sialylation, thus modulating neural transmission.
[Mh] Termos MeSH primário: Proteínas de Drosophila/química
Proteínas de Drosophila/metabolismo
N-Acilneuraminato Citidililtransferase/química
N-Acilneuraminato Citidililtransferase/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Ácido Aspártico/química
Ácido Aspártico/metabolismo
Células Cultivadas
Drosophila
Proteínas de Drosophila/classificação
Proteínas de Drosophila/genética
Seres Humanos
Concentração de Íons de Hidrogênio
Cinética
Magnésio/metabolismo
Manganês/metabolismo
Mutação
N-Acilneuraminato Citidililtransferase/classificação
N-Acilneuraminato Citidililtransferase/genética
Filogenia
Relação Estrutura-Atividade
Especificidade por Substrato
Temperatura Ambiente
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Drosophila Proteins); 30KYC7MIAI (Aspartic Acid); 42Z2K6ZL8P (Manganese); EC 2.7.7.43 (N-Acylneuraminate Cytidylyltransferase); I38ZP9992A (Magnesium)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170515
[Lr] Data última revisão:
170515
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160427
[St] Status:MEDLINE
[do] DOI:10.1042/BCJ20160347


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[PMID]:26023910
[Au] Autor:Li L; Liu Y; Li T; Wang W; Yu Z; Ma C; Qu J; Zhao W; Chen X; Wang PG
[Ad] Endereço:Department of Chemistry and Center for Diagnostics & Therapeutics, Georgia State University, Atlanta, GA 30303, USA. lli22@gsu.edu pwang11@gsu.edu.
[Ti] Título:Efficient chemoenzymatic synthesis of novel galacto-N-biose derivatives and their sialylated forms.
[So] Source:Chem Commun (Camb);51(51):10310-3, 2015 Jun 28.
[Is] ISSN:1364-548X
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Galacto-N-biose (GNB) derivatives were efficiently synthesized from galactose derivatives via a one-pot two-enzyme system containing two promiscuous enzymes from Bifidobacterium infantis: a galactokinase (BiGalK) and a d-galactosyl-ß1-3-N-acetyl-d-hexosamine phosphorylase (BiGalHexNAcP). Mono-sialyl and di-sialyl galacto-N-biose derivatives were then prepared using a one-pot two-enzyme system containing a CMP-sialic acid synthetase and an α2-3-sialyltransferase or an α2-6-sialyltransferase.
[Mh] Termos MeSH primário: Dissacarídeos/síntese química
Galactanos/síntese química
Ácidos Siálicos/síntese química
[Mh] Termos MeSH secundário: Bifidobacterium/enzimologia
Galactoquinase/química
Galactoquinase/metabolismo
Galactosiltransferases/química
Galactosiltransferases/metabolismo
N-Acilneuraminato Citidililtransferase/química
N-Acilneuraminato Citidililtransferase/metabolismo
Sialiltransferases/química
Sialiltransferases/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Disaccharides); 0 (Galactans); 0 (Sialic Acids); EC 2.4.1.- (Galactosyltransferases); EC 2.4.1.- (beta-1,3-galactosyl-N-acetylhexosamine phosphorylase); EC 2.4.99.- (Sialyltransferases); EC 2.4.99.1 (beta-D-galactoside alpha 2-6-sialyltransferase); EC 2.4.99.4 (beta-galactoside alpha-2,3-sialyltransferase); EC 2.7.1.6 (Galactokinase); EC 2.7.7.43 (N-Acylneuraminate Cytidylyltransferase)
[Em] Mês de entrada:1602
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150530
[St] Status:MEDLINE
[do] DOI:10.1039/c5cc03746h


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[PMID]:24141690
[Au] Autor:Sellmeier M; Weinhold B; Münster-Kühnel A
[Ad] Endereço:Institute for Cellular Chemistry, Hannover Medical School (MHH), Hannover, 30625, Germany.
[Ti] Título:CMP-Sialic Acid Synthetase: The Point of Constriction in the Sialylation Pathway.
[So] Source:Top Curr Chem;366:139-67, 2015.
[Is] ISSN:0340-1022
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Sialoglycoconjugates form the outermost layer of animal cells and play a crucial role in cellular communication processes. An essential step in the biosynthesis of sialylated glycoconjugates is the activation of sialic acid to the monophosphate diester CMP-sialic acid. Only the activated sugar is transported into the Golgi apparatus and serves as a substrate for the linkage-specific sialyltransferases. Interference with sugar activation abolishes sialylation and is embryonic lethal in mammals. In this chapter we focus on the enzyme catalyzing the activation of sialic acid, the CMP-sialic acid synthetase (CMAS), and compare the enzymatic properties of CMASs isolated from different species. Information concerning the reaction mechanism and active site architecture is included. Moreover, the unusual nuclear localization of vertebrate CMASs as well as the biotechnological application of bacterial CMAS enzymes is addressed.
[Mh] Termos MeSH primário: Bactérias/enzimologia
Ácido N-Acetilneuramínico Citidina Monofosfato/metabolismo
Células Eucarióticas/enzimologia
Glicoconjugados/metabolismo
N-Acilneuraminato Citidililtransferase/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Bactérias/química
Transporte Biológico
Domínio Catalítico
Comunicação Celular
Ácido N-Acetilneuramínico Citidina Monofosfato/química
Células Eucarióticas/química
Glicoconjugados/química
Complexo de Golgi/química
Complexo de Golgi/metabolismo
Cinética
Modelos Moleculares
Dados de Sequência Molecular
N-Acilneuraminato Citidililtransferase/química
Homologia de Sequência de Aminoácidos
Especificidade da Espécie
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; REVIEW
[Nm] Nome de substância:
0 (Glycoconjugates); 3063-71-6 (Cytidine Monophosphate N-Acetylneuraminic Acid); EC 2.7.7.43 (N-Acylneuraminate Cytidylyltransferase)
[Em] Mês de entrada:1511
[Cu] Atualização por classe:150729
[Lr] Data última revisão:
150729
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:131022
[St] Status:MEDLINE
[do] DOI:10.1007/128_2013_477


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[PMID]:24245827
[Au] Autor:Mentasti M; Underwood A; Lück C; Kozak-Muiznieks NA; Harrison TG; Fry NK
[Ad] Endereço:Respiratory and Vaccine Preventable Bacteria Reference Unit, London, UK.
[Ti] Título:Extension of the Legionella pneumophila sequence-based typing scheme to include strains carrying a variant of the N-acylneuraminate cytidylyltransferase gene.
[So] Source:Clin Microbiol Infect;20(7):O435-41, 2014 Jul.
[Is] ISSN:1469-0691
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Sequence-based typing (SBT) combined with monoclonal antibody subgrouping of Legionella pneumophila isolates is at present considered to be the reference standard during epidemiological investigation of Legionnaires' disease outbreaks. In some isolates of L. pneumophila, the seventh allele of the standard SBT scheme, neuA, is not amplified, because a homologue that is refractory to amplification with the standard neuA primers is present. Consequently, a complete seven-allele profile, and hence a sequence type, cannot be obtained. Subsequently, primers were designed to amplify both neuA and the homologue, but these yielded suboptimal sequencing results. In this study, novel primers specific for the neuA homologue were designed and internationally validated by members of the ESCMID Study Group for Legionella Infections at national and regional Legionella reference laboratories with a modified version of the online L. pneumophila sequence quality tool. To date, the addition of the neuAh target to the SBT protocol has allowed full typing data to be obtained for 108 isolates of 11 different serogroups, namely 1, 2, 3, 4, 5, 6, 7, 8, 10, 13, and 14, which could not previously be typed with the standard SBT neuA primers. Further studies are necessary to determine why it is still not possible to obtain either a neuA or a neuAh allele from three serogroup 11 isolates.
[Mh] Termos MeSH primário: Legionella pneumophila/classificação
Legionella pneumophila/genética
Tipagem Molecular/métodos
N-Acilneuraminato Citidililtransferase/genética
[Mh] Termos MeSH secundário: DNA Bacteriano/química
DNA Bacteriano/genética
Surtos de Doenças
Seres Humanos
Legionella pneumophila/enzimologia
Doença dos Legionários/epidemiologia
Doença dos Legionários/microbiologia
Epidemiologia Molecular/métodos
Dados de Sequência Molecular
Análise de Sequência de DNA
[Pt] Tipo de publicação:JOURNAL ARTICLE; VALIDATION STUDIES
[Nm] Nome de substância:
0 (DNA, Bacterial); EC 2.7.7.43 (N-Acylneuraminate Cytidylyltransferase)
[Em] Mês de entrada:1503
[Cu] Atualização por classe:140728
[Lr] Data última revisão:
140728
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:131120
[St] Status:MEDLINE
[do] DOI:10.1111/1469-0691.12459


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[PMID]:23884937
[Au] Autor:Islam R; Nakamura M; Scott H; Repnikova E; Carnahan M; Pandey D; Caster C; Khan S; Zimmermann T; Zoran MJ; Panin VM
[Ad] Endereço:Department of Biochemistry and Biophysics and Department of Biology, Texas A&M University, College Station, Texas 77843, USA.
[Ti] Título:The role of Drosophila cytidine monophosphate-sialic acid synthetase in the nervous system.
[So] Source:J Neurosci;33(30):12306-15, 2013 Jul 24.
[Is] ISSN:1529-2401
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:While sialylation plays important functions in the nervous system, the complexity of glycosylation pathways and limitations of genetic approaches preclude the efficient analysis of these functions in mammalian organisms. Drosophila has recently emerged as a promising model for studying neural sialylation. Drosophila sialyltransferase, DSiaT, was shown to be involved in the regulation of neural transmission. However, the sialylation pathway was not investigated in Drosophila beyond the DSiaT-mediated step. Here we focused on the function of Drosophila cytidine monophosphate-sialic acid synthetase (CSAS), the enzyme providing a sugar donor for DSiaT. Our results revealed that the expression of CSAS is tightly regulated and restricted to the CNS throughout development and in adult flies. We generated CSAS mutants and analyzed their phenotypes using behavioral and physiological approaches. Our experiments demonstrated that mutant phenotypes of CSAS are similar to those of DSiaT, including decreased longevity, temperature-induced paralysis, locomotor abnormalities, and defects of neural transmission at neuromuscular junctions. Genetic interactions between CSAS, DSiaT, and voltage-gated channel genes paralytic and seizure were consistent with the hypothesis that CSAS and DSiaT function within the same pathway regulating neural excitability. Intriguingly, these interactions also suggested that CSAS and DSiaT have some additional, independent functions. Moreover, unlike its mammalian counterparts that work in the nucleus, Drosophila CSAS was found to be a glycoprotein-bearing N-glycans and predominantly localized in vivo to the Golgi compartment. Our work provides the first systematic analysis of in vivo functions of a eukaryotic CSAS gene and sheds light on evolutionary relationships among metazoan CSAS proteins.
[Mh] Termos MeSH primário: Citidina Monofosfato/metabolismo
Proteínas de Drosophila/genética
Drosophila/enzimologia
Ligases/genética
Ácido N-Acetilneuramínico/metabolismo
N-Acilneuraminato Citidililtransferase/genética
Fenômenos Fisiológicos do Sistema Nervoso/genética
[Mh] Termos MeSH secundário: Animais
Animais Geneticamente Modificados
Drosophila/genética
Proteínas de Drosophila/metabolismo
Evolução Molecular
Regulação da Expressão Gênica no Desenvolvimento/fisiologia
Ligases/metabolismo
Longevidade/genética
N-Acilneuraminato Citidililtransferase/metabolismo
Junção Neuromuscular/genética
Junção Neuromuscular/metabolismo
Paralisia/genética
Paralisia/metabolismo
Vesículas Secretórias/fisiologia
Sialiltransferases/genética
Sialiltransferases/metabolismo
Transmissão Sináptica/genética
Transmissão Sináptica/fisiologia
Temperatura Ambiente
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Drosophila Proteins); EC 2.4.99.- (Sialyltransferases); EC 2.7.7.43 (N-Acylneuraminate Cytidylyltransferase); EC 6.- (Ligases); F469818O25 (Cytidine Monophosphate); GZP2782OP0 (N-Acetylneuraminic Acid)
[Em] Mês de entrada:1310
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130726
[St] Status:MEDLINE
[do] DOI:10.1523/JNEUROSCI.5220-12.2013


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[PMID]:23266097
[Au] Autor:Martínez-Martínez S; Frandoloso R; Rodríguez Ferri EF; Gil C; Hernández-Haro C; Yubero S; Gutiérrez Martín CB
[Ad] Endereço:Unidad de Microbiología e Inmunología, Departamento de Sanidad Animal, Universidad de León, Spain.
[Ti] Título:Immunoproteomic analysis of the protective response obtained with subunit and commercial vaccines against Glässer's disease in pigs.
[So] Source:Vet Immunol Immunopathol;151(3-4):235-47, 2013 Feb 15.
[Is] ISSN:1873-2534
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:An immunoproteomic analysis of the protective response of subunit and commercial vaccines in colostrum-deprived pigs against Glässer's disease was carried out. A mixture of proteins with affinity to porcine transferrin (PAPT) from Haemophilus parasuis Nagasaki strain (serovar 5) was inoculated intramuscularly (PAPT(M)) and intratracheally (PAPT(Cp)), along with a commercial bacterin. PAPT were separated using 2 dimensional electrophoresis (2DE) gels and with them, 2DE Western blots were carried out. A total of 17 spots were identified as positive with sera of pigs from any of the three vaccinated groups, the highest number of immunoreactive proteins being detected in those having received PAPT(Cp). Among them, six proteins (FKBP-type peptidyl-prolyl cis-trans isomerase, neuraminidase exo-α-sialidase, xanthine-guanine phosphoribosyl transferase, CMP-N-acetylneuraminic acid synthetase, phenylalanyl-tRNA synthetase and glyceraldehyde 3-phosphate dehydrogenase) were found to be novel immunogens in H. parasuis. These proteins showed a high potential as candidates in future subunit vaccines against Glässer's disease. The three experimental groups developed specific systemic total IgG (IgGt), IgG1, IgG2 and IgM antibodies after immunizations. In addition, those receiving PAPT(Cp) yielded a serum IgA response.
[Mh] Termos MeSH primário: Proteínas de Bactérias/imunologia
Infecções por Haemophilus/veterinária
Vacinas Anti-Haemophilus/imunologia
Haemophilus parasuis
Doenças dos Suínos/imunologia
Doenças dos Suínos/prevenção & controle
[Mh] Termos MeSH secundário: Animais
Anticorpos Antibacterianos/biossíntese
Antígenos de Bactérias/imunologia
Antígenos de Bactérias/isolamento & purificação
Proteínas de Bactérias/isolamento & purificação
Vacinas Bacterianas/imunologia
Gliceraldeído-3-Fosfato Desidrogenases/imunologia
Infecções por Haemophilus/imunologia
Infecções por Haemophilus/prevenção & controle
Haemophilus parasuis/classificação
Haemophilus parasuis/imunologia
N-Acilneuraminato Citidililtransferase/imunologia
Neuraminidase/imunologia
Pentosiltransferases/imunologia
Peptidilprolil Isomerase/imunologia
Fenilalanina-tRNA Ligase/imunologia
Proteômica
Sus scrofa
Suínos
Transferrina/imunologia
Vacinas de Subunidades/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antibodies, Bacterial); 0 (Antigens, Bacterial); 0 (Bacterial Proteins); 0 (Bacterial Vaccines); 0 (Haemophilus Vaccines); 0 (Transferrin); 0 (Vaccines, Subunit); EC 1.2.1.- (Glyceraldehyde-3-Phosphate Dehydrogenases); EC 2.4.2.- (Pentosyltransferases); EC 2.4.2.22 (xanthine phosphoribosyltransferase); EC 2.7.7.43 (N-Acylneuraminate Cytidylyltransferase); EC 3.2.1.18 (Neuraminidase); EC 5.2.1.8 (Peptidylprolyl Isomerase); EC 6.1.1.20 (Phenylalanine-tRNA Ligase)
[Em] Mês de entrada:1309
[Cu] Atualização por classe:130128
[Lr] Data última revisão:
130128
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:121226
[St] Status:MEDLINE



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