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  1 / 7938 MEDLINE  
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[PMID]:28463571
[Au] Autor:Penaud-Budloo M; Lecomte E; Guy-Duché A; Saleun S; Roulet A; Lopez-Roques C; Tournaire B; Cogné B; Léger A; Blouin V; Lindenbaum P; Moullier P; Ayuso E
[Ad] Endereço:1 INSERM UMR1089, University of Nantes, Centre Hospitalier Universitaire, Nantes, France.
[Ti] Título:Accurate Identification and Quantification of DNA Species by Next-Generation Sequencing in Adeno-Associated Viral Vectors Produced in Insect Cells.
[So] Source:Hum Gene Ther Methods;28(3):148-162, 2017 06.
[Is] ISSN:1946-6544
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Recombinant adeno-associated viral (rAAV) vectors have proven excellent tools for the treatment of many genetic diseases and other complex diseases. However, the illegitimate encapsidation of DNA contaminants within viral particles constitutes a major safety concern for rAAV-based therapies. Moreover, the development of rAAV vectors for early-phase clinical trials has revealed the limited accuracy of the analytical tools used to characterize these new and complex drugs. Although most published data concerning residual DNA in rAAV preparations have been generated by quantitative PCR, we have developed a novel single-strand virus sequencing (SSV-Seq) method for quantification of DNA contaminants in AAV vectors produced in mammalian cells by next-generation sequencing (NGS). Here, we describe the adaptation of SSV-Seq for the accurate identification and quantification of DNA species in rAAV stocks produced in insect cells. We found that baculoviral DNA was the most abundant contaminant, representing less than 2.1% of NGS reads regardless of serotype (2, 8, or rh10). Sf9 producer cell DNA was detected at low frequency (≤0.03%) in rAAV lots. Advanced computational analyses revealed that (1) baculoviral sequences close to the inverted terminal repeats preferentially underwent illegitimate encapsidation, and (2) single-nucleotide variants were absent from the rAAV genome. The high-throughput sequencing protocol described here enables effective DNA quality control of rAAV vectors produced in insect cells, and is adapted to conform with regulatory agency safety requirements.
[Mh] Termos MeSH primário: Dependovirus/genética
Sequenciamento de Nucleotídeos em Larga Escala/métodos
Análise de Sequência de DNA/métodos
[Mh] Termos MeSH secundário: Animais
Baculoviridae/genética
Contaminação por DNA
Células HEK293
Sequenciamento de Nucleotídeos em Larga Escala/normas
Seres Humanos
Análise de Sequência de DNA/normas
Células Sf9
Spodoptera
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Em] Mês de entrada:1710
[Cu] Atualização por classe:180310
[Lr] Data última revisão:
180310
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170503
[St] Status:MEDLINE
[do] DOI:10.1089/hgtb.2016.185


  2 / 7938 MEDLINE  
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[PMID]:29295984
[Au] Autor:Goyal N; Rossi MJ; Mazina OM; Chi Y; Moritz RL; Clurman BE; Mazin AV
[Ad] Endereço:Department of Biochemistry and Molecular Biology, Drexel University College of Medicine, Philadelphia, PA, 19102, USA.
[Ti] Título:RAD54 N-terminal domain is a DNA sensor that couples ATP hydrolysis with branch migration of Holliday junctions.
[So] Source:Nat Commun;9(1):34, 2018 01 02.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:In eukaryotes, RAD54 catalyzes branch migration (BM) of Holliday junctions, a basic process during DNA repair, replication, and recombination. RAD54 also stimulates RAD51 recombinase and has other activities. Here, we investigate the structural determinants for different RAD54 activities. We find that the RAD54 N-terminal domain (NTD) is responsible for initiation of BM through two coupled, but distinct steps; specific binding to Holliday junctions and RAD54 oligomerization. Furthermore, we find that the RAD54 oligomeric state can be controlled by NTD phosphorylation at S49, a CDK2 consensus site, which inhibits RAD54 oligomerization and, consequently, BM. Importantly, the effect of phosphorylation on RAD54 oligomerization is specific for BM, as it does not affect stimulation of RAD51 recombinase by RAD54. Thus, the transition of the oligomeric states provides an important control of the biological functions of RAD54 and, likely, other multifunctional proteins.
[Mh] Termos MeSH primário: Adenosina Trifosfatases/metabolismo
DNA Helicases/metabolismo
DNA Cruciforme/metabolismo
Proteínas Nucleares/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Sítios de Ligação/genética
Linhagem Celular
DNA Helicases/química
DNA Helicases/genética
Reparo do DNA
DNA Cruciforme/química
DNA Cruciforme/genética
Seres Humanos
Hidrólise
Proteínas Nucleares/química
Proteínas Nucleares/genética
Conformação de Ácido Nucleico
Fosforilação
Multimerização Proteica
Recombinação Genética
Homologia de Sequência de Aminoácidos
Células Sf9
Spodoptera
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (DNA, Cruciform); 0 (Nuclear Proteins); 0 (RAD54L protein, human); EC 3.6.1.- (Adenosine Triphosphatases); EC 3.6.4.- (DNA Helicases)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180306
[Lr] Data última revisão:
180306
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180104
[St] Status:MEDLINE
[do] DOI:10.1038/s41467-017-02497-x


  3 / 7938 MEDLINE  
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[PMID]:28460121
[Au] Autor:Dwi Sutanto K; El Salamouny S; Tufail M; Ghulam Rasool K; Sukirno S; Shepard M; Shapiro M; Saad Aldawood A
[Ad] Endereço:Economic Entomology Research Unit (EERU), Department of Plant Protection, College of Food and Agriculture Sciences, King Saud University, Riyadh 11451, Saudi Arabia (kokodwisutanto@yahoo.com; said_elsalamouny@yahoo.com; mtufail@ksu.edu.sa; krasool@ksu.edu.sa; sukirnobiougm@ugm.ac.id; aldawood@ksu.ed
[Ti] Título:Evaluation of Natural Additives to Enhance the Persistence of Spodoptera littoralis (Lepidoptera: Noctuidae) Nucleopolyhedrovirus (SpliMNPV) Under Field Conditions in Saudi Arabia.
[So] Source:J Econ Entomol;110(3):924-930, 2017 06 01.
[Is] ISSN:1938-291X
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Nucleopolyhedrovirus is an effective biocontrol agent but for its biggest disadvantage of short persistence under sunlight conditions. In this study, 10 plant extracts were evaluated as ultraviolet (UV) protectants to improve the persistence of Spodoptera littoralis multiple-embedded nucleopolyhedrovirus (SpliMNPV) against cotton leafworm (Spodoptera littoralis Boisduval). In the primary lab screening test, 5 out of 10 additives (cloves, henna, green tea, pomegranate, and grape extracts) presented a high rate of virus protection with original activity remaining (OAR) percentage of 100%, 97%, 91%, 90.6%, and 77%, respectively, when used at a concentration of 1% and exposed to UVB for a period of 1 h. A secondary screening was then performed with these best five extracts at a concentration of 0.5% and for an exposure timing of 5 h to UVB. Among these, clove and henna that showed highest protection with OAR values of 96.6% and 76.5%, respectively, were selected for the field trials. When applied on cabbage in the field during sunny summer conditions, clove and henna extracts enhanced the persistence of SpliMNPV by twofold. These findings are encouraging to be applied in the field studies.
[Mh] Termos MeSH primário: Nucleopolyhedrovirus/fisiologia
Controle Biológico de Vetores/métodos
Spodoptera/virologia
[Mh] Termos MeSH secundário: Animais
Larva/crescimento & desenvolvimento
Larva/virologia
Nucleopolyhedrovirus/efeitos da radiação
Arábia Saudita
Spodoptera/crescimento & desenvolvimento
Luz Solar
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Em] Mês de entrada:1709
[Cu] Atualização por classe:180301
[Lr] Data última revisão:
180301
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170502
[St] Status:MEDLINE
[do] DOI:10.1093/jee/tox085


  4 / 7938 MEDLINE  
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[PMID]:29293621
[Au] Autor:Wang S; Ding T; Xu M; Zhang B
[Ad] Endereço:Key Lab of Integrated Crop Pest Management of Shandong, College of Plant Health and Medicine, Qingdao Agricultural University, Qingdao, Shandong, the People Republic of China.
[Ti] Título:Bidirectional interactions between beet armyworm and its host in response to different fertilization conditions.
[So] Source:PLoS One;13(1):e0190502, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Fertilizer with different ratios of nitrogen (N) to phosphorus (P) can influence crop plant performance and defense against herbivores. Spodoptera exigua is an important agricultural pest that has caused serious economic loss, especially in recent decades. In the present study, we explored effects of different intensities and durations of S. exigua herbivory on host plant biomass and on S. exigua enzyme activities in response to five fertilizer treatments with different N: P ratios of 1: 5, 1: 3, 1: 1, 3: 1 and 5: 1. The results showed that fertilizer type can significantly influence interactions between caterpillars and its hosts. Compensatory growth of leaf biomass was detected under fertilizer with N: P = 3: 1. Fertilizer with a higher proportion of N appears to maintain stem biomass in defoliated seedlings similar to controls that are not exposed to herbivory. There was no significant difference in root biomass under most conditions. High proportion of N also enhanced the activity of two antioxidant enzymes, catalase (CAT) and superoxide dismutase (SOD) in low density of beet armyworm. However, with increased herbivorous intensity, a higher proportion of P played a more important role in increasing the activities of CAT and SOD. Higher P likely enhanced acetylcholine esterase (AChE) activity at lower degrees of defoliation, but a higher N proportion resulted in higher AChE activity at higher degrees of defoliation. Higher N proportion contributed to reduced carboxylesterase (CarE) activity at high intensity, short-term defoliation. However, when defoliation intensity increased, the difference in CarE activity between fertilizer categories was little. The study explored the interaction between the damage of S. exigua and the biomass accumulation of its host plant Brassica rapa, and the influence of the N/P ratio in plant fertilizer on this interaction. Systematic analysis was provided on the biomass of B. rapa and the activity of metabolic enzymes of S. exigua under different treatments.
[Mh] Termos MeSH primário: Fertilizantes
Spodoptera/fisiologia
[Mh] Termos MeSH secundário: Acetilcolinesterase/metabolismo
Animais
Catalase/metabolismo
Interações Hospedeiro-Parasita
Superóxido Dismutase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Fertilizers); EC 1.11.1.6 (Catalase); EC 1.15.1.1 (Superoxide Dismutase); EC 3.1.1.7 (Acetylcholinesterase)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180221
[Lr] Data última revisão:
180221
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180103
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0190502


  5 / 7938 MEDLINE  
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[PMID]:29235695
[Au] Autor:Hirowatari A; Chen Z; Mita K; Yamamoto K
[Ad] Endereço:Kyushu University Graduate School, Fukuoka, Japan.
[Ti] Título:Enzymatic characterization of two epsilon-class glutathione S-transferases of Spodoptera litura.
[So] Source:Arch Insect Biochem Physiol;97(3), 2018 Mar.
[Is] ISSN:1520-6327
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Two cDNAs encoding glutathione S-transferase (GST) of the tobacco cutworm, Spodoptera litura, were cloned by reverse transcriptase-polymerase chain reaction. The deduced amino acid sequences of the resulting clones revealed 32-51% identities to the epsilon-class GSTs from other organisms. The recombinant proteins were functionally overexpressed in Escherichia coli cells in soluble form and were purified to homogeneity. The enzymes were capable of catalyzing the bioconjugation of glutathione with 1-chloro-2,4-dinitrobenzene, 1,2-epoxy-3-(4-nitrophenoxy)-propane, and ethacrynic acid. A competition assay revealed that the GST activity was inhibited by insecticides, suggesting that it could be conducive to insecticide tolerance in the tobacco cutworm.
[Mh] Termos MeSH primário: Glutationa Transferase/metabolismo
Spodoptera/enzimologia
[Mh] Termos MeSH secundário: Animais
Glutationa Transferase/química
Glutationa Transferase/genética
Glutationa Transferase/isolamento & purificação
Proteínas de Insetos/química
Proteínas de Insetos/genética
Proteínas de Insetos/isolamento & purificação
Proteínas de Insetos/metabolismo
Filogenia
Análise de Sequência de DNA
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Insect Proteins); EC 2.5.1.18 (Glutathione Transferase)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180216
[Lr] Data última revisão:
180216
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171214
[St] Status:MEDLINE
[do] DOI:10.1002/arch.21443


  6 / 7938 MEDLINE  
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[PMID]:29208467
[Au] Autor:Aduri NG; Ernst HA; Prabhala BK; Bhatt S; Boesen T; Gajhede M; Mirza O
[Ad] Endereço:Department of Drug Design and Pharmacology, Faculty of Health and Medical Sciences, University of Copenhagen, Copenhagen, Denmark.
[Ti] Título:Human proton coupled folic acid transporter is a monodisperse oligomer in the lauryl maltose neopentyl glycol solubilized state.
[So] Source:Biochem Biophys Res Commun;495(2):1738-1743, 2018 01 08.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The human proton coupled folic acid transporter PCFT is the major import route for dietary folates. Mutations in the gene encoding PCFT cause hereditary folic acid malabsorption, which manifests itself by compromised folate absorption from the intestine and also in impaired folate transport into the central nervous system. Since its recent discovery, PCFT has been the subject of numerous biochemical studies aiming at understanding its structure and mechanism. One major focus has been its oligomeric state, with some reports supporting oligomers and others a monomer. Here, we report the overexpression and purification of recombinant PCFT. Following detergent screening, n-Dodecyl ß-D-maltoside (DDM) and lauryl maltose neopentyl glycol (LMNG) were chosen for further work as they exhibited the most optimal solubilization. We found that purified detergent solubilized PCFT was able to bind folic acid, thus indicating a functionally active protein. Size exclusion chromatography showed that PCFT in DDM was polydisperse; the LMNG preparation was clearly monodisperse but with shorter retention time than the major DDM peak. To assess the oligomeric state negative stain electron microscopy was performed which showed a particle with the size of a PCFT dimer.
[Mh] Termos MeSH primário: Transportador de Folato Acoplado a Próton/química
[Mh] Termos MeSH secundário: Animais
Detergentes
Ácido Fólico/metabolismo
Glucosídeos
Glicóis
Seres Humanos
Ligantes
Microscopia Eletrônica
Modelos Moleculares
Multimerização Proteica
Estrutura Quaternária de Proteína
Transportador de Folato Acoplado a Próton/metabolismo
Transportador de Folato Acoplado a Próton/ultraestrutura
Proteínas Recombinantes/química
Proteínas Recombinantes/metabolismo
Proteínas Recombinantes/ultraestrutura
Células Sf9
Solubilidade
Spodoptera
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Detergents); 0 (Glucosides); 0 (Glycols); 0 (Ligands); 0 (Proton-Coupled Folate Transporter); 0 (Recombinant Proteins); 0 (SLC46A1 protein, human); 69227-93-6 (dodecyl maltoside); 935E97BOY8 (Folic Acid)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180212
[Lr] Data última revisão:
180212
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171207
[St] Status:MEDLINE


  7 / 7938 MEDLINE  
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[PMID]:29324805
[Au] Autor:Lee YT; Ko EJ; Lee Y; Kim KH; Kim MC; Lee YN; Kang SM
[Ad] Endereço:Center for Inflammation, Immunity & Infection, Institute for Biomedical Sciences, Georgia State University, Atlanta, Georgia, United States of America.
[Ti] Título:Intranasal vaccination with M2e5x virus-like particles induces humoral and cellular immune responses conferring cross-protection against heterosubtypic influenza viruses.
[So] Source:PLoS One;13(1):e0190868, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Current influenza vaccines do not provide broad cross-protection. Here, we report that intranasal vaccination with virus-like particles containing the highly conserved multiple ectodomains of matrix protein 2 (M2e5x VLP) of influenza virus induces broad cross-protection by M2-specific humoral and cellular immune responses. M2e5x VLP intranasal vaccination prevented severe weight loss, attenuated inflammatory cytokines and cellular infiltrates, and lowered viral loads, and induced germinal center phenotypic B and plasma cells. In addition, depletion studies demonstrate the protective roles of CD4 and CD8 T cells induced by M2e5x VLP intranasal vaccination. Thus, this study provides evidence that mucosal delivery of M2e5x VLP vaccine provides cross-protection by inducing humoral and cellular immune responses.
[Mh] Termos MeSH primário: Proteção Cruzada
Vírus da Influenza A Subtipo H3N2/imunologia
Vírus da Influenza A Subtipo H5N1/imunologia
Vacinas contra Influenza/administração & dosagem
Vacinas de Partículas Semelhantes a Vírus/administração & dosagem
Proteínas da Matriz Viral/imunologia
[Mh] Termos MeSH secundário: Administração Intranasal
Animais
Anticorpos Antivirais/análise
Anticorpos Antivirais/sangue
Linfócitos B/imunologia
Linfócitos T CD4-Positivos/imunologia
Linfócitos T CD8-Positivos/imunologia
Embrião de Galinha
Feminino
Pulmão/imunologia
Pulmão/virologia
Camundongos Endogâmicos BALB C
Infecções por Orthomyxoviridae/imunologia
Infecções por Orthomyxoviridae/prevenção & controle
Infecções por Orthomyxoviridae/virologia
Células Sf9
Spodoptera
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Antibodies, Viral); 0 (Influenza Vaccines); 0 (Vaccines, Virus-Like Particle); 0 (Viral Matrix Proteins)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180206
[Lr] Data última revisão:
180206
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180112
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0190868


  8 / 7938 MEDLINE  
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[PMID]:29232719
[Au] Autor:Oki N; Kaga A; Shimizu T; Takahashi M; Kono Y; Takahashi M
[Ad] Endereço:Kyushu Okinawa Agricultural Research Center,National Agriculture and Food Research Organization, Suya, Koushi, Kumamoto, Japan.
[Ti] Título:QTL mapping of antixenosis resistance to common cutworm (Spodoptera litura Fabricius) in wild soybean (Glycine soja).
[So] Source:PLoS One;12(12):e0189440, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The common cutworm (CCW; Spodoptera litura Fabricius) is a serious herbivorous insect pest of soybean (Glycine max) in Asia and Oceania. Previously, we identified quantitative trait loci (QTLs) for CCW-antibiosis-resistance, CCW-1 and CCW-2, and antixenosis-resistance, qRslx1 and qRslx2, in the cultivar 'Himeshirazu'. The effects of these QTLs are useful in the breeding of CCW-resistant cultivars. In this study, we conducted an antixenosis bioassay on CCW using recombinant inbred lines derived from a cross between a wild soybean (Glycine soja) and the leading cultivar 'Fukuyutaka' to identify CCW-resistance genes in G. soja. The QTL analysis revealed six and four novel antixenosis-resistance QTLs in 2012 and 2013, respectively. Among them, the QTLs on chromosomes 2 and 7, designated qRslx4 and qRslx3, respectively, were stably detected in both years. qRslx3 exhibited the largest effect in both years, suggesting that qRslx3 can be exploited in the breeding of CCW-resistant soybean. Furthermore, qRslx3 and qRslx4 can be used, along with previously reported QTLs from 'Himeshirazu', to enhance the CCW-resistance of soybean cultivars because their chromosomal positions are unique. These new CCW-resistance QTLs from G. soja should play important roles in the breeding of CCW-resistant soybean cultivars.
[Mh] Termos MeSH primário: Locos de Características Quantitativas
Feijão de Soja/parasitologia
Spodoptera/patogenicidade
[Mh] Termos MeSH secundário: Animais
Ligação Genética
Feijão de Soja/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180104
[Lr] Data última revisão:
180104
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171213
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0189440


  9 / 7938 MEDLINE  
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[PMID]:29182509
[Au] Autor:Xie L; Lu B; Zheng Z; Miao Y; Liu Y; Zhang Y; Zheng C; Ke X; Hu Q; Wang H
[Ad] Endereço:1​CAS Key Laboratory of Special Pathogens and Biosafety, Center for Emerging Infectious Diseases, Wuhan Institute of Virology, Chinese Academy of Sciences, Wuhan, PR China.
[Ti] Título:The 3C protease of enterovirus A71 counteracts the activity of host zinc-finger antiviral protein (ZAP).
[So] Source:J Gen Virol;99(1):73-85, 2018 Jan.
[Is] ISSN:1465-2099
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Enterovirus A71 (EV-A71) is a positive-strand RNA virus that causes hand-foot-mouth disease and neurological complications in children and infants. Although the underlying mechanisms remain to be further defined, impaired immunity is thought to play an important role. The host zinc-finger antiviral protein (ZAP), an IFN-stimulated gene product, has been reported to specifically inhibit the replication of certain viruses. However, whether ZAP restricts the infection of enteroviruses remains unknown. Here, we report that EV-A71 infection upregulates ZAP mRNA in RD and HeLa cells. Moreover, ZAP overexpression rendered 293 T cells resistant to EV-A71 infection, whereas siRNA-mediated depletion of endogenous ZAP enhanced EV-A71 infection. The EV-A71 infection stimulated site-specific proteolysis of two ZAP isoforms, leading to the accumulation of a 40 kDa N-terminal ZAP fragment in virus-infected cells. We further revealed that the 3C protease (3Cpro) of EV-A71 mediates ZAP cleavage, which requires protease activity. Furthermore, ZAP variants with single amino acid substitutions at Gln-369 were resistant to 3Cpro cleavage, implying that Gln-369 is the sole cleavage site in ZAP. Moreover, although ZAP overexpression inhibited EV-A71 replication, the cleaved fragments did not show this effect. Our results indicate that an equilibrium between ZAP and enterovirus 3Cpro controls viral infection. The findings in this study suggest that viral 3Cpro mediated ZAP cleavage may represent a mechanism to escape host antiviral responses.
[Mh] Termos MeSH primário: Cisteína Endopeptidases/metabolismo
Enterovirus Humano A/enzimologia
Interações Hospedeiro-Patógeno
Proteínas de Ligação a RNA/metabolismo
Proteínas Virais/metabolismo
Replicação Viral
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Substituição de Aminoácidos
Animais
Linhagem Celular Tumoral
Cisteína Endopeptidases/genética
Enterovirus Humano A/genética
Regulação da Expressão Gênica
Genes Reporter
Células HEK293
Células HeLa
Seres Humanos
Luciferases/genética
Luciferases/metabolismo
Células Musculares/metabolismo
Células Musculares/virologia
Proteólise
RNA Interferente Pequeno/genética
RNA Interferente Pequeno/metabolismo
Proteínas de Ligação a RNA/antagonistas & inibidores
Proteínas de Ligação a RNA/genética
Células Sf9/imunologia
Células Sf9/virologia
Transdução de Sinais
Spodoptera
Proteínas Virais/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (RNA, Small Interfering); 0 (RNA-Binding Proteins); 0 (Viral Proteins); 0 (ZC3HAV1 protein, human); EC 1.13.12.- (Luciferases); EC 3.4.22.- (Cysteine Endopeptidases); EC 3.4.22.28 (3C proteases)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171229
[Lr] Data última revisão:
171229
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171129
[St] Status:MEDLINE
[do] DOI:10.1099/jgv.0.000982


  10 / 7938 MEDLINE  
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[PMID]:28450392
[Au] Autor:Wu D; Zhao L; Feng Z; Yu C; Ding J; Wang L; Wang F; Liu D; Zhu H; Xing F; Conaway JW; Conaway RC; Cai Y; Jin J
[Ad] Endereço:From the School of Life Sciences.
[Ti] Título:-Linked -acetylglucosamine transferase 1 regulates global histone H4 acetylation via stabilization of the nonspecific lethal protein NSL3.
[So] Source:J Biol Chem;292(24):10014-10025, 2017 06 16.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The human males absent on the first (MOF)-containing histone acetyltransferase nonspecific lethal (NSL) complex comprises nine subunits including the -linked -acetylglucosamine ( -GlcNAc) transferase, isoform 1 (OGT1). However, whether the -GlcNAc transferase activity of OGT1 controls histone acetyltransferase activity of the NSL complex and whether OGT1 physically interacts with the other NSL complex subunits remain unclear. Here, we demonstrate that OGT1 regulates the activity of the NSL complex by mainly acetylating histone H4 Lys-16, Lys-5, and Lys-8 via -GlcNAcylation and stabilization of the NSL complex subunit NSL3. Knocking down or overexpressing OGT1 in human cells remarkably affected the global acetylation of histone H4 residues Lys-16, Lys-5, and Lys-8. Because OGT1 is a subunit of the NSL complex, we also investigated the function of OGT1 in this complex. Co-transfection/co-immunoprecipitation experiments combined with -GlcNAc transferase assays confirmed that OGT1 specifically binds to and -GlcNAcylates NSL3. In addition, wheat germ agglutinin affinity purification verified the occurrence of -GlcNAc modification on NSL3 in cells. Moreover, -GlcNAcylation of NSL3 by wild-type OGT1 (OGT1-WT) stabilized NSL3. This stabilization was lost after co-transfection of NSL3 with an OGT1 mutant, OGT1 , that lacks -GlcNAc transferase activity. Furthermore, stabilization of NSL3 by OGT1-WT significantly increased the global acetylation levels of H4 Lys-5, Lys-8, and Lys-16 in cells. These results suggest that OGT1 regulates the activity of the NSL complex by stabilizing NSL3.
[Mh] Termos MeSH primário: Histona Acetiltransferases/metabolismo
Histonas/metabolismo
N-Acetilglucosaminiltransferases/metabolismo
Proteínas Nucleares/metabolismo
Processamento de Proteína Pós-Traducional
[Mh] Termos MeSH secundário: Acetilação
Substituição de Aminoácidos
Animais
Células HEK293
Células HeLa
Histona Acetiltransferases/antagonistas & inibidores
Histona Acetiltransferases/química
Histona Acetiltransferases/genética
Seres Humanos
Isoenzimas/química
Isoenzimas/genética
Isoenzimas/metabolismo
N-Acetilglucosaminiltransferases/antagonistas & inibidores
N-Acetilglucosaminiltransferases/química
N-Acetilglucosaminiltransferases/genética
Proteínas Nucleares/antagonistas & inibidores
Proteínas Nucleares/química
Proteínas Nucleares/genética
Mutação Puntual
Isoformas de Proteínas/química
Isoformas de Proteínas/genética
Isoformas de Proteínas/metabolismo
Estabilidade Proteica
Subunidades Proteicas/química
Subunidades Proteicas/genética
Subunidades Proteicas/metabolismo
Interferência de RNA
Proteínas Recombinantes de Fusão/química
Proteínas Recombinantes de Fusão/metabolismo
Proteínas Recombinantes/química
Proteínas Recombinantes/metabolismo
Células Sf9
Spodoptera
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Histones); 0 (Isoenzymes); 0 (KANSL3 protein, human); 0 (Nuclear Proteins); 0 (Protein Isoforms); 0 (Protein Subunits); 0 (Recombinant Fusion Proteins); 0 (Recombinant Proteins); EC 2.3.1.48 (Histone Acetyltransferases); EC 2.4.1.- (N-Acetylglucosaminyltransferases); EC 2.4.1.- (UDP-N-acetylglucosamine-peptide beta-N-acetylglucosaminyltransferase)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171228
[Lr] Data última revisão:
171228
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170429
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.781401



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