Base de dados : MEDLINE
Pesquisa : D25.479.900 [Categoria DeCS]
Referências encontradas : 388 [refinar]
Mostrando: 1 .. 10   no formato [Detalhado]

página 1 de 39 ir para página                         

  1 / 388 MEDLINE  
              next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[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


  2 / 388 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28866835
[Au] Autor:Zheng L; Wang W; Liu J; Huo Y; Qin C; Wang M; Shen S
[Ad] Endereço:The Sixth People's Hospital of Zhengzhou, No. 29 Jingguangnan Road, Zhengzhou, 450000, People's Republic of China.
[Ti] Título:Comprehensive characterization of a major capsid protein derived from a documented GII.6 norovirus strain.
[So] Source:Arch Virol;162(12):3863-3868, 2017 Dec.
[Is] ISSN:1432-8798
[Cp] País de publicação:Austria
[La] Idioma:eng
[Ab] Resumo:In this study, we successfully produced VLPs derived from full-length or chimeric VP1 of a documented GII.6 strain. Trypsin digestion of purified VLPs led to total cleavage of VP1, while the integrity of assembled VLPs was not affected. In vitro VLP-histo-blood group antigen (HBGA) binding and binding blockade assays indicated that trypsin digestion enhanced the binding of GII.6 VLPs to salivary HBGAs and that this binding could only be blocked by serum produced against a homologous strain. The data regarding the assembly, morphology and binding patterns of GII.6 NoV VLPs presented here might be useful for further study of GII.6 NoVs.
[Mh] Termos MeSH primário: Proteínas do Capsídeo/genética
Norovirus/genética
Virossomos/genética
Virossomos/metabolismo
[Mh] Termos MeSH secundário: Antígenos de Grupos Sanguíneos/metabolismo
Seres Humanos
Multimerização Proteica
Virossomos/ultraestrutura
Montagem de Vírus
Ligação Viral
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Blood Group Antigens); 0 (Capsid Proteins); 0 (Virosomes)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171113
[Lr] Data última revisão:
171113
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170904
[St] Status:MEDLINE
[do] DOI:10.1007/s00705-017-3537-4


  3 / 388 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28843813
[Au] Autor:Heinimäki S; Tamminen K; Malm M; Vesikari T; Blazevic V
[Ad] Endereço:Vaccine Research Center, University of Tampere, Finland. Electronic address: suvi.heinimaki@uta.fi.
[Ti] Título:Live baculovirus acts as a strong B and T cell adjuvant for monomeric and oligomeric protein antigens.
[So] Source:Virology;511:114-122, 2017 Nov.
[Is] ISSN:1096-0341
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Recombinant proteins produced by baculovirus (BV) expression systems contain residual BV after crude purification. We studied adjuvant effect of BV on antibody and T cell responses against two model antigens, monomeric ovalbumin (OVA) protein and oligomeric norovirus (NoV) virus-like particles (VLPs). BALB/c mice were immunized intradermally with OVA alone or OVA formulated with live or inactivated BV, and VLP formulations comprised of chromatographically purified NoV GII.4 VLPs alone or mixed with BV, or of crude purified VLPs containing BV impurities from expression system. Live BV improved immunogenicity of NoV VLPs, sparing VLP dose up to 10-fold. Moreover, soluble OVA protein induced IgG2a antibodies and T cell response only when co-administered with live BV. BV adjuvant effect was completely abrogated by removal or inactivation of BV. These findings support the usage of crude purified proteins containing residual BV as vaccine antigens.
[Mh] Termos MeSH primário: Adjuvantes Imunológicos/metabolismo
Linfócitos B/imunologia
Baculoviridae/metabolismo
Norovirus/imunologia
Ovalbumina/imunologia
Linfócitos T/imunologia
Virossomos/imunologia
[Mh] Termos MeSH secundário: Animais
Injeções Intradérmicas
Camundongos Endogâmicos BALB C
Ovalbumina/administração & dosagem
Virossomos/administração & dosagem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adjuvants, Immunologic); 0 (Virosomes); 9006-59-1 (Ovalbumin)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171010
[Lr] Data última revisão:
171010
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170828
[St] Status:MEDLINE


  4 / 388 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28750325
[Au] Autor:Subramanian S; Organtini LJ; Grossman A; Domeier PP; Cifuente JO; Makhov AM; Conway JF; D'Abramo A; Cotmore SF; Tattersall P; Hafenstein S
[Ad] Endereço:Department of Medicine, Pennsylvania State University College of Medicine, 500 University Drive, Hershey, PA 17033, USA.
[Ti] Título:Cryo-EM maps reveal five-fold channel structures and their modification by gatekeeper mutations in the parvovirus minute virus of mice (MVM) capsid.
[So] Source:Virology;510:216-223, 2017 Oct.
[Is] ISSN:1096-0341
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In minute virus of mice (MVM) capsids, icosahedral five-fold channels serve as portals mediating genome packaging, genome release, and the phased extrusion of viral peptides. Previous studies suggest that residues L172 and V40 are essential for channel function. The structures of MVMi wildtype, and mutant L172T and V40A virus-like particles (VLPs) were solved from cryo-EM data. Two constriction points, termed the mid-gate and inner-gate, were observed in the channels of wildtype particles, involving residues L172 and V40 respectively. While the mid-gate of V40A VLPs appeared normal, in L172T adjacent channel walls were altered, and in both mutants there was major disruption of the inner-gate, demonstrating that direct L172:V40 bonding is essential for its structural integrity. In wildtype particles, residues from the N-termini of VP2 map into claw-like densities positioned below the channel opening, which become disordered in the mutants, implicating both L172 and V40 in the organization of VP2 N-termini.
[Mh] Termos MeSH primário: Capsídeo/ultraestrutura
Microscopia Crioeletrônica
Vírus Miúdo do Camundongo/ultraestrutura
[Mh] Termos MeSH secundário: Mutação
Virossomos/ultraestrutura
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Virosomes)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170920
[Lr] Data última revisão:
170920
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170728
[St] Status:MEDLINE


  5 / 388 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28566373
[Au] Autor:Schäfer G; Graham LM; Lang DM; Blumenthal MJ; Bergant Marusic M; Katz AA
[Ad] Endereço:Division of Medical Biochemistry and Structural Biology, Department of Integrative Biomedical Sciences, University of Cape Town, Cape Town, South Africa georgia.schafer@uct.ac.za.
[Ti] Título:Vimentin Modulates Infectious Internalization of Human Papillomavirus 16 Pseudovirions.
[So] Source:J Virol;91(16), 2017 Aug 15.
[Is] ISSN:1098-5514
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Human papillomavirus (HPV) infection is the most common viral infection of the reproductive tract, with virtually all cases of cervical cancer being attributable to infection by oncogenic HPVs. However, the exact mechanism and receptors used by HPV to infect epithelial cells are controversial. The current entry model suggests that HPV initially attaches to heparan sulfate proteoglycans (HSPGs) at the cell surface, followed by conformational changes, cleavage by furin convertase, and subsequent transfer of the virus to an as-yet-unidentified high-affinity receptor. In line with this model, we established an infection system using the HSPG-deficient cell line pgsD677 together with HPV16 pseudovirions (HPV16-PsVs). While pgsD677 cells were nonpermissive for untreated HPV16-PsVs, furin cleavage of the particles led to a substantial increase in infection. Biochemical pulldown assays followed by mass spectrometry analysis showed that furin-precleaved HPV16-PsVs specifically interacted with surface-expressed vimentin on pgsD677 cells. We further demonstrated that both furin-precleaved and uncleaved HPV16-PsVs colocalized with surface-expressed vimentin on pgsD677, HeLa, HaCaT, and NIKS cells, while binding of incoming viral particles to soluble vimentin protein before infection led to a substantial decrease in viral uptake. Interestingly, decreasing cell surface vimentin by small interfering RNA (siRNA) knockdown in HeLa and NIKS cells significantly increased HPV16-PsV infectious internalization, while overexpression of vimentin had the opposite effect. The identification of vimentin as an HPV restriction factor enhances our understanding of the initial steps of HPV-host interaction and may lay the basis for the design of novel antiviral drugs preventing HPV internalization into epithelial cells. Despite HPV being a highly prevalent sexually transmitted virus causing significant disease burden worldwide, particularly cancer of the cervix, cell surface events preceding oncogenic HPV internalization are poorly understood. We herein describe the identification of surface-expressed vimentin as a novel molecule not previously implicated in the infectious internalization of HPV16. Contrary to our expectations, vimentin was found to act not as a receptor but rather as a restriction factor dampening the initial steps of HPV16 infection. These results importantly contribute to our current understanding of the molecular events during the infectious internalization of HPV16 and open a new direction in the development of alternative drugs to prevent HPV infection.
[Mh] Termos MeSH primário: Células Epiteliais/virologia
Interações Hospedeiro-Patógeno
Papillomavirus Humano 16/imunologia
Papillomavirus Humano 16/fisiologia
Vimentina/metabolismo
Virossomos/imunologia
Internalização do Vírus
[Mh] Termos MeSH secundário: Linhagem Celular
Centrifugação
Seres Humanos
Espectrometria de Massas
Mapeamento de Interação de Proteínas
Proteômica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Vimentin); 0 (Virosomes)
[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:170602
[St] Status:MEDLINE


  6 / 388 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28515293
[Au] Autor:Gong D; Dai X; Xiao Y; Du Y; Chapa TJ; Johnson JR; Li X; Krogan NJ; Deng H; Wu TT; Sun R
[Ad] Endereço:Department of Molecular and Medical Pharmacology, University of California-Los Angeles, Los Angeles, California, USA.
[Ti] Título:Virus-Like Vesicles of Kaposi's Sarcoma-Associated Herpesvirus Activate Lytic Replication by Triggering Differentiation Signaling.
[So] Source:J Virol;91(15), 2017 Aug 01.
[Is] ISSN:1098-5514
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Virus-like vesicles (VLVs) are membrane-enclosed vesicles that resemble native enveloped viruses in organization but lack the viral capsid and genome. During the productive infection of tumor-associated gammaherpesviruses, both virions and VLVs are produced and are released into the extracellular space. However, studies of gammaherpesvirus-associated VLVs have been largely restricted by the technical difficulty of separating VLVs from mature virions. Here we report a strategy of selectively isolating VLVs by using a Kaposi's sarcoma-associated herpesvirus (KSHV) mutant that is defective in small capsid protein and is unable to produce mature virions. Using mass spectrometry analysis, we found that VLVs contained viral glycoproteins required for cellular entry, as well as tegument proteins involved in regulating lytic replication, but lacked capsid proteins. Functional analysis showed that VLVs induced the expression of the viral lytic activator RTA, initiating KSHV lytic gene expression. Furthermore, employing RNA sequencing, we performed a genomewide analysis of cellular responses triggered by VLVs and found that PRDM1, a master regulator in cell differentiation, was significantly upregulated. In the context of KSHV replication, we demonstrated that VLV-induced upregulation of PRDM1 was necessary and sufficient to reactivate KSHV by activating its RTA promoter. In sum, our study systematically examined the composition of VLVs and demonstrated their biological roles in manipulating host cell responses and facilitating KSHV lytic replication. Cells lytically infected with tumor-associated herpesviruses produce a high proportion of virus-like vesicles (VLVs). The composition and function of VLVs have not been well defined, largely due to the inability to efficiently isolate VLVs that are free of virions. Using a cell system capable of establishing latent KSHV infection and robust reactivation, we successfully isolated VLVs from a KSHV mutant defective in the small capsid protein. We quantitatively analyzed proteins and microRNAs in VLVs and characterized the roles of VLVs in manipulating host cells and facilitating viral infection. More importantly, we demonstrated that by upregulating PRDM1 expression, VLVs triggered differentiation signaling in targeted cells and facilitated viral lytic infection via activation of the RTA promoter. Our study not only demonstrates a new strategy for isolating VLVs but also shows the important roles of KSHV-associated VLVs in intercellular communication and the viral life cycle.
[Mh] Termos MeSH primário: Regulação Viral da Expressão Gênica
Herpesvirus Humano 8/fisiologia
Interações Hospedeiro-Patógeno
Proteínas Repressoras/biossíntese
Transdução de Sinais
Virossomos/química
Replicação Viral
[Mh] Termos MeSH secundário: Diferenciação Celular
Linhagem Celular
Herpesvirus Humano 8/química
Seres Humanos
Proteínas Imediatamente Precoces/metabolismo
Fator 1 de Ligação ao Domínio I Regulador Positivo
Transativadores/metabolismo
Regulação para Cima
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Immediate-Early Proteins); 0 (Repressor Proteins); 0 (Rta protein, Human herpesvirus 8); 0 (Trans-Activators); 0 (Virosomes); 138415-26-6 (PRDM1 protein, human); EC 2.1.1.- (Positive Regulatory Domain I-Binding Factor 1)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170519
[St] Status:MEDLINE


  7 / 388 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28446665
[Au] Autor:Stano A; Leaman DP; Kim AS; Zhang L; Autin L; Ingale J; Gift SK; Truong J; Wyatt RT; Olson AJ; Zwick MB
[Ad] Endereço:Department of Immunology and Microbial Science, The Scripps Research Institute, La Jolla, California, USA.
[Ti] Título:Dense Array of Spikes on HIV-1 Virion Particles.
[So] Source:J Virol;91(14), 2017 Jul 15.
[Is] ISSN:1098-5514
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:HIV-1 is rare among viruses for having a low number of envelope glycoprotein (Env) spikes per virion, i.e., ∼7 to 14. This exceptional feature has been associated with avoidance of humoral immunity, i.e., B cell activation and antibody neutralization. Virus-like particles (VLPs) with increased density of Env are being pursued for vaccine development; however, these typically require protein engineering that alters Env structure. Here, we used instead a strategy that targets the producer cell. We employed fluorescence-activated cell sorting (FACS) to sort for cells that are recognized by trimer cross-reactive broadly neutralizing antibody (bnAb) and not by nonneutralizing antibodies. Following multiple iterations of FACS, cells and progeny virions were shown to display higher levels of antigenically correct Env in a manner that correlated between cells and cognate virions ( = 0.027). High-Env VLPs, or hVLPs, were shown to be monodisperse and to display more than a 10-fold increase in spikes per particle by electron microscopy (average, 127 spikes; range, 90 to 214 spikes). Sequencing revealed a partial truncation in the C-terminal tail of Env that had emerged in the sort; however, iterative rounds of "cell factory" selection were required for the high-Env phenotype. hVLPs showed greater infectivity than standard pseudovirions but largely similar neutralization sensitivity. Importantly, hVLPs also showed superior activation of Env-specific B cells. Hence, high-Env HIV-1 virions, obtained through selection of producer cells, represent an adaptable platform for vaccine design and should aid in the study of native Env. The paucity of spikes on HIV is a unique feature that has been associated with evasion of the immune system, while increasing spike density has been a goal of vaccine design. Increasing the density of Env by modifying it in various ways has met with limited success. Here, we focused instead on the producer cell. Cells that stably express HIV spikes were screened on the basis of high binding by bnAbs and low binding by nonneutralizing antibodies. Levels of spikes on cells correlated well with those on progeny virions. Importantly, high-Env virus-like particles (hVLPs) were produced with a manifest array of well-defined spikes, and these were shown to be superior in activating desirable B cells. Our study describes HIV particles that are densely coated with functional spikes, which should facilitate the study of HIV spikes and their development as immunogens.
[Mh] Termos MeSH primário: HIV-1/ultraestrutura
Vírion/ultraestrutura
Virossomos/ultraestrutura
Produtos do Gene env do Vírus da Imunodeficiência Humana/metabolismo
[Mh] Termos MeSH secundário: Linfócitos B/imunologia
Células Cultivadas
HIV-1/crescimento & desenvolvimento
HIV-1/imunologia
Seres Humanos
Microscopia Eletrônica de Transmissão
Testes de Neutralização
Virossomos/imunologia
Virossomos/metabolismo
Produtos do Gene env do Vírus da Imunodeficiência Humana/genética
Produtos do Gene env do Vírus da Imunodeficiência Humana/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Virosomes); 0 (env Gene Products, Human Immunodeficiency Virus)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170718
[Lr] Data última revisão:
170718
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170428
[St] Status:MEDLINE


  8 / 388 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28423032
[Au] Autor:Hashimoto Y; Macri D; Srivastava I; McPherson C; Felberbaum R; Post P; Cox M
[Ad] Endereço:Protein Sciences Corporation, Meriden, Connecticut, Unites States of America.
[Ti] Título:Complete study demonstrating the absence of rhabdovirus in a distinct Sf9 cell line.
[So] Source:PLoS One;12(4):e0175633, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:A putative novel rhabdovirus (SfRV) was previously identified in a Spodoptera frugiperda cell line (Sf9 cells [ATCC CRL-1711 lot 58078522]) by next generation sequencing and extensive bioinformatic analysis. We performed an extensive analysis of our Sf9 cell bank (ATCC CRL-1711 lot 5814 [Sf9L5814]) to determine whether this virus was already present in cells obtained from ATCC in 1987. Inverse PCR of DNA isolated from Sf9 L5814 cellular DNA revealed integration of SfRV sequences in the cellular genome. RT-PCR of total RNA showed a deletion of 320 nucleotides in the SfRV RNA that includes the transcriptional motifs for genes X and L. Concentrated cell culture supernatant was analyzed by sucrose density gradient centrifugation and revealed a single band at a density of 1.14 g/ml. This fraction was further analysed by electron microscopy and showed amorphous and particulate debris that did not resemble a rhabdovirus in morphology or size. SDS-PAGE analysis confirmed that the protein composition did not contain the typical five rhabdovirus structural proteins and LC-MS/MS analysis revealed primarily of exosomal marker proteins, the SfRV N protein, and truncated forms of SfRV N, P, and G proteins. The SfRV L gene fragment RNA sequence was recovered from the supernatant after ultracentrifugation of the 1.14 g/ml fraction treated with diethyl ether suggesting that the SfRV L gene fragment sequence is not associated with a diethyl ether resistant nucleocapsid. Interestingly, the 1.14 g/ml fraction was able to transfer baculovirus DNA into Sf9L5814 cells, consistent with the presence of functional exosomes. Our results demonstrate the absence of viral particles in ATCC CRL-1711 lot 5814 Sf9 cells in contrast to a previous study that suggested the presence of infectious rhabdoviral particles in Sf9 cells from a different lot. This study highlights how cell lines with different lineages may present different virosomes and therefore no general conclusions can be drawn across Sf9 cells from different laboratories.
[Mh] Termos MeSH primário: Genoma Viral
RNA Viral/genética
Rhabdoviridae/genética
Células Sf9/virologia
Virossomos/genética
[Mh] Termos MeSH secundário: Animais
Baculoviridae/genética
Baculoviridae/ultraestrutura
Centrifugação com Gradiente de Concentração
DNA/genética
DNA/isolamento & purificação
Eletroforese em Gel de Poliacrilamida
Sequenciamento de Nucleotídeos em Larga Escala
RNA Viral/isolamento & purificação
Rhabdoviridae/ultraestrutura
Spodoptera
Vírion/genética
Vírion/ultraestrutura
Virossomos/isolamento & purificação
Virossomos/ultraestrutura
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (RNA, Viral); 0 (Virosomes); 9007-49-2 (DNA)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170505
[Lr] Data última revisão:
170505
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170420
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0175633


  9 / 388 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28219831
[Au] Autor:Huo Y; Zheng L; Chen X; Ge L; Wang Y
[Ad] Endereço:The Sixth People's Hospital of Zhengzhou, Zhengzhou, PR China. Electronic address: 1246105971@qq.com.
[Ti] Título:Expression and characterization of the major capsid protein derived from a GII.6 norovirus strain isolated in China.
[So] Source:Microb Pathog;105:131-137, 2017 Apr.
[Is] ISSN:1096-1208
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The objective of this study was to express and characterize the major capsid protein (VP1) of a GII.6 Norovirus (NoV)strain isolated in China. The newly identified GII.6 NoV strain was isolated from a five-year old boy presenting acute gastroenteritis. The genome of the GII.6 strain was 7550 nucleotides in length, excluding the poly-adenylation tail. Multiple sequence alignment and phylogenetic analysis based on deduced VP1 amino acid sequences from different genotypes indicated close relationship between GII.3 and GII.6 NoVs, as demonstrated by the presence of a short sequence insertion in the P2 domain and clustering in the same subgroup. Expression of GII.6 VP1 led to assembly of virus like particles (VLPs). In vitro VLP-salivary histo-blood group antigens (HBGAs) binding assay demonstrated wide-spectrum binding activities of assembled VLPs to blood type A, B, AB and O salivary HBGAs with highest binding capacity to type A salivary HBGAs and lowest to type AB and O salivary HBGAs. In vitro VLP-salivary HBGAs binding blockade assay indicated absence of cross-blocking effects for hyperimmune sera produced against different genotypes. In conclusion, our results suggest a rational VLPs-based multivalent NoV vaccine should contain capsid proteins of a GII.6 strain.
[Mh] Termos MeSH primário: Infecções por Caliciviridae/virologia
Proteínas do Capsídeo/genética
Genótipo
Norovirus/genética
Norovirus/isolamento & purificação
[Mh] Termos MeSH secundário: Antígenos de Grupos Sanguíneos/metabolismo
Proteínas do Capsídeo/metabolismo
Pré-Escolar
China
Clonagem Molecular
Gastroenterite/virologia
Expressão Gênica
Genoma Viral
Seres Humanos
Masculino
Norovirus/classificação
Filogenia
Ligação Proteica
Multimerização Proteica
Análise de Sequência de DNA
Homologia de Sequência
Virossomos/metabolismo
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Blood Group Antigens); 0 (Capsid Proteins); 0 (Virosomes)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170417
[Lr] Data última revisão:
170417
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170222
[St] Status:MEDLINE


  10 / 388 MEDLINE  
              first record previous record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28214610
[Au] Autor:Blom RAM; Amacker M; Moser C; van Dijk RM; Bonetti R; Seydoux E; Hall SRR; von Garnier C; Blank F
[Ad] Endereço:Department of Pulmonary Medicine, Bern University Hospital, University of Bern, Bern, Switzerland; Graduate School for Cellular and Biomedical Sciences, University of Bern, Bern, Switzerland.
[Ti] Título:Virosome-bound antigen enhances DC-dependent specific CD4 T cell stimulation, inducing a Th1 and Treg profile in vitro.
[So] Source:Nanomedicine;13(5):1725-1737, 2017 Jul.
[Is] ISSN:1549-9642
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:There is considerable interest to develop antigen-carriers for immune-modulatory clinical applications, but insufficient information is available on their effects on antigen-presenting cells. We employed virosomes coupled to ovalbumin (OVA) to study their interaction with murine bone marrow-derived dendritic cells (BMDCs) and modulation of downstream T cell responses. BMDCs were treated in vitro with virosomes or liposomes prior to determining BMDC phenotype, viability, and intracellular trafficking. Antigen-specific CD4 T cell activation was measured by co-culture of BMDCs with DO11.10 CD4 T cells. Compared to liposomes, virosomes were rapidly taken up. Neither nanocarrier type affected BMDC viability, nor did a moderate degree of activation differ for markers such as CD40, CD80, CD86. Virosome uptake occurred via clathrin-mediated endocytosis and phagocytosis, with co-localization in late endosomes. Only BMDCs treated with OVA-coupled virosomes induced enhanced OVA-specific CD4 T cell proliferation. Antigen-coupled virosomes are endowed with an intrinsic ability to modulate DC-dependent adaptive immune responses.
[Mh] Termos MeSH primário: Linfócitos T CD4-Positivos
Células Dendríticas
Virossomos
[Mh] Termos MeSH secundário: Imunidade Adaptativa
Animais
Antígenos
Camundongos
Camundongos Endogâmicos BALB C
Ovalbumina
Linfócitos T Reguladores
Células Th1
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antigens); 0 (Virosomes); 9006-59-1 (Ovalbumin)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171004
[Lr] Data última revisão:
171004
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170220
[St] Status:MEDLINE



página 1 de 39 ir para página                         
   


Refinar a pesquisa
  Base de dados : MEDLINE Formulário avançado   

    Pesquisar no campo  
1  
2
3
 
           



Search engine: iAH v2.6 powered by WWWISIS

BIREME/OPAS/OMS - Centro Latino-Americano e do Caribe de Informação em Ciências da Saúde