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Pesquisa : D12.776.964.970.880.940 [Categoria DeCS]
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[PMID]:29377916
[Au] Autor:Tutykhina I; Esmagambetov I; Bagaev A; Pichugin A; Lysenko A; Shcherbinin D; Sedova E; Logunov D; Shmarov M; Ataullakhanov R; Naroditsky B; Gintsburg A
[Ad] Endereço:Federal Research Centre of Epidemiology and Microbiology named after Honorary Academician N. F. Gamaleya, Ministry of Health, Moscow, Russia.
[Ti] Título:Vaccination potential of B and T epitope-enriched NP and M2 against Influenza A viruses from different clades and hosts.
[So] Source:PLoS One;13(1):e0191574, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:To avoid outbreaks of influenza virus epidemics and pandemics among human populations, modern medicine requires the development of new universal vaccines that are able to provide protection from a wide range of influenza A virus strains. In the course of development of a universal vaccine, it is necessary to consider that immunity must be generated even against viruses from different hosts because new human epidemic virus strains have their origins in viruses of birds and other animals. We have enriched conserved viral proteins-nucleoprotein (NP) and matrix protein 2 (M2)-by B and T-cell epitopes not only human origin but also swine and avian origin. For this purpose, we analyzed M2 and NP sequences with respect to changes in the sequences of known T and B-cell epitopes and chose conserved and evolutionarily significant epitopes. Eventually, we found consensus sequences of M2 and NP that have the maximum quantity of epitopes that are 100% coincident with them. Consensus epitope-enriched amino acid sequences of M2 and NP proteins were included in a recombinant adenoviral vector. Immunization with Ad5-tet-M2NP induced strong CD8 and CD4 T cells responses, specific to each of the encoded antigens, i.e. M2 and NP. Eight months after immunization with Ad5-tet-M2NP, high numbers of M2- and NP-responding "effector memory" CD44posCD62neg T cells were found in the mouse spleens, which revealed a long-term T cell immune memory conferred by the immunization. In all, the challenge experiments showed an extraordinarily wide-ranging efficacy of protection by the Ad5-tet-M2NP vaccine, covering 5 different heterosubtypes of influenza A virus (2 human, 2 avian and 1 swine).
[Mh] Termos MeSH primário: Linfócitos B/imunologia
Epitopos/imunologia
Vírus da Influenza A/imunologia
Nucleoproteínas/imunologia
Linfócitos T/imunologia
Vacinação
Proteínas da Matriz Viral/imunologia
[Mh] Termos MeSH secundário: Animais
Anticorpos Antivirais/biossíntese
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antibodies, Viral); 0 (Epitopes); 0 (Nucleoproteins); 0 (Viral Matrix 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:180130
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0191574


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[PMID]:29247573
[Au] Autor:Yoshizaki T; Kondo S; Endo K; Nakanishi Y; Aga M; Kobayashi E; Hirai N; Sugimoto H; Hatano M; Ueno T; Ishikawa K; Wakisaka N
[Ad] Endereço:Department of Otolaryngology - Head and Neck Surgery, Graduate School of Medicine, Kanazawa University, Kanazawa, Japan.
[Ti] Título:Modulation of the tumor microenvironment by Epstein-Barr virus latent membrane protein 1 in nasopharyngeal carcinoma.
[So] Source:Cancer Sci;109(2):272-278, 2018 Feb.
[Is] ISSN:1349-7006
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Latent membrane protein 1 (LMP1) is a primary oncogene encoded by the Epstein-Barr virus, and various portions of LMP1 are detected in nasopharyngeal carcinoma (NPC) tumor cells. LMP1 has been extensively studied since the discovery of its transforming property in 1985. LMP1 promotes cancer cell growth during NPC development and facilitates the interaction of cancer cells with surrounding stromal cells for invasion, angiogenesis, and immune modulation. LMP1 is detected in 100% of pre-invasive NPC tumors and in approximately 50% of advanced NPC tumors. Moreover, a small population of LMP1-expressing cells in advanced NPC tumor tissue is proposed to orchestrate NPC tumor tissue maintenance and development through cancer stem cells and progenitor cells. Recent studies suggest that LMP1 activity shifts according to tumor development stage, but it still has a pivotal role during all stages of NPC development.
[Mh] Termos MeSH primário: Carcinoma/patologia
Infecções por Vírus Epstein-Barr/metabolismo
Neoplasias Nasofaríngeas/patologia
Proteínas da Matriz Viral/metabolismo
[Mh] Termos MeSH secundário: Carcinoma/metabolismo
Carcinoma/virologia
Proliferação Celular
Herpesvirus Humano 4/metabolismo
Seres Humanos
Neoplasias Nasofaríngeas/metabolismo
Neoplasias Nasofaríngeas/virologia
Estadiamento de Neoplasias
Células-Tronco Neoplásicas/metabolismo
Microambiente Tumoral
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (EBV-associated membrane antigen, Epstein-Barr virus); 0 (Viral Matrix Proteins)
[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:171217
[St] Status:MEDLINE
[do] DOI:10.1111/cas.13473


  3 / 6472 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


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[PMID]:28993123
[Au] Autor:Duh D; Blazic B
[Ad] Endereço:Department for Medical Microbiology Maribor, Centre for Medical Microbiology, National Laboratory of Health, Environment and Food, Maribor, Slovenia. Electronic address: darja.duh@nlzoh.si.
[Ti] Título:Single mutation in the matrix gene of seasonal influenza A viruses critically affects the performance of diagnostic molecular assay.
[So] Source:J Virol Methods;251:43-45, 2018 Jan.
[Is] ISSN:1879-0984
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Reduced intensity of the fluorescence signal in the amplification curve was observed when using a WHO recommended real time RT-PCR for influenza virus detection. A single mutation, G189T, in the conserved region of influenza virus matrix gene was detected by Sanger sequencing. The mutation is located in the probe binding region, hence we speculated it could be the reason for the atypical shape of amplification curve. The mutation was first noted in Slovenia in 2011 and 2013 for seasonal influenza A virus types A(H1N1)pdm09 and A(H3N2), respectively. In the following years, 2014 and 2015, the majority of influenza A(H3N2) viruses alone carried the mutation. The amplification of matrix gene for these influenza A(H3N2) viruses continuously resulted in the atypically shaped amplification curves. The performance of the particular assay was critically affected; therefore, the assay was no longer usable as diagnostic tool for influenza virus detection. Mutations in the conserved region of influenza virus genome are more common than expected and this would need to be considered when targeting matrix gene.
[Mh] Termos MeSH primário: Vírus da Influenza A/genética
Vírus da Influenza A/isolamento & purificação
Técnicas de Diagnóstico Molecular/métodos
Mutação Puntual
Reação em Cadeia da Polimerase em Tempo Real/métodos
Proteínas da Matriz Viral/genética
[Mh] Termos MeSH secundário: Seres Humanos
Influenza Humana/diagnóstico
Influenza Humana/virologia
Reação em Cadeia da Polimerase Via Transcriptase Reversa/métodos
Sensibilidade e Especificidade
Eslovênia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (M1 protein, Influenza A virus); 0 (Viral Matrix Proteins)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180201
[Lr] Data última revisão:
180201
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171011
[St] Status:MEDLINE


  5 / 6472 MEDLINE  
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[PMID]:29228057
[Au] Autor:Gao X; Lampraki EM; Al-Khalidi S; Qureshi MA; Desai R; Wilson JB
[Ad] Endereço:College of Medical, Veterinary and Life Sciences, University of Glasgow, Glasgow, United Kingdom.
[Ti] Título:N-acetylcysteine (NAC) ameliorates Epstein-Barr virus latent membrane protein 1 induced chronic inflammation.
[So] Source:PLoS One;12(12):e0189167, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Chronic inflammation results when the immune system responds to trauma, injury or infection and the response is not resolved. It can lead to tissue damage and dysfunction and in some cases predispose to cancer. Some viruses (including Epstein-Barr virus (EBV)) can induce inflammation, which may persist even after the infection has been controlled or cleared. The damage caused by inflammation, can itself act to perpetuate the inflammatory response. The latent membrane protein 1 (LMP1) of EBV is a pro-inflammatory factor and in the skin of transgenic mice causes a phenotype of hyperplasia with chronic inflammation of increasing severity, which can progress to pre-malignant and malignant lesions. LMP1 signalling leads to persistent deregulated expression of multiple proteins throughout the mouse life span, including TGFα S100A9 and chitinase-like proteins. Additionally, as the inflammation increases, numerous chemokines and cytokines are produced which promulgate the inflammation. Deposition of IgM, IgG, IgA and IgE and complement activation form part of this process and through genetic deletion of CD40, we show that this contributes to the more tissue-destructive aspects of the phenotype. Treatment of the mice with N-acetylcysteine (NAC), an antioxidant which feeds into the body's natural redox regulatory system through glutathione synthesis, resulted in a significantly reduced leukocyte infiltrate in the inflamed tissue, amelioration of the pathological features and delay in the inflammatory signature measured by in vivo imaging. Reducing the degree of inflammation achieved through NAC treatment, had the knock on effect of reducing leukocyte recruitment to the inflamed site, thereby slowing the progression of the pathology. These data support the idea that NAC could be considered as a treatment to alleviate chronic inflammatory pathologies, including post-viral disease. Additionally, the model described can be used to effectively monitor and accurately measure therapies for chronic inflammation.
[Mh] Termos MeSH primário: Acetilcisteína/farmacologia
Herpesvirus Humano 4/fisiologia
Inflamação/fisiopatologia
Proteínas da Matriz Viral/fisiologia
[Mh] Termos MeSH secundário: Animais
Doença Crônica
Camundongos
Camundongos Transgênicos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (EBV-associated membrane antigen, Epstein-Barr virus); 0 (Viral Matrix Proteins); WYQ7N0BPYC (Acetylcysteine)
[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:171212
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0189167


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[PMID]:28468881
[Au] Autor:Cifuentes-Muñoz N; Sun W; Ray G; Schmitt PT; Webb S; Gibson K; Dutch RE; Schmitt AP
[Ad] Endereço:Department of Molecular and Cellular Biochemistry, University of Kentucky College of Medicine, Lexington, Kentucky, USA.
[Ti] Título:Mutations in the Transmembrane Domain and Cytoplasmic Tail of Hendra Virus Fusion Protein Disrupt Virus-Like-Particle Assembly.
[So] Source:J Virol;91(14), 2017 Jul 15.
[Is] ISSN:1098-5514
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Hendra virus (HeV) is a zoonotic paramyxovirus that causes deadly illness in horses and humans. An intriguing feature of HeV is the utilization of endosomal protease for activation of the viral fusion protein (F). Here we investigated how endosomal F trafficking affects HeV assembly. We found that the HeV matrix (M) and F proteins each induced particle release when they were expressed alone but that their coexpression led to coordinated assembly of virus-like particles (VLPs) that were morphologically and physically distinct from M-only or F-only VLPs. Mutations to the F protein transmembrane domain or cytoplasmic tail that disrupted endocytic trafficking led to failure of F to function with M for VLP assembly. Wild-type F functioned normally for VLP assembly even when its cleavage was prevented with a cathepsin inhibitor, indicating that it is endocytic F trafficking that is important for VLP assembly, not proteolytic F cleavage. Under specific conditions of reduced M expression, we found that M could no longer induce significant VLP release but retained the ability to be incorporated as a passenger into F-driven VLPs, provided that the F protein was competent for endocytic trafficking. The F and M proteins were both found to traffic through Rab11-positive recycling endosomes (REs), suggesting a model in which F and M trafficking pathways converge at REs, enabling these proteins to preassemble before arriving at plasma membrane budding sites. Hendra virus and Nipah virus are zoonotic paramyxoviruses that cause lethal infections in humans. Unlike that for most paramyxoviruses, activation of the henipavirus fusion protein occurs in recycling endosomal compartments. In this study, we demonstrate that the unique endocytic trafficking pathway of Hendra virus F protein is required for proper viral assembly and particle release. These results advance our basic understanding of the henipavirus assembly process and provide a novel model for the interplay between glycoprotein trafficking and paramyxovirus assembly.
[Mh] Termos MeSH primário: Vírus Hendra/genética
Multimerização Proteica
Proteínas Virais de Fusão/genética
Proteínas Virais de Fusão/metabolismo
Virossomos/metabolismo
[Mh] Termos MeSH secundário: Linhagem Celular
Endossomos/metabolismo
Seres Humanos
Proteínas Mutantes/genética
Proteínas Mutantes/metabolismo
Domínios Proteicos
Transporte Proteico
Proteínas da Matriz Viral/metabolismo
Virossomos/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Mutant Proteins); 0 (Viral Fusion Proteins); 0 (Viral Matrix Proteins); 0 (Virosomes)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171226
[Lr] Data última revisão:
171226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170505
[St] Status:MEDLINE


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[PMID]:29028839
[Au] Autor:Ward C; Maselko M; Lupfer C; Prescott M; Pastey MK
[Ad] Endereço:Department of Veterinary Biomedical Sciences, Oregon State University, Corvallis, Oregon, United States of America.
[Ti] Título:Interaction of the Human Respiratory Syncytial Virus matrix protein with cellular adaptor protein complex 3 plays a critical role in trafficking.
[So] Source:PLoS One;12(10):e0184629, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Human Respiratory Syncytial Virus (HRSV) is a leading cause of bronchopneumonia in infants and the elderly. To date, knowledge of viral and host protein interactions within HRSV is limited and are critical areas of research. Here, we show that HRSV Matrix (M) protein interacts with the cellular adaptor protein complex 3 specifically via its medium subunit (AP-3Mu3A). This novel protein-protein interaction was first detected via yeast-two hybrid screen and was further confirmed in a mammalian system by immunofluorescence colocalization and co-immunoprecipitation. This novel interaction is further substantiated by the presence of a known tyrosine-based adaptor protein MU subunit sorting signal sequence, YXXФ: where Ф is a bulky hydrophobic residue, which is conserved across the related RSV M proteins. Analysis of point-mutated HRSV M derivatives indicated that AP-3Mu3A- mediated trafficking is contingent on the presence of the tyrosine residue within the YXXL sorting sequence at amino acids 197-200 of the M protein. AP-3Mu3A is up regulated at 24 hours post-infection in infected cells versus mock-infected HEp2 cells. Together, our data suggests that the AP-3 complex plays a critical role in the trafficking of HRSV proteins specifically matrix in epithelial cells. The results of this study add new insights and targets that may lead to the development of potential antivirals and attenuating mutations suitable for candidate vaccines in the future.
[Mh] Termos MeSH primário: Complexo 3 de Proteínas Adaptadoras/metabolismo
Vírus Sincicial Respiratório Humano/metabolismo
Proteínas da Matriz Viral/metabolismo
[Mh] Termos MeSH secundário: Complexo 3 de Proteínas Adaptadoras/química
Motivos de Aminoácidos
Sequência de Aminoácidos
Sequência Conservada
Células HeLa
Seres Humanos
Ligação Proteica
Estabilidade Proteica
Subunidades Proteicas/química
Subunidades Proteicas/metabolismo
Transporte Proteico
Vírus Sincicial Respiratório Humano/fisiologia
Regulação para Cima
Proteínas da Matriz Viral/química
Montagem de Vírus
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adaptor Protein Complex 3); 0 (Protein Subunits); 0 (Viral Matrix Proteins)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171031
[Lr] Data última revisão:
171031
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171014
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0184629


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[PMID]:28917841
[Au] Autor:Gc JB; Pokhrel R; Bhattarai N; Johnson KA; Gerstman BS; Stahelin RV; Chapagain PP
[Ad] Endereço:Department of Physics, Florida International University, Miami, FL 33199, United States.
[Ti] Título:Graphene-VP40 interactions and potential disruption of the Ebola virus matrix filaments.
[So] Source:Biochem Biophys Res Commun;493(1):176-181, 2017 Nov 04.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Ebola virus infections cause hemorrhagic fever that often results in very high fatality rates. In addition to exploring vaccines, development of drugs is also essential for treating the disease and preventing the spread of the infection. The Ebola virus matrix protein VP40 exists in various conformational and oligomeric forms and is a potential pharmacological target for disrupting the virus life-cycle. Here we explored graphene-VP40 interactions using molecular dynamics simulations and graphene pelleting assays. We found that graphene sheets associate strongly with VP40 at various interfaces. We also found that the graphene is able to disrupt the C-terminal domain (CTD-CTD) interface of VP40 hexamers. This VP40 hexamer-hexamer interface is crucial in forming the Ebola viral matrix and disruption of this interface may provide a method to use graphene or similar nanoparticle based solutions as a disinfectant that can significantly reduce the spread of the disease and prevent an Ebola epidemic.
[Mh] Termos MeSH primário: Grafite/química
Nucleoproteínas/química
Nucleoproteínas/ultraestrutura
Proteínas do Core Viral/química
Proteínas do Core Viral/ultraestrutura
Proteínas da Matriz Viral/química
Proteínas da Matriz Viral/ultraestrutura
[Mh] Termos MeSH secundário: Sítios de Ligação
Simulação de Dinâmica Molecular
Ligação Proteica
Conformação Proteica
Multimerização Proteica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Nucleoproteins); 0 (VP40 protein, virus); 0 (Viral Core Proteins); 0 (Viral Matrix Proteins); 0 (nucleoprotein VP40, Ebola virus); 7782-42-5 (Graphite)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171023
[Lr] Data última revisão:
171023
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170918
[St] Status:MEDLINE


  9 / 6472 MEDLINE  
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[PMID]:28910387
[Au] Autor:Termini JM; Gupta S; Raffa FN; Guirado E; Fischl MA; Niu L; Kanagavelu S; Stone GW
[Ad] Endereço:Department of Microbiology and Immunology, Miami Center for AIDS Research and the Sylvester Comprehensive Cancer Center, University of Miami Miller School of Medicine, Miami, FL, United States of America.
[Ti] Título:Epstein Barr virus Latent Membrane Protein-1 enhances dendritic cell therapy lymph node migration, activation, and IL-12 secretion.
[So] Source:PLoS One;12(9):e0184915, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Dendritic cells (DC) are a promising cell type for cancer vaccines due to their high immunostimulatory capacity. However, improper maturation of DC prior to treatment may account for the limited efficacy of DC vaccine clinical trials. Latent Membrane Protein-1 (LMP1) of Epstein-Barr virus was examined for its ability to mature and activate DC as a gene-based molecular adjuvant for DC vaccines. DC were transduced with an adenovirus 5 vector (Ad5) expressing LMP1 under the control of a Tet-inducible promoter. Ad5-LMP1 was found to mature and activate both human and mouse DC. LMP1 enhanced in vitro migration of DC toward CCL19, as well as in vivo migration of DC to the inguinal lymph nodes of mice following intradermal injection. LMP1-transduced DC increased T cell proliferation in a Pmel-1 adoptive transfer model and enhanced survival in B16-F10 melanoma models. LMP1-DC also enhanced protection in a vaccinia-Gag viral challenge assay. LMP1 induced high levels of IL-12p70 secretion in mouse DC when compared to standard maturation protocols. Importantly, LMP1-transduced human DC retained the capacity to secrete IL-12p70 and TNF in response to DC restimulation. In contrast, DC matured with Monocyte Conditioned Media-Mimic cocktail (Mimic) were impaired in IL-12p70 secretion following restimulation. Overall, LMP1 matured and activated DC, induced migration to the lymph node, and generated high levels of IL-12p70 in a murine model. We propose LMP1 as a promising molecular adjuvant for DC vaccines.
[Mh] Termos MeSH primário: Células Dendríticas/transplante
Herpesvirus Humano 4/metabolismo
Interleucina-12/secreção
Linfonodos/imunologia
Melanoma Experimental/terapia
Proteínas da Matriz Viral/genética
[Mh] Termos MeSH secundário: Animais
Vacinas Anticâncer/imunologia
Movimento Celular
Quimiocina CCL19/metabolismo
Células Dendríticas/citologia
Células Dendríticas/imunologia
Dependovirus/genética
Dependovirus/fisiologia
Feminino
Células HEK293
Seres Humanos
Injeções Intradérmicas
Melanoma Experimental/imunologia
Camundongos
Proteínas da Matriz Viral/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cancer Vaccines); 0 (Chemokine CCL19); 0 (EBV-associated membrane antigen, Epstein-Barr virus); 0 (Viral Matrix Proteins); 187348-17-0 (Interleukin-12)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171012
[Lr] Data última revisão:
171012
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170915
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0184915


  10 / 6472 MEDLINE  
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[PMID]:28893910
[Au] Autor:Williams JK; Shcherbakov AA; Wang J; Hong M
[Ad] Endereço:From the Department of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139 and.
[Ti] Título:Protonation equilibria and pore-opening structure of the dual-histidine influenza B virus M2 transmembrane proton channel from solid-state NMR.
[So] Source:J Biol Chem;292(43):17876-17884, 2017 Oct 27.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The influenza A and B viruses are the primary cause of seasonal flu epidemics. Common to both viruses is the M2 protein, a homotetrameric transmembrane proton channel that acidifies the virion after endocytosis. Although influenza A M2 (AM2) and B M2 (BM2) are functional analogs, they have little sequence homology, except for a conserved H W motif, which is responsible for proton selectivity and channel gating. Importantly, BM2 contains a second titratable histidine, His-27, in the tetrameric transmembrane domain that forms a reverse W H motif with the gating tryptophan. To understand how His-27 affects the proton conduction property of BM2, we have used solid-state NMR to characterize the pH-dependent structure and dynamics of His-27. In cholesterol-containing lipid membranes mimicking the virus envelope, N NMR spectra show that the His-27 tetrad protonates with higher p values than His-19, indicating that the solvent-accessible His-27 facilitates proton conduction of the channel by increasing the proton dissociation rates of His-19. AM2 is inhibited by the amantadine class of antiviral drugs, whereas BM2 has no known inhibitors. We measured the N-terminal interhelical separation of the BM2 channel using fluorinated Phe-5. The interhelical F- F distances show a bimodal distribution of a short distance of 7 Å and a long distance of 15-20 Å, indicating that the phenylene rings do not block small-molecule entry into the channel pore. These results give insights into the lack of amantadine inhibition of BM2 and reveal structural diversities in this family of viral proton channels.
[Mh] Termos MeSH primário: Vírus da Influenza B/química
Canais Iônicos/química
Membranas Artificiais
Proteínas da Matriz Viral/química
[Mh] Termos MeSH secundário: Motivos de Aminoácidos
Vírus da Influenza B/genética
Vírus da Influenza B/metabolismo
Canais Iônicos/genética
Canais Iônicos/metabolismo
Ressonância Magnética Nuclear Biomolecular
Domínios Proteicos
Proteínas da Matriz Viral/genética
Proteínas da Matriz Viral/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Ion Channels); 0 (Membranes, Artificial); 0 (Viral Matrix Proteins)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171104
[Lr] Data última revisão:
171104
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170913
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.813998



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