Base de dados : MEDLINE
Pesquisa : G06.920.925.950 [Categoria DeCS]
Referências encontradas : 5124 [refinar]
Mostrando: 1 .. 10   no formato [Detalhado]

página 1 de 513 ir para página                         

  1 / 5124 MEDLINE  
              next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28456575
[Au] Autor:Grzesik P; MacMath D; Henson B; Prasad S; Joshi P; Desai PJ
[Ad] Endereço:Department of Oncology, The Sidney Kimmel Comprehensive Cancer Center at Johns Hopkins, The Johns Hopkins University, Baltimore, MD, USA.
[Ti] Título:Incorporation of the Kaposi's sarcoma-associated herpesvirus capsid vertex-specific component (CVSC) into self-assembled capsids.
[So] Source:Virus Res;236:9-13, 2017 05 15.
[Is] ISSN:1872-7492
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Self-assembly of herpesvirus capsids can be accomplished in heterologous expression systems provided all six capsid proteins are present. We have demonstrated the assembly of icosahedral Kaposi's sarcoma-associated herpesvirus (KSHV) capsids in insect cells using the baculovirus expression system. Using this self-assembly system we investigated whether we could add additional capsid associated proteins and determine their incorporation into the assembled capsid. We chose the capsid vertex-specific component (CVSC) proteins encoded by open reading frames (ORFs) 19 and 32 to test this. This complex sits on the capsid vertex and is important for capsid maturation in herpesvirus-infected cells. Co-immunoprecipitation assays were used to initially confirm a bi-molecular interaction between ORF19 and ORF32. Both proteins also precipitated the triplex proteins of the capsid shell (ORF26 and ORF62) as well as the major capsid protein (ORF25). Capsid immunoprecipitation assays revealed the incorporation of ORF19 as well as ORF32 into assembled capsids. Similar experiments also showed that the incorporation of each protein occurred independent of the other. These studies reveal biochemically how the KSHV CVSC interacts with the capsid shell.
[Mh] Termos MeSH primário: Capsídeo/metabolismo
Herpesvirus Humano 8/fisiologia
Sarcoma de Kaposi/virologia
Proteínas Virais/metabolismo
Montagem de Vírus
[Mh] Termos MeSH secundário: Proteínas do Capsídeo/genética
Proteínas do Capsídeo/metabolismo
Herpesvirus Humano 8/genética
Seres Humanos
Fases de Leitura Aberta
Proteínas Virais/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Capsid Proteins); 0 (Viral 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


  2 / 5124 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:29302061
[Au] Autor:Noda T; Murakami S; Nakatsu S; Imai H; Muramoto Y; Shindo K; Sagara H; Kawaoka Y
[Ad] Endereço:Division of Virology, Department of Microbiology and Immunology, Institute of Medical Science, University of Tokyo, 4-6-1 Shirokanedai, Minato-ku, Tokyo, 108-8639, Japan. t-noda@infront.kyoto-u.ac.jp.
[Ti] Título:Importance of the 1+7 configuration of ribonucleoprotein complexes for influenza A virus genome packaging.
[So] Source:Nat Commun;9(1):54, 2018 01 04.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The influenza A virus genome is composed of eight single-stranded negative-sense RNAs. Eight distinct viral RNA segments (vRNAs) are selectively packaged into progeny virions, with eight vRNAs in ribonucleoprotein complexes (RNPs) arranged in a specific "1+7" pattern, that is, one central RNP surrounded by seven RNPs. Here we report the genome packaging of an artificially generated seven-segment virus that lacks the hemagglutinin (HA) vRNA. Electron microscopy shows that, even in the presence of only seven vRNAs, the virions efficiently package eight RNPs arranged in the same "1+7" pattern as wild-type virions. Next-generation sequencing reveals that the virions specifically incorporate host-derived 18S and 28S ribosomal RNAs (rRNAs) seemingly as the eighth RNP in place of the HA vRNA. These findings highlight the importance of the assembly of eight RNPs into a specific "1+7" configuration for genome packaging in progeny virions and suggest a potential role for cellular RNAs in viral genome packaging.
[Mh] Termos MeSH primário: Genoma Viral
Vírus da Influenza A/genética
Ribonucleoproteínas/metabolismo
Montagem de Vírus
[Mh] Termos MeSH secundário: Regulação Viral da Expressão Gênica/fisiologia
Células HEK293
Seres Humanos
RNA Viral/genética
Ribonucleoproteínas/química
Ribonucleoproteínas/genética
Proteínas Virais/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (RNA, Viral); 0 (Ribonucleoproteins); 0 (Viral Proteins)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180202
[Lr] Data última revisão:
180202
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180106
[St] Status:MEDLINE
[do] DOI:10.1038/s41467-017-02517-w


  3 / 5124 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:29059239
[Au] Autor:Prasanth KR; Chuang C; Nagy PD
[Ad] Endereço:Department of Plant Pathology, University of Kentucky, Plant Science Building, Lexington, KY, United States of America.
[Ti] Título:Co-opting ATP-generating glycolytic enzyme PGK1 phosphoglycerate kinase facilitates the assembly of viral replicase complexes.
[So] Source:PLoS Pathog;13(10):e1006689, 2017 Oct.
[Is] ISSN:1553-7374
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The intricate interactions between viruses and hosts include exploitation of host cells for viral replication by using many cellular resources, metabolites and energy. Tomato bushy stunt virus (TBSV), similar to other (+)RNA viruses, induces major changes in infected cells that lead to the formation of large replication compartments consisting of aggregated peroxisomal and ER membranes. Yet, it is not known how TBSV obtains the energy to fuel these energy-consuming processes. In the current work, the authors discovered that TBSV co-opts the glycolytic ATP-generating Pgk1 phosphoglycerate kinase to facilitate the assembly of new viral replicase complexes. The recruitment of Pgk1 into the viral replication compartment is through direct interaction with the viral replication proteins. Altogether, we provide evidence that the ATP generated locally within the replication compartment by the co-opted Pgk1 is used to fuel the ATP-requirement of the co-opted heat shock protein 70 (Hsp70) chaperone, which is essential for the assembly of new viral replicase complexes and the activation of functional viral RNA-dependent RNA polymerase. The advantage of direct recruitment of Pgk1 into the virus replication compartment could be that the virus replicase assembly does not need to intensively compete with cellular processes for access to ATP. In addition, local production of ATP within the replication compartment could greatly facilitate the efficiency of Hsp70-driven replicase assembly by providing high ATP concentration within the replication compartment.
[Mh] Termos MeSH primário: Interações Hospedeiro-Patógeno/fisiologia
Fosfoglicerato Quinase/metabolismo
Tombusvirus/crescimento & desenvolvimento
Montagem de Vírus/fisiologia
[Mh] Termos MeSH secundário: RNA Replicase/metabolismo
Saccharomyces cerevisiae
Tabaco/virologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 2.7.2.3 (Phosphoglycerate Kinase); EC 2.7.7.48 (RNA Replicase)
[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:171024
[St] Status:MEDLINE
[do] DOI:10.1371/journal.ppat.1006689


  4 / 5124 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[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


  5 / 5124 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28946005
[Au] Autor:Alam SB; Reade R; Theilmann J; Rochon D
[Ad] Endereço:Faculty of Land and Food Systems, University of British Columbia, Vancouver, B.C., Canada.
[Ti] Título:Evidence for the role of basic amino acids in the coat protein arm region of Cucumber necrosis virus in particle assembly and selective encapsidation of viral RNA.
[So] Source:Virology;512:83-94, 2017 Dec.
[Is] ISSN:1096-0341
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Cucumber necrosis virus (CNV) is a T = 3 icosahedral virus with a (+)ssRNA genome. The N-terminal CNV coat protein arm contains a conserved, highly basic sequence ("KGRKPR"), which we postulate is involved in RNA encapsidation during virion assembly. Seven mutants were constructed by altering the CNV "KGRKPR" sequence; the four basic residues were mutated to alanine individually, in pairs, or in total. Virion accumulation and vRNA encapsidation were significantly reduced in mutants containing two or four substitutions and virion morphology was also affected, where both T = 1 and intermediate-sized particles were produced. Mutants with two or four substitutions encapsidated significantly greater levels of truncated RNA than that of WT, suggesting that basic residues in the "KGRKPR" sequence are important for encapsidation of full-length CNV RNA. Interestingly, "KGRKPR" mutants also encapsidated relatively higher levels of host RNA, suggesting that the "KGRKPR" sequence also contributes to selective encapsidation of CNV RNA.
[Mh] Termos MeSH primário: Aminoácidos Básicos/química
Proteínas do Capsídeo/metabolismo
Vírus de Plantas/metabolismo
RNA Viral/fisiologia
Montagem de Vírus/fisiologia
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Proteínas do Capsídeo/química
Proteínas do Capsídeo/genética
Mutação
Vírus de Plantas/genética
Conformação Proteica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amino Acids, Basic); 0 (Capsid Proteins); 0 (RNA, Viral)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171109
[Lr] Data última revisão:
171109
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170926
[St] Status:MEDLINE


  6 / 5124 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28922356
[Au] Autor:Liu Y; Zou X
[Ad] Endereço:School of Mathematics and Statistics, Wuhan University, Computational Science Hubei Key Laboratory, Wuhan University, Wuhan, China.
[Ti] Título:Mathematical modeling and quantitative analysis of HIV-1 Gag trafficking and polymerization.
[So] Source:PLoS Comput Biol;13(9):e1005733, 2017 Sep.
[Is] ISSN:1553-7358
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Gag, as the major structural protein of HIV-1, is necessary for the assembly of the HIV-1 sphere shell. An in-depth understanding of its trafficking and polymerization is important for gaining further insights into the mechanisms of HIV-1 replication and the design of antiviral drugs. We developed a mathematical model to simulate two biophysical processes, specifically Gag monomer and dimer transport in the cytoplasm and the polymerization of monomers to form a hexamer underneath the plasma membrane. Using experimental data, an optimization approach was utilized to identify the model parameters, and the identifiability and sensitivity of these parameters were then analyzed. Using our model, we analyzed the weight of the pathways involved in the polymerization reactions and concluded that the predominant pathways for the formation of a hexamer might be the polymerization of two monomers to form a dimer, the polymerization of a dimer and a monomer to form a trimer, and the polymerization of two trimers to form a hexamer. We then deduced that the dimer and trimer intermediates might be crucial in hexamer formation. We also explored four theoretical combined methods for Gag suppression, and hypothesized that the N-terminal glycine residue of the MA domain of Gag might be a promising drug target. This work serves as a guide for future theoretical and experimental efforts aiming to understand HIV-1 Gag trafficking and polymerization, and might help accelerate the efficiency of anti-AIDS drug design.
[Mh] Termos MeSH primário: Infecções por HIV/virologia
HIV-1/metabolismo
HIV-1/fisiologia
Produtos do Gene gag do Vírus da Imunodeficiência Humana/química
Produtos do Gene gag do Vírus da Imunodeficiência Humana/metabolismo
[Mh] Termos MeSH secundário: Biologia Computacional
Infecções por HIV/metabolismo
Interações Hospedeiro-Patógeno/fisiologia
Seres Humanos
Modelos Biológicos
Polimerização
Transporte Proteico
Montagem de Vírus
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (gag Gene Products, Human Immunodeficiency Virus)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171018
[Lr] Data última revisão:
171018
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170919
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pcbi.1005733


  7 / 5124 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28911100
[Au] Autor:Lee N; Le Sage V; Nanni AV; Snyder DJ; Cooper VS; Lakdawala SS
[Ad] Endereço:University of Pittsburgh School of Medicine, Department of Microbiology and Molecular Genetics, 450 Technology Drive, Pittsburgh, PA 15219, USA.
[Ti] Título:Genome-wide analysis of influenza viral RNA and nucleoprotein association.
[So] Source:Nucleic Acids Res;45(15):8968-8977, 2017 Sep 06.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Influenza A virus (IAV) genomes are composed of eight single-stranded RNA segments that are coated by viral nucleoprotein (NP) molecules. Classically, the interaction between NP and viral RNA (vRNA) is depicted as a uniform pattern of 'beads on a string'. Using high-throughput sequencing of RNA isolated by crosslinking immunoprecipitation (HITS-CLIP), we identified the vRNA binding profiles of NP for two H1N1 IAV strains in virions. Contrary to the prevailing model for vRNA packaging, NP does not bind vRNA uniformly in the A/WSN/1933 and A/California/07/2009 strains, but instead each vRNA segment exhibits a unique binding profile, containing sites that are enriched or poor in NP association. Intriguingly, both H1N1 strains have similar yet distinct NP binding profiles despite extensive sequence conservation. Peaks identified by HITS-CLIP were verified as true NP binding sites based on insensitivity to DNA antisense oligonucleotide-mediated RNase H digestion. Moreover, nucleotide content analysis of NP peaks revealed that these sites are relatively G-rich and U-poor compared to the genome-wide nucleotide content, indicating an as-yet unidentified sequence bias for NP association in vivo. Taken together, our genome-wide study of NP-vRNA interaction has implications for the understanding of influenza vRNA architecture and genome packaging.
[Mh] Termos MeSH primário: Genoma Viral
Vírus da Influenza A Subtipo H1N1/genética
Nucleoproteínas/química
RNA Viral/química
Proteínas Virais/química
Vírion/genética
[Mh] Termos MeSH secundário: Sequência de Bases
Sítios de Ligação
Sequência Conservada
Expressão Gênica
Sequenciamento de Nucleotídeos em Larga Escala
Vírus da Influenza A Subtipo H1N1/metabolismo
Vírus da Influenza A Subtipo H1N1/ultraestrutura
Modelos Moleculares
Nucleoproteínas/genética
Nucleoproteínas/metabolismo
Oligonucleotídeos Antissenso/química
Ligação Proteica
RNA Viral/genética
RNA Viral/metabolismo
Ribonuclease H/química
Proteínas Virais/genética
Proteínas Virais/metabolismo
Vírion/metabolismo
Vírion/ultraestrutura
Montagem de Vírus/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Nucleoproteins); 0 (Oligonucleotides, Antisense); 0 (RNA, Viral); 0 (Viral Proteins); EC 3.1.26.4 (Ribonuclease H)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170916
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkx584


  8 / 5124 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


  9 / 5124 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28850602
[Au] Autor:Milrot E; Shimoni E; Dadosh T; Rechav K; Unger T; Van Etten JL; Minsky A
[Ad] Endereço:Department of Structural Biology, The Weizmann Institute of Science, Rehovot, Israel.
[Ti] Título:Structural studies demonstrating a bacteriophage-like replication cycle of the eukaryote-infecting Paramecium bursaria chlorella virus-1.
[So] Source:PLoS Pathog;13(8):e1006562, 2017 Aug.
[Is] ISSN:1553-7374
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:A fundamental stage in viral infection is the internalization of viral genomes in host cells. Although extensively studied, the mechanisms and factors responsible for the genome internalization process remain poorly understood. Here we report our observations, derived from diverse imaging methods on genome internalization of the large dsDNA Paramecium bursaria chlorella virus-1 (PBCV-1). Our studies reveal that early infection stages of this eukaryotic-infecting virus occurs by a bacteriophage-like pathway, whereby PBCV-1 generates a hole in the host cell wall and ejects its dsDNA genome in a linear, base-pair-by-base-pair process, through a membrane tunnel generated by the fusion of the virus internal membrane with the host membrane. Furthermore, our results imply that PBCV-1 DNA condensation that occurs shortly after infection probably plays a role in genome internalization, as hypothesized for the infection of some bacteriophages. The subsequent perforation of the host photosynthetic membranes presumably enables trafficking of viral genomes towards host nuclei. Previous studies established that at late infection stages PBCV-1 generates cytoplasmic organelles, termed viral factories, where viral assembly takes place, a feature characteristic of many large dsDNA viruses that infect eukaryotic organisms. PBCV-1 thus appears to combine a bacteriophage-like mechanism during early infection stages with a eukaryotic-like infection pathway in its late replication cycle.
[Mh] Termos MeSH primário: Chlorella/virologia
Infecções por Vírus de DNA
Interações Hospedeiro-Parasita/fisiologia
Phycodnaviridae/fisiologia
Montagem de Vírus/fisiologia
[Mh] Termos MeSH secundário: DNA Viral/fisiologia
Imunofluorescência
Imagem Tridimensional
Microscopia Eletrônica de Transmissão
Phycodnaviridae/ultraestrutura
Reação em Cadeia da Polimerase
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA, Viral)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171002
[Lr] Data última revisão:
171002
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170830
[St] Status:MEDLINE
[do] DOI:10.1371/journal.ppat.1006562


  10 / 5124 MEDLINE  
              first record previous record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28835504
[Au] Autor:Liu X; Liang B; Ngwuta J; Liu X; Surman S; Lingemann M; Kwong PD; Graham BS; Collins PL; Munir S
[Ad] Endereço:RNA Viruses Section, Laboratory of Infectious Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland, USA.
[Ti] Título:Attenuated Human Parainfluenza Virus Type 1 Expressing the Respiratory Syncytial Virus (RSV) Fusion (F) Glycoprotein from an Added Gene: Effects of Prefusion Stabilization and Packaging of RSV F.
[So] Source:J Virol;91(22), 2017 Nov 15.
[Is] ISSN:1098-5514
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Human respiratory syncytial virus (RSV) is the most prevalent worldwide cause of severe respiratory tract infection in infants and young children. Human parainfluenza virus type 1 (HPIV1) also causes severe pediatric respiratory illness, especially croup. Both viruses lack vaccines. Here, we describe the preclinical development of a bivalent RSV/HPIV1 vaccine based on a recombinant HPIV1 vector, attenuated by a stabilized mutation, that expresses RSV F protein modified for increased stability in the prefusion (pre-F) conformation by previously described disulfide bond (DS) and hydrophobic cavity-filling (Cav1) mutations. RSV F was expressed from the first or second gene position as the full-length protein or as a chimeric protein with its transmembrane and cytoplasmic tail (TMCT) domains substituted with those of HPIV1 F in an effort to direct packaging in the vector particles. All constructs were recovered by reverse genetics. The TMCT versions of RSV F were packaged in the rHPIV1 particles much more efficiently than their full-length counterparts. In hamsters, the presence of the RSV F gene, and in particular the TMCT versions, was attenuating and resulted in reduced immunogenicity. However, the vector expressing full-length RSV F from the pre-N position was immunogenic for RSV and HPIV1. It conferred complement-independent high-quality RSV-neutralizing antibodies at titers similar to those of wild-type RSV and provided protection against RSV challenge. The vectors exhibited stable RSV F expression and In conclusion, an attenuated rHPIV1 vector expressing a pre-F-stabilized form of RSV F demonstrated promising immunogenicity and should be further developed as an intranasal pediatric vaccine. RSV and HPIV1 are major viral causes of acute pediatric respiratory illness for which no vaccines or suitable antiviral drugs are available. The RSV F glycoprotein is the major RSV neutralization antigen. We used a rHPIV1 vector, bearing a stabilized attenuating mutation, to express the RSV F glycoprotein bearing amino acid substitutions that increase its stability in the pre-F form, the most immunogenic form that elicits highly functional virus-neutralizing antibodies. RSV F was expressed from the pre-N or N-P gene position of the rHPIV1 vector as a full-length protein or as a chimeric form with its TMCT domain derived from HPIV1 F. TMCT modification greatly increased packaging of RSV F into the vector particles but also increased vector attenuation , resulting in reduced immunogenicity. In contrast, full-length RSV F expressed from the pre-N position was immunogenic, eliciting complement-independent RSV-neutralizing antibodies and providing protection against RSV challenge.
[Mh] Termos MeSH primário: Expressão Gênica
Vetores Genéticos
Vírus da Parainfluenza 1 Humana/fisiologia
Infecções por Vírus Respiratório Sincicial
Vacinas contra Vírus Sincicial Respiratório
Vírus Sinciciais Respiratórios
Proteínas Virais de Fusão
Montagem de Vírus
[Mh] Termos MeSH secundário: Animais
Anticorpos Neutralizantes/imunologia
Anticorpos Antivirais/imunologia
Cercopithecus aethiops
Cobaias
Seres Humanos
Mesocricetus
Proteínas Recombinantes/genética
Proteínas Recombinantes/imunologia
Infecções por Vírus Respiratório Sincicial/genética
Infecções por Vírus Respiratório Sincicial/imunologia
Infecções por Vírus Respiratório Sincicial/prevenção & controle
Vacinas contra Vírus Sincicial Respiratório/genética
Vacinas contra Vírus Sincicial Respiratório/imunologia
Vírus Sinciciais Respiratórios/genética
Vírus Sinciciais Respiratórios/imunologia
Células Vero
Proteínas Virais de Fusão/genética
Proteínas Virais de Fusão/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antibodies, Neutralizing); 0 (Antibodies, Viral); 0 (Recombinant Proteins); 0 (Respiratory Syncytial Virus Vaccines); 0 (Viral Fusion Proteins)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171102
[Lr] Data última revisão:
171102
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170825
[St] Status:MEDLINE



página 1 de 513 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