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[PMID]:28456663
[Au] Autor:Singh S; Anupriya MG; Sreekumar E
[Ad] Endereço:Molecular Virology Laboratory, Rajiv Gandhi Centre for Biotechnology (RGCB), Thycaud P.O., Thiruvananthapuram 695014, Kerala, India.
[Ti] Título:Comparative whole genome analysis of dengue virus serotype-2 strains differing in trans-endothelial cell leakage induction in vitro.
[So] Source:Infect Genet Evol;52:34-43, 2017 Aug.
[Is] ISSN:1567-7257
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:The role of genetic differences among dengue virus (DENV) in causing increased microvascular permeability is less explored. In the present study, we compared two closely related DENV serotype-2 strains of Cosmopolitan genotype for their in vitro infectivity phenotype and ability to induce trans-endothelial leakage. We found that these laboratory strains differed significantly in infecting human microvascular endothelial cells (HMEC-1) and hepatocytes (Huh7), two major target cells of DENV in in vivo infections. There was a reciprocal correlation in infectivity and vascular leakage induced by these strains, with the less infective strain inducing more trans-endothelial cell leakage in HMEC-1 monolayer upon infection. The cells infected with the strain capable of inducing more permeability were found to secrete more Non-Structural protein (sNS1) into the culture supernatant. A whole genome analysis revealed 37 predicted amino acid changes and changes in the secondary structure of 3' non-translated region between the strains. But none of these changes involved the signal sequence coded by the C-terminal of the Envelope protein and the two glycosylation sites within the NS1 protein critical for its secretion, and the N-terminal NS2A sequence important for surface targeting of NS1. The strain that secreted lower levels of NS1 and caused less leakage had two mutations within the NS1 protein coding region, F103S and T146I that significantly changed amino acid properties. A comparison of the sequences of the two strains with published sequences of various DENV strains known to cause clinically severe dengue identified a number of amino acid changes which could be implicated as possible key genetic differences. Our data supports the earlier observations that the vascular leakage induction potential of DENV strains is linked to the sNS1 levels. The results also indicate that viral genetic determinants, especially the mutations within the NS1 coding region, could affect this critical phenotype of DENV strains.
[Mh] Termos MeSH primário: Vírus da Dengue/fisiologia
Células Endoteliais/virologia
Hepatócitos/virologia
Proteínas não Estruturais Virais/genética
[Mh] Termos MeSH secundário: Regiões 3' não Traduzidas
Animais
Permeabilidade Capilar
Linhagem Celular
Vírus da Dengue/genética
Células Endoteliais/citologia
Variação Genética
Genoma Viral
Hepatócitos/citologia
Seres Humanos
Estrutura Secundária de Proteína
Análise de Sequência de RNA
Proteínas não Estruturais Virais/química
Proteínas não Estruturais Virais/secreção
Replicação Viral/fisiologia
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (3' Untranslated Regions); 0 (NS1 protein, Dengue virus type 2); 0 (Viral Nonstructural Proteins)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180309
[Lr] Data última revisão:
180309
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170501
[St] Status:MEDLINE


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[PMID]:28461069
[Au] Autor:Shiryaev SA; Farhy C; Pinto A; Huang CT; Simonetti N; Elong Ngono A; Dewing A; Shresta S; Pinkerton AB; Cieplak P; Strongin AY; Terskikh AV
[Ad] Endereço:Sanford-Burnham-Prebys Medical Discovery Institute, Center for Neuroscience, Aging, and Stem Cell Research, La Jolla, CA 92037, United States.
[Ti] Título:Characterization of the Zika virus two-component NS2B-NS3 protease and structure-assisted identification of allosteric small-molecule antagonists.
[So] Source:Antiviral Res;143:218-229, 2017 07.
[Is] ISSN:1872-9096
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:The recent re-emergence of Zika virus (ZIKV) , a member of the Flaviviridae family, has become a global emergency. Currently, there are no effective methods of preventing or treating ZIKV infection, which causes severe neuroimmunopathology and is particularly harmful to the developing fetuses of infected pregnant women. However, the pathology induced by ZIKV is unique among flaviviruses, and knowledge of the biology of other family members cannot easily be extrapolated to ZIKV. Thus, structure-function studies of ZIKV proteins are urgently needed to facilitate the development of effective preventative and therapeutic agents. Like other flaviviruses, ZIKV expresses an NS2B-NS3 protease, which consists of the NS2B cofactor and the NS3 protease domain and is essential for cleavage of the ZIKV polyprotein precursor and generation of fully functional viral proteins. Here, we report the enzymatic characterization of ZIKV protease, and we identify structural scaffolds for allosteric small-molecule inhibitors of this protease. Molecular modeling of the protease-inhibitor complexes suggests that these compounds bind to the druggable cavity in the NS2B-NS3 protease interface and affect productive interactions of the protease domain with its cofactor. The most potent compound demonstrated efficient inhibition of ZIKV propagation in vitro in human fetal neural progenitor cells and in vivo in SJL mice. The inhibitory scaffolds could be further developed into valuable research reagents and, ultimately, provide a roadmap for the selection of efficient inhibitors of ZIKV infection.
[Mh] Termos MeSH primário: Sítio Alostérico
Inibidores de Proteases/química
Inibidores de Proteases/farmacologia
Proteínas não Estruturais Virais/química
Zika virus/enzimologia
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Antivirais/antagonistas & inibidores
Antivirais/química
Sequência de Bases
Ativação Enzimática
Feminino
Flavivirus/química
Expressão Gênica
Seres Humanos
Concentração Inibidora 50
Camundongos
Modelos Moleculares
Ligação Proteica
Conformação Proteica
Domínios e Motivos de Interação entre Proteínas
RNA Helicases/química
RNA Helicases/efeitos dos fármacos
Fatores de Transcrição SOXB1/genética
Alinhamento de Sequência
Serina Endopeptidases/química
Serina Endopeptidases/efeitos dos fármacos
Células-Tronco
Proteínas não Estruturais Virais/efeitos dos fármacos
Proteínas Virais/química
Proteínas Virais/genética
Zika virus/química
Zika virus/genética
Zika virus/crescimento & desenvolvimento
Infecção pelo Zika virus/virologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Antiviral Agents); 0 (NS2B protein, flavivirus); 0 (NS3 protein, flavivirus); 0 (Protease Inhibitors); 0 (SOX2 protein, human); 0 (SOXB1 Transcription Factors); 0 (Viral Nonstructural Proteins); 0 (Viral Proteins); EC 3.4.21.- (Serine Endopeptidases); EC 3.6.4.13 (RNA Helicases)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:180228
[Lr] Data última revisão:
180228
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170503
[St] Status:MEDLINE


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[PMID]:28951254
[Au] Autor:Palanisamy N; Akaberi D; Lennerstrand J
[Ad] Endereço:Molecular and Cellular Engineering Group, BioQuant, University of Heidelberg, Heidelberg, Germany; The Hartmut Hoffmann-Berling International Graduate School of Molecular and Cellular Biology (HBIGS), University of Heidelberg, Heidelberg, Germany. Electronic address: navaneethan.palanisamy@bioquant.uni-heidelberg.de.
[Ti] Título:Protein backbone flexibility pattern is evolutionarily conserved in the Flaviviridae family: A case of NS3 protease in Flavivirus and Hepacivirus.
[So] Source:Mol Phylogenet Evol;118:58-63, 2018 Jan.
[Is] ISSN:1095-9513
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Viruses belonging to the Flaviviridae family have been an important health concern for humans, animals and birds alike. No specific treatment is available yet for many of the viral infections caused by the members of this family. Lack of specific drugs against these viruses is mainly due to lack of protein structure information. It has been known that protein backbone fluctuation pattern is highly conserved in protein pairs with similar folds, in spite of the lack of sequence similarity. We hypothesized that this concept should also hold true for proteins (especially enzymes) of viruses included in different genera of the Flaviviridae family, as we know that the sequence similarity between them is low. Using available NS3 protease crystal structures of the Flaviviridae family, our preliminary results have shown that the Cα (i.e. backbone) fluctuation patterns are highly similar between Flaviviruses and a Hepacivirus (i.e. hepatitis C virus, HCV). This has to be validated further experimentally.
[Mh] Termos MeSH primário: Evolução Molecular
Flavivirus/enzimologia
Hepacivirus/enzimologia
Proteínas não Estruturais Virais/classificação
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Seres Humanos
Funções Verossimilhança
Filogenia
Estrutura Terciária de Proteína
RNA Helicases/química
RNA Helicases/classificação
RNA Helicases/genética
Alinhamento de Sequência
Serina Endopeptidases/química
Serina Endopeptidases/classificação
Serina Endopeptidases/genética
Proteínas não Estruturais Virais/química
Proteínas não Estruturais Virais/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (NS3 protein, flavivirus); 0 (NS3 protein, hepatitis C virus); 0 (Viral Nonstructural Proteins); EC 3.4.21.- (Serine Endopeptidases); EC 3.6.4.13 (RNA Helicases)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180226
[Lr] Data última revisão:
180226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170928
[St] Status:MEDLINE


  4 / 10047 MEDLINE  
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[PMID]:28456667
[Au] Autor:Chantratita W; Song KS; Nimse SB; Pongthanapisith V; Thongbaiphet N; Wongtabtim G; Pasomsub E; Angkanavin K; Sonawane MD; Warkad SD; Kim T
[Ad] Endereço:Virology Laboratory, Department of Pathology, Faculty of Medicine, Ramathibodi Hospital, Mahidol University, Bangkok 10400, Thailand. Electronic address: wasun.cha@mahidol.ac.th.
[Ti] Título:6 HCV Genotyping 9G test for HCV 1a, 1b, 2, 3, 4 and 6 (6a, 6f, 6i and 6n) with high accuracy.
[So] Source:J Virol Methods;246:95-99, 2017 Aug.
[Is] ISSN:1879-0984
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:According to EASL guidelines and WHO recommendations, the accurate detection of HCV genotypes such as HCV 1a, HCV1b, HCV 2, HCV 3, HCV 4, and HCV 6 (6a, 6f, 6i, 6n) is crucial for the efficient treatment of hepatitis C. HCV Genotyping 9G test allows simultaneous genotyping of HCV 1a, 1b, 2, 3, 4, and 6 (6a, 6f, 6i, and 6n) in clinical samples in 30min. The performance of the test was evaluated by comparison with sequence analysis. Serum samples (n=152) from HCV-infected patients (n=110) and healthy individuals (n=42) were processed under blinded codes. The k coefficient (kappa) values indicated high agreement between the HCV Genotyping 9G test and sequencing. The sensitivity and specificity of the test were 99.1% and 99.7%, respectively. The results indicate that HCV Genotyping 9G test is rapid, reliable, sensitive, and accurate for screening and genotyping of HCV in the clinical specimens.
[Mh] Termos MeSH primário: Técnicas de Genotipagem/métodos
Hepacivirus/genética
[Mh] Termos MeSH secundário: Primers do DNA
Genótipo
Hepacivirus/classificação
Seres Humanos
Cirrose Hepática/virologia
Reação em Cadeia da Polimerase/métodos
Sensibilidade e Especificidade
Análise de Sequência de DNA
Proteínas não Estruturais Virais/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA Primers); 0 (Viral Nonstructural Proteins)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180226
[Lr] Data última revisão:
180226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170501
[St] Status:MEDLINE


  5 / 10047 MEDLINE  
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[PMID]:28467359
[Au] Autor:Yoshida K; Hai H; Tamori A; Teranishi Y; Kozuka R; Motoyama H; Kawamura E; Hagihara A; Uchida-Kobayashi S; Morikawa H; Enomoto M; Murakami Y; Kawada N
[Ad] Endereço:Department of Hepatology, Osaka City University Graduate School of Medicine, Osaka 545-8585, Japan. m2028081@med.osaka-cu.ac.jp.
[Ti] Título:Long-Term Follow-Up of Resistance-Associated Substitutions in Hepatitis C Virus in Patients in Which Direct Acting Antiviral-Based Therapy Failed.
[So] Source:Int J Mol Sci;18(5), 2017 May 03.
[Is] ISSN:1422-0067
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:We evaluated the transition of dominant resistance-associated substitutions (RASs) in hepatitis C virus during long-term follow-up after the failure of DAAs (direct acting antivirals)-based therapy. RASs in non-structure (NS)3/4A, NS5A, NS5B, and deletions in NS5A from 20 patients who failed simeprevir/pegylated-interferon/ribavirin (SMV/PEG-IFN/RBV) and 25 patients who failed daclatasvir/asunaprevir (DCV/ASV) treatment were examined by direct sequencing. With respect to SMV/PEG-IFN/RBV treatment, RAS was detected at D168 in NS3/4A but not detected in NS5A and NS5B at treatment failure in 16 of 20 patients. During the median follow-up period of 64 weeks, the RAS at D168 became less dominant in 9 of 16 patients. Among 25 DCV/ASV failures, RASs at D168, L31, and Y93 were found in 57.1%, 72.2%, and 76.9%, respectively. NS5A deletions were detected in 3 of 10 patients treated previously with SMV/PEG-IFN/RBV. The number of RASs in the breakthrough patients exceeded that in relapsers (mean 3.9 vs. 2.7, < 0.05). RAS at D168 in NS3/4A became less dominant in 6 of 15 patients within 80 weeks. Y93H emerged at the time of relapse, then decreased gradually by 99% at 130 weeks post-treatment. Emerged RASs were associated with the clinical course of treatment and could not be detected during longer follow-up.
[Mh] Termos MeSH primário: Farmacorresistência Viral/genética
Hepacivirus/genética
Hepatite C Crônica/tratamento farmacológico
Serina Proteases/genética
Proteínas não Estruturais Virais/genética
[Mh] Termos MeSH secundário: Adulto
Idoso
Antivirais/farmacologia
Antivirais/uso terapêutico
Quimioterapia Combinada
Feminino
Seguimentos
Hepacivirus/efeitos dos fármacos
Hepatite C Crônica/virologia
Seres Humanos
Imidazóis/farmacologia
Imidazóis/uso terapêutico
Interferon-alfa/uso terapêutico
Isoquinolinas/farmacologia
Isoquinolinas/uso terapêutico
Masculino
Meia-Idade
Polietilenoglicóis/uso terapêutico
Inibidores de Proteases/farmacologia
Inibidores de Proteases/uso terapêutico
Proteínas Recombinantes/uso terapêutico
Ribavirina/farmacologia
Ribavirina/uso terapêutico
Simeprevir/farmacologia
Simeprevir/uso terapêutico
Sulfonamidas/farmacologia
Sulfonamidas/uso terapêutico
Fatores de Tempo
Falha de Tratamento
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antiviral Agents); 0 (BMS-790052); 0 (Imidazoles); 0 (Interferon-alpha); 0 (Isoquinolines); 0 (NS-5 protein, hepatitis C virus); 0 (Protease Inhibitors); 0 (Recombinant Proteins); 0 (Sulfonamides); 0 (Viral Nonstructural Proteins); 30IQX730WE (Polyethylene Glycols); 49717AWG6K (Ribavirin); 9WS5RD66HZ (Simeprevir); EC 3.4.- (NS3-4A serine protease, Hepatitis C virus); EC 3.4.- (Serine Proteases); G8RGG88B68 (peginterferon alfa-2b); S9X0KRJ00S (asunaprevir)
[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:170504
[St] Status:MEDLINE


  6 / 10047 MEDLINE  
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[PMID]:28453108
[Au] Autor:Castro-Orozco R; Castro-García LR; Gómez-Camargo DE
[Ad] Endereço:Universidad de San Buenaventura, Cartagena de Indias, Colombia.
[Ti] Título:[Phylogenetic analysis of South American sequences of the nonstructural protein-1 (ns1) of dengue serotype 2 associated with severe clinical bleeding].
[Ti] Título:Análisis filogenético de secuencias suramericanas del gen ns1 del serotipo dengue-2, relacionadas con sangrado clínico severo..
[So] Source:Rev Salud Publica (Bogota);18(3):459-469, 2016 Jun.
[Is] ISSN:0124-0064
[Cp] País de publicação:Colombia
[La] Idioma:spa
[Ab] Resumo:Objective The objective of this in silico study was to compare nucleotide and amino acids DENV-2-NS1 sequences isolated from febrile patients, with and without disease severity, from different South American countries. Matherials and Methods A bayesian MCMC phylogenetic analysis was carried out using 28 complete sequences of the gene NS1 of the DENV-2 serotype (1 056 bp), using MrBayes v.3.2.0 software, with the model SYM+G (2.5 million generations). We also carried out a phylogenetic analysis with Neighbor-Joining method (Jukes-Cantor model). In addition, the amino acids sequences were aligned and compared with each other, using Clustal W included in MEGA v.5.2 software. Results In the amino acids sequences associated with bleeding, the most frequent substitution was isoleucine → threonine at posicion 93. These sequences showed a high percentage (94.6 %) of amino acid homology in comparison with the percentage of amino acids homology (74 %) of DENV-2 isolates not associated with bleeding. Five clades were identified that group the vast majority of the DENV-2-NS1 sequences analyzed (19/24; 79.2 %) with posterior probability values greater than or equal to 58 %. Seven sequences (87.5 %) associated with bleeding were phylogenetically related within clades 4 and 5, the posterior probability values were 58 % and 97 %, respectively. Conclusion Neither phylogenetic characteristics nor differences between amino acids of the DENV-2-NS1 sequences studied were found that could be associated directly with severity of the disease.
[Mh] Termos MeSH primário: Vírus da Dengue/genética
Hemorragia/virologia
Filogenia
Dengue Grave/virologia
Proteínas não Estruturais Virais/genética
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Sequência de Bases
Teorema de Bayes
Seres Humanos
Sorogrupo
Dengue Grave/complicações
Proteínas não Estruturais Virais/classificação
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (NS1 protein, Dengue virus type 2); 0 (Viral Nonstructural Proteins)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180215
[Lr] Data última revisão:
180215
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170429
[St] Status:MEDLINE


  7 / 10047 MEDLINE  
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[PMID]:28457855
[Au] Autor:Tan CW; Sam IC; Chong WL; Lee VS; Chan YF
[Ad] Endereço:Department of Medical Microbiology, Faculty of Medicine, University of Malaya, 50603 Kuala Lumpur, Malaysia. Electronic address: tancw86@gmail.com.
[Ti] Título:Polysulfonate suramin inhibits Zika virus infection.
[So] Source:Antiviral Res;143:186-194, 2017 07.
[Is] ISSN:1872-9096
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Zika virus (ZIKV) is an arthropod-borne flavivirus that causes newborn microcephaly and Guillian-Barré syndrome in adults. No therapeutics are available to treat ZIKV infection or other flaviviruses. In this study, we explored the inhibitory effect of glycosaminoglycans and analogues against ZIKV infection. Highly sulfated heparin, dextran sulfate and suramin significantly inhibited ZIKV infection in Vero cells. De-sulfated heparin analogues lose inhibitory effect, implying that sulfonate groups are critical for viral inhibition. Suramin, an FDA-approved anti-parasitic drug, inhibits ZIKV infection with 3-5 log PFU viral reduction with IC value of ∼2.5-5 µg/ml (1.93 µM-3.85 µM). A time-of-drug-addition study revealed that suramin remains potent even when administrated at 1-24 hpi. Suramin inhibits ZIKV infection by preventing viral adsorption, entry and replication. Molecular dynamics simulation revealed stronger interaction of suramin with ZIKV NS3 helicase than with the envelope protein. Suramin warrants further investigation as a potential antiviral candidate for ZIKV infection. Heparan sulfate (HS) is a cellular attachment receptor for multiple flaviviruses. However, no direct ZIKV-heparin interaction was observed in heparin-binding analysis, and downregulate or removal of cellular HS with sodium chlorate or heparinase I/III did not inhibit ZIKV infection. This indicates that cell surface HS is not utilized by ZIKV as an attachment receptor.
[Mh] Termos MeSH primário: Suramina/antagonistas & inibidores
Infecção pelo Zika virus/prevenção & controle
Zika virus/efeitos dos fármacos
[Mh] Termos MeSH secundário: Animais
Anticorpos Antivirais
Cercopithecus aethiops
Cloratos/farmacologia
DNA Helicases/metabolismo
Sulfato de Dextrana/antagonistas & inibidores
Flavivirus/efeitos dos fármacos
Glicosaminoglicanos/farmacologia
Heparina/análogos & derivados
Heparina/química
Heparina/farmacologia
Heparitina Sulfato/farmacologia
Concentração Inibidora 50
Camundongos
Simulação de Acoplamento Molecular
Simulação de Dinâmica Molecular
RNA Helicases/química
RNA Helicases/efeitos dos fármacos
Serina Endopeptidases/química
Serina Endopeptidases/efeitos dos fármacos
Suramina/administração & dosagem
Células Vero
Proteínas do Envelope Viral/metabolismo
Proteínas não Estruturais Virais/química
Proteínas não Estruturais Virais/efeitos dos fármacos
Internalização do Vírus/efeitos dos fármacos
Replicação Viral/efeitos dos fármacos
Zika virus/fisiologia
Infecção pelo Zika virus/virologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antibodies, Viral); 0 (Chlorates); 0 (Glycosaminoglycans); 0 (NS3 protein, flavivirus); 0 (Viral Envelope Proteins); 0 (Viral Nonstructural Proteins); 6032D45BEM (Suramin); 9005-49-6 (Heparin); 9042-14-2 (Dextran Sulfate); 9050-30-0 (Heparitin Sulfate); EC 3.4.21.- (Serine Endopeptidases); EC 3.6.4.- (DNA Helicases); EC 3.6.4.13 (RNA Helicases); T95DR77GMR (sodium chlorate)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:180213
[Lr] Data última revisão:
180213
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170502
[St] Status:MEDLINE


  8 / 10047 MEDLINE  
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[PMID]:28454913
[Au] Autor:You SH; Kim T; Choi JH; Park G; Lee KN; Kim B; Lee MH; Kim HS; Kim SM; Park JH
[Ad] Endereço:Foot-and-Mouth Disease Vaccine Research Center, Animal and Plant Quarantine Agency, 177 Hyeoksin 8-ro, Gimcheon-City, Gyeongsangbuk-do, Republic of Korea; Veterinary College of Chungnam National University, 99 Daehak-ro, Yuseong-gu, Daejeon, Republic of Korea.
[Ti] Título:Coinjection of a vaccine and anti-viral agents can provide fast-acting protection from foot-and-mouth disease.
[So] Source:Antiviral Res;143:195-204, 2017 07.
[Is] ISSN:1872-9096
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Foot-and-mouth disease (FMD) is the cause of an economically devastating animal disease. With commercial inactivated FMD vaccines, the protection against FMD virus (FMDV) begins a minimum of 4 days post vaccination (dpv). Therefore, antiviral agents could be proposed for rapid protection and to reduce the spread of FMDV during outbreaks until vaccine-induced protective immunity occurs. In previous studies, we have developed two recombinant adenoviruses that simultaneously express porcine interferon-α and interferon-γ (Ad-porcine IFN-αγ) and multiple siRNAs that target the non-structural protein-regions of FMDV (Ad-3siRNA), and we have shown that the combination of the two antiviral agents (referred to here as Ad combination) induced robust protection against FMDV in pigs. In an attempt to provide complete protection against FMDV, we co-administered Ad combination and the FMD vaccine to mice and pigs. In the C57BL/6 mice model, we observed rapid and continuous protection against homologous FMDV challenge from 1 to 3 dpv-the period in which vaccine-mediated immunity is absent. In the pig experiments, we found that most of the pigs (five out of six) that received vaccine + Ad combination and were challenged with FMDV at 1 or 2 dpv were clinically protected from FMDV. In addition, most of the pigs that received vaccine + Ad combination and all pigs inoculated with the vaccine only were clinically protected from an FMDV challenge at 7 dpv. We believe that the antiviral agent ensures early protection from FMDV, and the vaccine participates in protection after 7 dpv. Therefore, we can say that the combination of the FMD vaccine and effective antiviral agents may offer both fast-acting and continuous protection against FMDV. In further studies, we plan to design coadministration of Ad combination and novel vaccines.
[Mh] Termos MeSH primário: Antivirais/farmacologia
Vírus da Febre Aftosa/efeitos dos fármacos
Febre Aftosa/prevenção & controle
Vacinação
Vacinas Virais/farmacologia
[Mh] Termos MeSH secundário: Adenoviridae/genética
Animais
Anticorpos Neutralizantes
Anticorpos Antivirais/imunologia
Antivirais/administração & dosagem
Citocinas/sangue
Combinação de Medicamentos
Vírus da Febre Aftosa/patogenicidade
Células HEK293
Seres Humanos
Injeções Intramusculares
Interferon-alfa/farmacologia
Interferon gama/farmacologia
Camundongos
Camundongos Endogâmicos C57BL
RNA Interferente Pequeno/farmacologia
Recombinação Genética
Taxa de Sobrevida
Suínos
Vacinas de Produtos Inativados/farmacologia
Proteínas não Estruturais Virais/imunologia
Vacinas Virais/administração & dosagem
Vacinas Virais/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antibodies, Neutralizing); 0 (Antibodies, Viral); 0 (Antiviral Agents); 0 (Cytokines); 0 (Drug Combinations); 0 (Interferon-alpha); 0 (RNA, Small Interfering); 0 (Vaccines, Inactivated); 0 (Viral Nonstructural Proteins); 0 (Viral Vaccines); 82115-62-6 (Interferon-gamma)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:180213
[Lr] Data última revisão:
180213
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170430
[St] Status:MEDLINE


  9 / 10047 MEDLINE  
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[PMID]:29323842
[Au] Autor:Kuznetsova TV; Smimova MS; Leonovich OA; Gordeichuk IV; Biriukova IK; Zylkova MV; Tyn'o YY; Belyakova AV; Shevelev AB
[Ti] Título:A new method of producing NS5A antigen of hepatitis C virus.
[So] Source:Vopr Virusol;62(1):17-25, 2017.
[Is] ISSN:0507-4088
[Cp] País de publicação:Russia (Federation)
[La] Idioma:eng
[Ab] Resumo:A task of creating a universal platform for engineering affordable recombinant producers of viral proteins conserving immunogenicity has not been solved yet. High toxicity of the viral proteins for the host cells, low yield and abnormal folding of the products often present severe obstacles to obtaining producers of the viral proteins. In this work, we report a new method of engineering and screening of deletion libraries from the viral antigen genes. This method allows selection of artificial derivatives of these genes adapted for expression in microbial producer cells. The method involves PCR amplification of the gene fragments using a system of randomized and adapter primers, which allows the spontaneous formation of duplexes from the random primers in the absence of the template DNA to be prevented. For selecting variants capable of in vivo expression, the obtained PCR products are cloned to a special vector of a direct phenotypical selection pQL30. It contains E. coli ß-galactosidase gene with an inserted polylinker producing a frame-shift mutation. Using this screening method, an artificial variant of hepatitis C (HCV) NS5a gene with optimal biotechnological properties was established. 27 clinical specimens of 1670 bp long HCV1b NS5a fragments were used as a source gene. A PCR bank of the deletion derivatives was produced. 40 LacZ-positive clones based on pQL30 vector with a 50-700 bp long insertion were selected. The LacZ activity of the cell lysates and the immunogenicity of the products were tested. As a result, a single clone encoding a soluble protein with Mr = 114 kDa was selected. Its yield reached 0.3% of the total cell protein. It was highly reactive with sera of HCV 1b infected patients but not with sera of the healthy donors.
[Mh] Termos MeSH primário: Antígenos Virais/genética
Escherichia coli/genética
Hepacivirus/genética
Hepatite C/diagnóstico
Engenharia de Proteínas/métodos
Proteínas Recombinantes/genética
Proteínas não Estruturais Virais/genética
[Mh] Termos MeSH secundário: Antígenos Virais/biossíntese
Antígenos Virais/imunologia
Antígenos Virais/isolamento & purificação
Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Primers do DNA/síntese química
Primers do DNA/genética
Escherichia coli/metabolismo
Mutação da Fase de Leitura
Biblioteca Gênica
Vetores Genéticos/química
Vetores Genéticos/metabolismo
Hepacivirus/imunologia
Hepatite C/imunologia
Hepatite C/virologia
Seres Humanos
Soros Imunes/química
Óperon Lac
Proteínas Recombinantes/biossíntese
Proteínas Recombinantes/imunologia
Proteínas Recombinantes/isolamento & purificação
Proteínas não Estruturais Virais/biossíntese
Proteínas não Estruturais Virais/imunologia
Proteínas não Estruturais Virais/isolamento & purificação
beta-Galactosidase/genética
beta-Galactosidase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antigens, Viral); 0 (Bacterial Proteins); 0 (DNA Primers); 0 (Immune Sera); 0 (NS-5 protein, hepatitis C virus); 0 (Recombinant Proteins); 0 (Viral Nonstructural Proteins); EC 3.2.1.23 (beta-Galactosidase)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180208
[Lr] Data última revisão:
180208
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180112
[St] Status:MEDLINE


  10 / 10047 MEDLINE  
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Texto completo
[PMID]:29037477
[Au] Autor:Bhatt M; Mohapatra JK; Pandey LK; Mohanty NN; Das B; Prusty BR; Pattnaik B
[Ad] Endereço:ICAR-Directorate of Foot and Mouth Disease, Mukteswar 263 138, Uttarakhand, India.
[Ti] Título:Mutational analysis of foot and mouth disease virus nonstructural polyprotein 3AB-coding region to design a negative marker virus.
[So] Source:Virus Res;243:36-43, 2018 01 02.
[Is] ISSN:1872-7492
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Inactivated purified whole virus vaccines are used for control of foot and mouth disease (FMD). ELISAs detecting antibodies to the nonstructural proteins (NSP), a marker of infection, are primarily used to differentiate FMD virus (FMDV) infected from vaccinated animals (DIVA). However, such DIVA assays have a limitation to their specificity since residual NSPs present in the relatively impure vaccines are suspected to induce an NSP-antibody response in the repeatedly vaccinated animals. Epitope-deleted negative marker vaccine strategy seems to have an advantage over the conventional vaccines in identifying the infected animals with accuracy. NSP 3AB contains an abundance of immunodominant B-cell epitopes of diagnostic importance. This study addresses the feasibility of producing 3AB-truncated FMDV mutant as a potential negative marker vaccine candidate. An infectious cDNA clone of FMDV serotype Asia 1 strain was used to engineer an array of deletion mutations in the established antigenic domain of 3AB. The maximum length of deletion tolerated by the virus was found to be restricted to amino acid residues 87-144 in the C-terminal half of 3A protein along with deletion of the first two copies of 3B peptide. The 3AB-truncated marker virus (Asia 1 IND 491/1997Δ3A 3B +FLAG) demonstrated infectivity titres comparable to that of the parental virus in BHK-21 (log 7.42 TCID /ml) and LFBK-α ß (log 8.30 TCID /ml) cell monolayer culture. The protein fragment corresponding to the viable deletion in the 3AB region was expressed in a prokaryotic system to standardize a companion assay (3A 3B I-ELISA) for the negative marker virus which showed reasonably high diagnostic sensitivity (96.9%) and specificity (100% for naïve and 97.1% for uninfected vaccinated samples). The marker virus and its companion ELISA designed in this study provide a basis to devise a marker vaccine strategy for FMD control.
[Mh] Termos MeSH primário: Vírus da Febre Aftosa/genética
Febre Aftosa/virologia
Poliproteínas/genética
Proteínas não Estruturais Virais/genética
Proteínas Virais/imunologia
[Mh] Termos MeSH secundário: Animais
Anticorpos Antivirais/imunologia
Análise Mutacional de DNA
Epitopos de Linfócito B/genética
Epitopos de Linfócito B/imunologia
Febre Aftosa/imunologia
Febre Aftosa/prevenção & controle
Vírus da Febre Aftosa/imunologia
Poliproteínas/imunologia
Proteínas não Estruturais Virais/imunologia
Proteínas Virais/genética
Vacinas Virais/genética
Vacinas Virais/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antibodies, Viral); 0 (Epitopes, B-Lymphocyte); 0 (Polyproteins); 0 (Viral Nonstructural Proteins); 0 (Viral Proteins); 0 (Viral Vaccines)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180209
[Lr] Data última revisão:
180209
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171018
[St] Status:MEDLINE



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