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  1 / 1084 MEDLINE  
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[PMID]:29191651
[Au] Autor:Fang Y; Xiao X; Li SX; Wolfe A; Chen XS
[Ad] Endereço:Molecular and Computational Biology, Departments of Biological Sciences and Chemistry, University of Southern California, Los Angeles, CA 90089, USA; 161 Hospital of PLA, Wuhan, 430012, China; Department of Clinical Microbiology and Immunology of Southwest Hospital, Third Military Medical University
[Ti] Título:Molecular Interactions of a DNA Modifying Enzyme APOBEC3F Catalytic Domain with a Single-Stranded DNA.
[So] Source:J Mol Biol;430(1):87-101, 2018 Jan 05.
[Is] ISSN:1089-8638
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The single-stranded DNA (ssDNA) cytidine deaminase APOBEC3F (A3F) deaminates cytosine (C) to uracil (U) and is a known restriction factor of HIV-1. Its C-terminal catalytic domain (CD2) alone is capable of binding single-stranded nucleic acids and is important for deamination. However, little is known about how the CD2 interacts with ssDNA. Here we report a crystal structure of A3F-CD2 in complex with a 10-nucleotide ssDNA composed of poly-thymine, which reveals a novel positively charged nucleic acid binding site distal to the active center that plays a key role in substrate DNA binding and catalytic activity. Lysine and tyrosine residues within this binding site interact with the ssDNA, and mutating these residues dramatically impairs both ssDNA binding and catalytic activity. This binding site is not conserved in APOBEC3G (A3G), which may explain differences in ssDNA-binding characteristics between A3F-CD2 and A3G-CD2. In addition, we observed an alternative Zn-coordination conformation around the active center. These findings reveal the structural relationships between nucleic acid interactions and catalytic activity of A3F.
[Mh] Termos MeSH primário: Citidina Desaminase/metabolismo
DNA de Cadeia Simples/metabolismo
[Mh] Termos MeSH secundário: Desaminase APOBEC-3G/metabolismo
Sequência de Aminoácidos
Sítios de Ligação/fisiologia
Domínio Catalítico/fisiologia
Citosina Desaminase/metabolismo
Desaminação/fisiologia
Escherichia coli/metabolismo
HIV-1/metabolismo
Seres Humanos
Ligação Proteica/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA, Single-Stranded); EC 3.5.4.1 (Cytosine Deaminase); EC 3.5.4.5 (APOBEC-3G Deaminase); EC 3.5.4.5 (Cytidine Deaminase)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171227
[Lr] Data última revisão:
171227
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171202
[St] Status:MEDLINE


  2 / 1084 MEDLINE  
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[PMID]:28748410
[Au] Autor:Komissarov A; Demidyuk I; Safina D; Roschina M; Shubin A; Lunina N; Karaseva M; Kostrov S
[Ad] Endereço:Laboratory of Protein Engineering, Institute of Molecular Genetics, Russian Academy of Science, 2 Kurchatova Sq., Moscow, Russia, 123182.
[Ti] Título:Cytotoxic effect of co-expression of human hepatitis A virus 3C protease and bifunctional suicide protein FCU1 genes in a bicistronic vector.
[So] Source:Mol Biol Rep;44(4):323-332, 2017 Aug.
[Is] ISSN:1573-4978
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Recent reports on various cancer models demonstrate a great potential of cytosine deaminase/5-fluorocytosine suicide system in cancer therapy. However, this approach has limited success and its application to patients has not reached the desirable clinical significance. Accordingly, the improvement of this suicide system is an actively developing trend in gene therapy. The purpose of this study was to explore the cytotoxic effect observed after co-expression of hepatitis A virus 3C protease (3C) and yeast cytosine deaminase/uracil phosphoribosyltransferase fusion protein (FCU1) in a bicistronic vector. A set of mono- and bicistronic plasmid constructs was generated to provide individual or combined expression of 3C and FCU1. The constructs were introduced into HEK293 and HeLa cells, and target protein synthesis as well as the effect of 5-fluorocytosine on cell death and the time course of the cytotoxic effect was studied. The obtained vectors provide for the synthesis of target proteins in human cells. The expression of the genes in a bicistronic construct provide for the cytotoxic effect comparable to that observed after the expression of genes in monocistronic constructs. At the same time, co-expression of FCU1 and 3C recapitulated their cytotoxic effects. The combined effect of the killer and suicide genes was studied for the first time on human cells in vitro. The integration of different gene therapy systems inducing cell death (FCU1 and 3C genes) in a bicistronic construct allowed us to demonstrate that it does not interfere with the cytotoxic effect of each of them. A combination of cytotoxic genes in multicistronic vectors can be used to develop pluripotent gene therapy agents.
[Mh] Termos MeSH primário: Cisteína Endopeptidases/biossíntese
Citosina Desaminase/biossíntese
Flucitosina/farmacologia
Terapia Genética/métodos
Vírus da Hepatite A Humana/enzimologia
Pentosiltransferases/biossíntese
Proteínas Virais/biossíntese
[Mh] Termos MeSH secundário: Cisteína Endopeptidases/genética
Cisteína Endopeptidases/metabolismo
Citosina Desaminase/genética
Citosina Desaminase/metabolismo
Flucitosina/farmacocinética
Genes Transgênicos Suicidas
Vetores Genéticos
Células HEK293
Células HeLa
Vírus da Hepatite A Humana/metabolismo
Seres Humanos
Pentosiltransferases/genética
Pentosiltransferases/metabolismo
Plasmídeos/genética
Pró-Fármacos/farmacocinética
Pró-Fármacos/farmacologia
Transdução Genética
Proteínas Virais/genética
Proteínas Virais/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Prodrugs); 0 (Viral Proteins); D83282DT06 (Flucytosine); EC 2.4.2.- (Pentosyltransferases); EC 2.4.2.9 (uracil phosphoribosyltransferase); EC 3.4.22.- (Cysteine Endopeptidases); EC 3.4.22.28 (3C proteases); EC 3.5.4.1 (Cytosine Deaminase)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171227
[Lr] Data última revisão:
171227
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170728
[St] Status:MEDLINE
[do] DOI:10.1007/s11033-017-4113-4


  3 / 1084 MEDLINE  
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[PMID]:28753428
[Au] Autor:Supek F; Lehner B
[Ad] Endereço:EMBL-CRG Systems Biology Unit, Centre for Genomic Regulation (CRG), the Barcelona Institute of Science and Technology, 08003 Barcelona, Spain; Universitat Pompeu Fabra (UPF), 08003 Barcelona, Spain; Division of Electronics, Rudjer Boskovic Institute, 10000 Zagreb, Croatia.
[Ti] Título:Clustered Mutation Signatures Reveal that Error-Prone DNA Repair Targets Mutations to Active Genes.
[So] Source:Cell;170(3):534-547.e23, 2017 Jul 27.
[Is] ISSN:1097-4172
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Many processes can cause the same nucleotide change in a genome, making the identification of the mechanisms causing mutations a difficult challenge. Here, we show that clustered mutations provide a more precise fingerprint of mutagenic processes. Of nine clustered mutation signatures identified from >1,000 tumor genomes, three relate to variable APOBEC activity and three are associated with tobacco smoking. An additional signature matches the spectrum of translesion DNA polymerase eta (POLH). In lymphoid cells, these mutations target promoters, consistent with AID-initiated somatic hypermutation. In solid tumors, however, they are associated with UV exposure and alcohol consumption and target the H3K36me3 chromatin of active genes in a mismatch repair (MMR)-dependent manner. These regions normally have a low mutation rate because error-free MMR also targets H3K36me3 chromatin. Carcinogens and error-prone repair therefore redistribute mutations to the more important regions of the genome, contributing a substantial mutation load in many tumors, including driver mutations.
[Mh] Termos MeSH primário: Reparo de Erro de Pareamento de DNA
Mutação
Neoplasias/genética
[Mh] Termos MeSH secundário: Citosina Desaminase/genética
DNA Polimerase Dirigida por DNA/genética
Seres Humanos
Neoplasias Hepáticas/induzido quimicamente
Neoplasias Hepáticas/genética
Melanoma/genética
Mutagênese
Fumar/efeitos adversos
Raios Ultravioleta/efeitos adversos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 2.7.7.7 (DNA-Directed DNA Polymerase); EC 2.7.7.7 (Rad30 protein); EC 3.5.4.1 (APOBEC3 protein, human); EC 3.5.4.1 (Cytosine Deaminase)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170808
[Lr] Data última revisão:
170808
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170729
[St] Status:MEDLINE


  4 / 1084 MEDLINE  
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[PMID]:28641402
[Au] Autor:Hida N; Aboukilila MY; Burow DA; Paul R; Greenberg MM; Fazio M; Beasley S; Spitale RC; Cleary MD
[Ad] Endereço:Molecular and Cell Biology Unit, Quantitative and Systems Biology Graduate Program, University of California, Merced, CA 95343, USA.
[Ti] Título:EC-tagging allows cell type-specific RNA analysis.
[So] Source:Nucleic Acids Res;45(15):e138, 2017 Sep 06.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Purification of cell type-specific RNAs remains a significant challenge. One solution involves biosynthetic tagging of target RNAs. RNA tagging via incorporation of 4-thiouracil (TU) in cells expressing transgenic uracil phosphoribosyltransferase (UPRT), a method known as TU-tagging, has been used in multiple systems but can have limited specificity due to endogenous pathways of TU incorporation. Here, we describe an alternative method that requires the activity of two enzymes: cytosine deaminase (CD) and UPRT. We found that the sequential activity of these enzymes converts 5-ethynylcytosine (EC) to 5-ethynyluridine monophosphate that is subsequently incorporated into nascent RNAs. The ethynyl group allows efficient detection and purification of tagged RNAs. We show that 'EC-tagging' occurs in tissue culture cells and Drosophila engineered to express CD and UPRT. Additional control can be achieved through a split-CD approach in which functional CD is reconstituted from independently expressed fragments. We demonstrate the sensitivity and specificity of EC-tagging by obtaining cell type-specific gene expression data from intact Drosophila larvae, including transcriptome measurements from a small population of central brain neurons. EC-tagging provides several advantages over existing techniques and should be broadly useful for investigating the role of differential RNA expression in cell identity, physiology and pathology.
[Mh] Termos MeSH primário: Linhagem da Célula/genética
Citosina/análogos & derivados
RNA/análise
Coloração e Rotulagem/métodos
[Mh] Termos MeSH secundário: Animais
Animais Geneticamente Modificados
Células Cultivadas
Citosina/metabolismo
Citosina/farmacologia
Citosina Desaminase/metabolismo
Drosophila melanogaster
Perfilação da Expressão Gênica/métodos
Células HeLa
Seres Humanos
Especificidade de Órgãos/genética
Pentosiltransferases/metabolismo
RNA/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (5-ethynylcytosine); 63231-63-0 (RNA); 8J337D1HZY (Cytosine); EC 2.4.2.- (Pentosyltransferases); EC 2.4.2.9 (uracil phosphoribosyltransferase); EC 3.5.4.1 (Cytosine Deaminase)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171107
[Lr] Data última revisão:
171107
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170624
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkx551


  5 / 1084 MEDLINE  
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[PMID]:28478051
[Au] Autor:Zhao Y; She N; Zhang X; Wang C; Mo Y
[Ad] Endereço:The Key Laboratory of Natural Medicine and Immuno-Engineering, Henan University, Kaifeng 475004, China. Electronic address: zhaoyuan@henu.edu.cn.
[Ti] Título:Product release mechanism and the complete enzyme catalysis cycle in yeast cytosine deaminase (yCD): A computational study.
[So] Source:Biochim Biophys Acta;1865(8):1020-1029, 2017 08.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Yeast cytosine deaminase (yCD) is critical in gene-directed enzyme prodrug therapy as it catalyzes the hydrolytic deamination of cytosine. The product (uracil) release process is considered as rate-limiting in the whole enzymatic catalysis and includes the cleavage of the uracil-metal bond and the delivery of free uracil out of the reactive site. Herein extensive combined random acceleration molecular dynamics (RAMD) and molecular dynamics (MD) simulations coupled with the umbrella sampling technique have been performed to study the product transport mechanism. Five channels have been identified, and the thermodynamic and dynamic characterizations for the two most favorable channels have been determined and analyzed. The free energy barrier for the most beneficial pathway is about 13kcal/mol and mainly results from the cleavage of hydrogen bonds between the ligand uracil and surrounding residues Asn51, Glu64, and Asp155. The conjugated rings of Phe114 and Trp152 play gating and guiding roles in the product delivery via π⋯π van der Waals interactions with the product. Finally, the full cycle of the enzymatic catalysis has been determined, making the whole process computationally more precise.
[Mh] Termos MeSH primário: Citosina Desaminase/química
Citosina Desaminase/metabolismo
Leveduras/metabolismo
[Mh] Termos MeSH secundário: Sítios de Ligação/fisiologia
Catálise
Biologia Computacional/métodos
Citosina/química
Citosina/metabolismo
Ligações de Hidrogênio
Simulação de Dinâmica Molecular
Pró-Fármacos/química
Termodinâmica
Uracila/química
Uracila/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Prodrugs); 56HH86ZVCT (Uracil); 8J337D1HZY (Cytosine); EC 3.5.4.1 (Cytosine Deaminase)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170926
[Lr] Data última revisão:
170926
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170508
[St] Status:MEDLINE


  6 / 1084 MEDLINE  
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[PMID]:28476782
[Au] Autor:Dore-Savard L; Chen Z; Winnard PT; Krishnamachary B; Raman V; Black ME; Bhujwalla ZM
[Ad] Endereço:Division of Cancer Imaging Research, The Russell H. Morgan Department of Radiology and Radiological Science, The Johns Hopkins University School of Medicine, Baltimore, MD, U.S.A.
[Ti] Título:Delayed Progression of Lung Metastases Following Delivery of a Prodrug-activating Enzyme.
[So] Source:Anticancer Res;37(5):2195-2200, 2017 05.
[Is] ISSN:1791-7530
[Cp] País de publicação:Greece
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Chemotherapy is an effective option to treat recurrent or metastatic cancer but its debilitating side-effects limit the dose and time of exposure. Prodrugs that can be activated locally by an activating enzyme can minimize collateral damage from chemotherapy. We previously demonstrated the efficacy of a poly-L-lysine-based theranostic nanoplex containing bacterial cytosine deaminase (bCD) that locally converted 5-fluorocytosine (5-FC) to the chemotherapeutic agent 5-fluorouracil in MDA-MB-231 primary tumor xenografts. MATERIALS AND METHODS: Here we used a more effective variant of bCD to target metastatic red fluorescence protein expressing MDA-MB-435 cells in the lungs. We used an intravenous injection of tumor cells and monitored tumor growth in the lungs for 5 weeks by which time metastatic nodules were detected with optical imaging. The animals were then treated with the bCD-nanoplex and 5-FC. RESULTS: We observed a significant decrease in metastatic burden with a single dose of the enzyme-nanoplex and two consecutive prodrug injections. CONCLUSION: These results are a first step towards the longitudinal evaluation of such a strategy with multiple doses. Additionally, the enzyme can be directly coupled to imaging reporters to time prodrug administration for the detection and treatment of aggressive metastatic cancer.
[Mh] Termos MeSH primário: Antineoplásicos/administração & dosagem
Citosina Desaminase/administração & dosagem
Proteínas de Escherichia coli/administração & dosagem
Fluoruracila/administração & dosagem
Neoplasias Pulmonares/tratamento farmacológico
Pró-Fármacos/administração & dosagem
[Mh] Termos MeSH secundário: Animais
Antineoplásicos/química
Antineoplásicos/uso terapêutico
Linhagem Celular Tumoral
Citosina Desaminase/química
Citosina Desaminase/uso terapêutico
Progressão da Doença
Portadores de Fármacos/administração & dosagem
Portadores de Fármacos/química
Portadores de Fármacos/uso terapêutico
Proteínas de Escherichia coli/química
Proteínas de Escherichia coli/uso terapêutico
Feminino
Fluoruracila/química
Fluoruracila/uso terapêutico
Seres Humanos
Neoplasias Pulmonares/patologia
Camundongos SCID
Nanoestruturas/administração & dosagem
Nanoestruturas/química
Nanoestruturas/uso terapêutico
Polietilenoimina/administração & dosagem
Polietilenoimina/química
Polietilenoimina/uso terapêutico
Polilisina/administração & dosagem
Polilisina/química
Polilisina/uso terapêutico
Pró-Fármacos/química
Pró-Fármacos/uso terapêutico
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antineoplastic Agents); 0 (Drug Carriers); 0 (Escherichia coli Proteins); 0 (Prodrugs); 25104-18-1 (Polylysine); 9002-98-6 (Polyethyleneimine); EC 3.5.4.1 (Cytosine Deaminase); EC 3.5.4.1 (codA protein, E coli); U3P01618RT (Fluorouracil)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170810
[Lr] Data última revisão:
170810
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170507
[St] Status:MEDLINE


  7 / 1084 MEDLINE  
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[PMID]:28475648
[Au] Autor:Nakano Y; Misawa N; Juarez-Fernandez G; Moriwaki M; Nakaoka S; Funo T; Yamada E; Soper A; Yoshikawa R; Ebrahimi D; Tachiki Y; Iwami S; Harris RS; Koyanagi Y; Sato K
[Ad] Endereço:Laboratory of Systems Virology, Department of Biosystems Science, Institute for Frontier Life and Medical Sciences, Kyoto University, Kyoto, Japan.
[Ti] Título:HIV-1 competition experiments in humanized mice show that APOBEC3H imposes selective pressure and promotes virus adaptation.
[So] Source:PLoS Pathog;13(5):e1006348, 2017 May.
[Is] ISSN:1553-7374
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:APOBEC3 (A3) family proteins are DNA cytosine deaminases recognized for contributing to HIV-1 restriction and mutation. Prior studies have demonstrated that A3D, A3F, and A3G enzymes elicit a robust anti-HIV-1 effect in cell cultures and in humanized mouse models. Human A3H is polymorphic and can be categorized into three phenotypes: stable, intermediate, and unstable. However, the anti-viral effect of endogenous A3H in vivo has yet to be examined. Here we utilize a hematopoietic stem cell-transplanted humanized mouse model and demonstrate that stable A3H robustly affects HIV-1 fitness in vivo. In contrast, the selection pressure mediated by intermediate A3H is relaxed. Intriguingly, viral genomic RNA sequencing reveled that HIV-1 frequently adapts to better counteract stable A3H during replication in humanized mice. Molecular phylogenetic analyses and mathematical modeling suggest that stable A3H may be a critical factor in human-to-human viral transmission. Taken together, this study provides evidence that stable variants of A3H impose selective pressure on HIV-1.
[Mh] Termos MeSH primário: Aminoidrolases/genética
Citosina Desaminase/genética
Infecções por HIV/virologia
HIV-1/fisiologia
Produtos do Gene vif do Vírus da Imunodeficiência Humana/genética
[Mh] Termos MeSH secundário: Aminoidrolases/metabolismo
Animais
Citosina Desaminase/metabolismo
Modelos Animais de Doenças
Células HEK293
Infecções por HIV/transmissão
HIV-1/genética
Seres Humanos
Camundongos
Camundongos Knockout
Modelos Genéticos
Mutação
Filogenia
RNA Viral/química
RNA Viral/genética
Análise de Sequência de RNA
Replicação Viral
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (RNA, Viral); 0 (vif Gene Products, Human Immunodeficiency Virus); 0 (vif protein, Human immunodeficiency virus 1); EC 3.5.4.- (APOBEC3H protein, human); EC 3.5.4.- (Aminohydrolases); EC 3.5.4.1 (APOBEC3 protein, human); EC 3.5.4.1 (Cytosine Deaminase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171114
[Lr] Data última revisão:
171114
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170506
[St] Status:MEDLINE
[do] DOI:10.1371/journal.ppat.1006348


  8 / 1084 MEDLINE  
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[PMID]:28299671
[Au] Autor:Kim DY; Gross JD
[Ad] Endereço:College of Pharmacy, Yeungnam University, Gyeongsan, 38541, South Korea.
[Ti] Título:CBFß and HIV Infection.
[So] Source:Adv Exp Med Biol;962:415-431, 2017.
[Is] ISSN:0065-2598
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In order to achieve a persistent infection, viruses must overcome the host immune system. Host restriction factors dominantly block virus transmission, but are subject to down regulation by viral accessory proteins. HIV encodes several accessory factors that overcome different cellular restriction factors. For example, the HIV-1 protein Vif down regulates the human APOBEC3 family of restriction factors by targeting them for proteolysis by the ubiquitin-proteasome pathway. Recently, this function was shown to require the transcription cofactor CBFß, which acts as a template to assist in Vif folding and allow for assembly of an APOBEC3-targeting E3 ligase complex. In uninfected cells, CBFß is an essential binding partner of RUNX transcription factors. By binding CBFß, Vif has also been shown to perturb transcription of genes regulated by the RUNX proteins, including restrictive APOBEC3 family members. Here we review how the link between CBFß and Vif supports transcriptional and post-transcriptional repression of innate immunity. The ability of a single viral protein to coopt multiple host pathways is an economical strategy for a pathogen with limited protein coding capacity to achieve a productive infection.
[Mh] Termos MeSH primário: Subunidade beta de Fator de Ligação ao Core/metabolismo
Infecções por HIV/metabolismo
Infecções por HIV/virologia
HIV-1/metabolismo
Produtos do Gene vif do Vírus da Imunodeficiência Humana/metabolismo
[Mh] Termos MeSH secundário: Animais
Subunidade beta de Fator de Ligação ao Core/imunologia
Citosina Desaminase/imunologia
Citosina Desaminase/metabolismo
Infecções por HIV/imunologia
HIV-1/imunologia
Interações Hospedeiro-Patógeno/imunologia
Interações Hospedeiro-Patógeno/fisiologia
Seres Humanos
Imunidade Inata/imunologia
Transcrição Genética/imunologia
Transcrição Genética/fisiologia
Produtos do Gene vif do Vírus da Imunodeficiência Humana/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T; REVIEW
[Nm] Nome de substância:
0 (Core Binding Factor beta Subunit); 0 (vif Gene Products, Human Immunodeficiency Virus); EC 3.5.4.1 (Cytosine Deaminase)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170926
[Lr] Data última revisão:
170926
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170317
[St] Status:MEDLINE
[do] DOI:10.1007/978-981-10-3233-2_25


  9 / 1084 MEDLINE  
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[PMID]:28266028
[Au] Autor:Cardinaud S; Urrutia A; Rouers A; Coulon PG; Kervevan J; Richetta C; Bet A; Maze EA; Larsen M; Iglesias MC; Appay V; Graff-Dubois S; Moris A
[Ad] Endereço:Sorbonne Universités, UPMC Univ Paris 06, INSERM U1135, CNRS ERL 8255, Center for Immunology and Microbial Infections - CIMI-Paris, Paris, France.
[Ti] Título:Triggering of TLR-3, -4, NOD2, and DC-SIGN reduces viral replication and increases T-cell activation capacity of HIV-infected human dendritic cells.
[So] Source:Eur J Immunol;47(5):818-829, 2017 May.
[Is] ISSN:1521-4141
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:A variety of signals influence the capacity of dendritic cells (DCs) to mount potent antiviral cytotoxic T-cell (CTL) responses. In particular, innate immune sensing by pathogen recognition receptors, such as TLR and C-type lectines, influences DC biology and affects their susceptibility to HIV infection. Yet, whether the combined effects of PPRs triggering and HIV infection influence HIV-specific (HS) CTL responses remain enigmatic. Here, we dissect the impact of innate immune sensing by pathogen recognition receptors on DC maturation, HIV infection, and on the quality of HS CTL activation. Remarkably, ligand-driven triggering of TLR-3, -4, NOD2, and DC-SIGN, despite reducing viral replication, markedly increased the capacity of infected DCs to stimulate HS CTLs. This was exemplified by the diversity and the quantity of cytokines produced by HS CTLs primed by these DCs. Infecting DCs with viruses harboring members of the APOBEC family of antiviral factors enhanced the antigen-presenting skills of infected DCs. Our results highlight the tight interplay between innate and adaptive immunity and may help develop innovative immunotherapies against viral infections.
[Mh] Termos MeSH primário: Células Dendríticas/imunologia
Células Dendríticas/virologia
HIV-1/fisiologia
Ativação Linfocitária
Replicação Viral
[Mh] Termos MeSH secundário: Apresentação do Antígeno
Moléculas de Adesão Celular/genética
Moléculas de Adesão Celular/imunologia
Moléculas de Adesão Celular/metabolismo
Citosina Desaminase/genética
Citosina Desaminase/metabolismo
Células Dendríticas/fisiologia
HIV-1/imunologia
Seres Humanos
Lectinas Tipo C/genética
Lectinas Tipo C/imunologia
Lectinas Tipo C/metabolismo
Proteína Adaptadora de Sinalização NOD2/genética
Proteína Adaptadora de Sinalização NOD2/imunologia
Proteína Adaptadora de Sinalização NOD2/metabolismo
Padrões Moleculares Associados a Patógenos
Receptores de Superfície Celular/genética
Receptores de Superfície Celular/imunologia
Receptores de Superfície Celular/metabolismo
Linfócitos T Citotóxicos/imunologia
Receptor 3 Toll-Like/genética
Receptor 3 Toll-Like/imunologia
Receptor 3 Toll-Like/metabolismo
Receptor 4 Toll-Like/genética
Receptor 4 Toll-Like/imunologia
Receptor 4 Toll-Like/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cell Adhesion Molecules); 0 (DC-specific ICAM-3 grabbing nonintegrin); 0 (Lectins, C-Type); 0 (NOD2 protein, human); 0 (Nod2 Signaling Adaptor Protein); 0 (Pathogen-Associated Molecular Pattern Molecules); 0 (Receptors, Cell Surface); 0 (TLR3 protein, human); 0 (TLR4 protein, human); 0 (Toll-Like Receptor 3); 0 (Toll-Like Receptor 4); EC 3.5.4.1 (APOBEC3 protein, human); EC 3.5.4.1 (Cytosine Deaminase)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170908
[Lr] Data última revisão:
170908
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170308
[St] Status:MEDLINE
[do] DOI:10.1002/eji.201646603


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[PMID]:27881650
[Au] Autor:Ara A; Love RP; Follack TB; Ahmed KA; Adolph MB; Chelico L
[Ad] Endereço:University of Saskatchewan, Microbiology and Immunology, College of Medicine, Saskatoon, Saskatchewan, Canada.
[Ti] Título:Mechanism of Enhanced HIV Restriction by Virion Coencapsidated Cytidine Deaminases APOBEC3F and APOBEC3G.
[So] Source:J Virol;91(3), 2017 Feb 01.
[Is] ISSN:1098-5514
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The APOBEC3 (A3) enzymes, A3G and A3F, are coordinately expressed in CD4 T cells and can become coencapsidated into HIV-1 virions, primarily in the absence of the viral infectivity factor (Vif). A3F and A3G are deoxycytidine deaminases that inhibit HIV-1 replication by inducing guanine-to-adenine hypermutation through deamination of cytosine to form uracil in minus-strand DNA. The effect of the simultaneous presence of both A3G and A3F on HIV-1 restriction ability is not clear. Here, we used a single-cycle infectivity assay and biochemical analyses to determine if coencapsidated A3G and A3F differ in their restriction capacity from A3G or A3F alone. Proviral DNA sequencing demonstrated that compared to each A3 enzyme alone, A3G and A3F, when combined, had a coordinate effect on hypermutation. Using size exclusion chromatography, rotational anisotropy, and in vitro deamination assays, we demonstrate that A3F promotes A3G deamination activity by forming an A3F/G hetero-oligomer in the absence of RNA which is more efficient at deaminating cytosines. Further, A3F caused the accumulation of shorter reverse transcripts due to decreasing reverse transcriptase efficiency, which would leave single-stranded minus-strand DNA exposed for longer periods of time, enabling more deamination events to occur. Although A3G and A3F are known to function alongside each other, these data provide evidence for an A3F/G hetero-oligomeric A3 with unique properties compared to each individual counterpart. IMPORTANCE: The APOBEC3 enzymes APOBEC3F and APOBEC3G act as a barrier to HIV-1 replication in the absence of the HIV-1 Vif protein. After APOBEC3 enzymes are encapsidated into virions, they deaminate cytosines in minus-strand DNA, which forms promutagenic uracils that induce transition mutations or proviral DNA degradation. Even in the presence of Vif, footprints of APOBEC3-catalyzed deaminations are found, demonstrating that APOBEC3s still have discernible activity against HIV-1 in infected individuals. We undertook a study to better understand the activity of coexpressed APOBEC3F and APOBEC3G. The data demonstrate that an APOBEC3F/APOBEC3G hetero-oligomer can form that has unique properties compared to each APOBEC3 alone. This hetero-oligomer has increased efficiency of virus hypermutation, raising the idea that we still may not fully realize the antiviral mechanisms of endogenous APOBEC3 enzymes. Hetero-oligomerization may be a mechanism to increase their antiviral activity in the presence of Vif.
[Mh] Termos MeSH primário: Desaminase APOBEC-3G/metabolismo
Capsídeo/metabolismo
Citosina Desaminase/metabolismo
Infecções por HIV/metabolismo
Infecções por HIV/virologia
HIV-1/fisiologia
Vírion/fisiologia
[Mh] Termos MeSH secundário: Desaminase APOBEC-3G/química
Linhagem Celular
Citosina Desaminase/química
Expressão Gênica
Seres Humanos
Espaço Intracelular
Ligação Proteica
Multimerização Proteica
Transporte Proteico
Proteínas de Ligação a RNA/química
Proteínas de Ligação a RNA/metabolismo
Proteínas Recombinantes de Fusão
Transcrição Reversa
Deleção de Sequência
Montagem de Vírus
Replicação Viral
Produtos do Gene vif do Vírus da Imunodeficiência Humana/genética
Produtos do Gene vif do Vírus da Imunodeficiência Humana/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (RNA-Binding Proteins); 0 (Recombinant Fusion Proteins); 0 (vif Gene Products, Human Immunodeficiency Virus); EC 3.5.4.1 (APOBEC3F protein, human); EC 3.5.4.1 (Cytosine Deaminase); EC 3.5.4.5 (APOBEC-3G Deaminase)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170718
[Lr] Data última revisão:
170718
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161125
[St] Status:MEDLINE



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