Base de dados : MEDLINE
Pesquisa : B04.820.455.600.650.750.800 [Categoria DeCS]
Referências encontradas : 78 [refinar]
Mostrando: 1 .. 10   no formato [Detalhado]

página 1 de 8 ir para página                    

  1 / 78 MEDLINE  
              next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28298602
[Au] Autor:Wang D; Phan S; DiStefano DJ; Citron MP; Callahan CL; Indrawati L; Dubey SA; Heidecker GJ; Govindarajan D; Liang X; He B; Espeseth AS
[Ad] Endereço:Department of Infectious Diseases and Vaccines, Merck Research Laboratories, Merck & Co., Inc., Kenilworth, New Jersey, USA dai_wang@merck.com.
[Ti] Título:A Single-Dose Recombinant Parainfluenza Virus 5-Vectored Vaccine Expressing Respiratory Syncytial Virus (RSV) F or G Protein Protected Cotton Rats and African Green Monkeys from RSV Challenge.
[So] Source:J Virol;91(11), 2017 Jun 01.
[Is] ISSN:1098-5514
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Human respiratory syncytial virus (RSV) is a common cause of severe respiratory disease among infants, immunocompromised individuals, and the elderly. No licensed vaccine is currently available. In this study, we evaluated two parainfluenza virus 5 (PIV5)-vectored vaccines expressing RSV F (PIV5/F) or G (PIV5/G) protein in the cotton rat and African green monkey models for their replication, immunogenicity, and efficacy of protection against RSV challenge. Following a single intranasal inoculation, both animal species shed the vaccine viruses for a limited time but without noticeable clinical symptoms. In cotton rats, the vaccines elicited RSV F- or G-specific serum antibodies and conferred complete lung protection against RSV challenge at doses as low as 10 PFU. Neither vaccine produced the enhanced lung pathology observed in animals immunized with formalin-inactivated RSV. In African green monkeys, vaccine-induced serum and mucosal antibody responses were readily detected, as well. PIV5/F provided nearly complete protection against RSV infection in the upper and lower respiratory tract at a dose of 10 PFU of vaccine. At the same dose levels, PIV5/G was less efficacious. Both PIV5/F and PIV5/G were also able to boost neutralization titers in RSV-preexposed African green monkeys. Overall, our data indicated that PIV5/F is a promising RSV vaccine candidate. A safe and efficacious respiratory syncytial virus (RSV) vaccine remains elusive. We tested the recombinant parainfluenza virus 5 (PIV5) vectors expressing RSV glycoproteins for their immunogenicity and protective efficacy in cotton rats and African green monkeys, which are among the best available animal models to study RSV infection. In both species, a single dose of intranasal immunization with PIV5-vectored vaccines was able to produce systemic and local immunity and to protect animals from RSV challenge. The vaccines could also boost RSV neutralization antibody titers in African green monkeys that had been infected previously. Our data suggest that PIV5-vectored vaccines could potentially protect both the pediatric and elderly populations and support continued development of the vector platform.
[Mh] Termos MeSH primário: Vírus da Parainfluenza 5/genética
Infecções por Vírus Respiratório Sincicial/prevenção & controle
Vacinas contra Vírus Sincicial Respiratório/imunologia
Vírus Sincicial Respiratório Humano/imunologia
[Mh] Termos MeSH secundário: Animais
Anticorpos Antivirais/sangue
Anticorpos Antivirais/imunologia
Cercopithecus aethiops
Modelos Animais de Doenças
Vetores Genéticos
Pulmão/virologia
Ratos
Infecções por Vírus Respiratório Sincicial/imunologia
Infecções por Vírus Respiratório Sincicial/virologia
Vacinas contra Vírus Sincicial Respiratório/administração & dosagem
Vacinas contra Vírus Sincicial Respiratório/genética
Vírus Sincicial Respiratório Humano/genética
Sigmodontinae
Vacinação
Vacinas Sintéticas/administração & dosagem
Vacinas Sintéticas/imunologia
Células Vero
Proteínas do Envelope Viral/genética
Proteínas Virais de Fusão/genética
[Pt] Tipo de publicação:EVALUATION STUDIES; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antibodies, Viral); 0 (F protein, human respiratory syncytial virus); 0 (Respiratory Syncytial Virus Vaccines); 0 (Vaccines, Synthetic); 0 (Viral Envelope Proteins); 0 (Viral Fusion Proteins); 0 (attachment protein G)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171112
[Lr] Data última revisão:
171112
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170317
[St] Status:MEDLINE


  2 / 78 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28138777
[Au] Autor:Zhai JQ; Zhai SL; Lin T; Liu JK; Wang HX; Li B; Zhang H; Zou SZ; Zhou X; Wu MF; Chen W; Luo ML
[Ad] Endereço:Key Laboratory of Zoonosis Prevention and Control of Guangdong Province, College of Veterinary Medicine, South China Agricultural University, Guangzhou, 510642, China.
[Ti] Título:First complete genome sequence of parainfluenza virus 5 isolated from lesser panda.
[So] Source:Arch Virol;162(5):1413-1418, 2017 May.
[Is] ISSN:1432-8798
[Cp] País de publicação:Austria
[La] Idioma:eng
[Ab] Resumo:Parainfluenza virus 5 (PIV5) is widespread in mammals and humans. Up to now, there is little information about PIV5 infection in lesser pandas. In this study, a PIV5 variant (named ZJQ-221) was isolated from a lesser panda with respiratory disease in Guangzhou zoo in Guangdong province, southern China. The full-length genome of ZJQ-221 was found to be 15,246 nucleotides and consisted of seven non-overlapping genes encoding eight proteins (i.e., NP, V, P, M, F, SH, HN and L). Sequence alignment and genetic analysis revealed that ZJQ-221 shared a close relationship with a PIV5 strain of canine-origin (1168-1) from South Korea. The findings of this study confirm the presence of PIV5 in lesser panda and indicate this mammal as a possible natural reservoir. Furthermore they highlight the urgent need to strengthen viral surveillance and control of PIV5 in zoo animals.
[Mh] Termos MeSH primário: Ailuridae/virologia
DNA Viral/genética
Genoma Viral/genética
Vírus da Parainfluenza 5/genética
Infecções por Rubulavirus/veterinária
[Mh] Termos MeSH secundário: Animais
Animais de Zoológico/virologia
Sequência de Bases
Linhagem Celular
Cercopithecus aethiops
Vírus da Parainfluenza 5/isolamento & purificação
Infecções por Rubulavirus/virologia
Análise de Sequência de DNA
Células Vero
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA, Viral)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170428
[Lr] Data última revisão:
170428
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170201
[St] Status:MEDLINE
[do] DOI:10.1007/s00705-017-3245-0


  3 / 78 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:27512068
[Au] Autor:Young DF; Andrejeva J; Li X; Inesta-Vaquera F; Dong C; Cowling VH; Goodbourn S; Randall RE
[Ad] Endereço:School of Biology, Centre for Biomolecular Sciences, University of St. Andrews, St. Andrews, Fife, United Kingdom.
[Ti] Título:Human IFIT1 Inhibits mRNA Translation of Rubulaviruses but Not Other Members of the Paramyxoviridae Family.
[So] Source:J Virol;90(20):9446-56, 2016 Oct 15.
[Is] ISSN:1098-5514
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:UNLABELLED: We have previously shown that IFIT1 is primarily responsible for the antiviral action of interferon (IFN) alpha/beta against parainfluenza virus type 5 (PIV5), selectively inhibiting the translation of PIV5 mRNAs. Here we report that while PIV2, PIV5, and mumps virus (MuV) are sensitive to IFIT1, nonrubulavirus members of the paramyxoviridae such as PIV3, Sendai virus (SeV), and canine distemper virus (CDV) are resistant. The IFIT1 sensitivity of PIV5 was not rescued by coinfection with an IFIT1-resistant virus (PIV3), demonstrating that PIV3 does not specifically inhibit the antiviral activity of IFIT1 and that the inhibition of PIV5 mRNAs is regulated by cis-acting elements. We developed an in vitro translation system using purified human IFIT1 to further investigate the mechanism of action of IFIT1. While the translations of PIV2, PIV5, and MuV mRNAs were directly inhibited by IFIT1, the translations of PIV3, SeV, and CDV mRNAs were not. Using purified human mRNA-capping enzymes, we show biochemically that efficient inhibition by IFIT1 is dependent upon a 5' guanosine nucleoside cap (which need not be N7 methylated) and that this sensitivity is partly abrogated by 2'O methylation of the cap 1 ribose. Intriguingly, PIV5 M mRNA, in contrast to NP mRNA, remained sensitive to inhibition by IFIT1 following in vitro 2'O methylation, suggesting that other structural features of mRNAs may influence their sensitivity to IFIT1. Thus, surprisingly, the viral polymerases (which have 2'-O-methyltransferase activity) of rubulaviruses do not protect these viruses from inhibition by IFIT1. Possible biological consequences of this are discussed. IMPORTANCE: Paramyxoviruses cause a wide variety of diseases, and yet most of their genes encode structural proteins and proteins involved in their replication cycle. Thus, the amount of genetic information that determines the type of disease that paramyxoviruses cause is relatively small. One factor that will influence disease outcomes is how they interact with innate host cell defenses, including the interferon (IFN) system. Here we show that different paramyxoviruses interact in distinct ways with cells in a preexisting IFN-induced antiviral state. Strikingly, all the rubulaviruses tested were sensitive to the antiviral action of ISG56/IFIT1, while all the other paramyxoviruses tested were resistant. We developed novel in vitro biochemical assays to investigate the mechanism of action of IFIT1, demonstrating that the mRNAs of rubulaviruses can be directly inhibited by IFIT1 and that this is at least partially because their mRNAs are not correctly methylated.
[Mh] Termos MeSH primário: Proteínas de Transporte/farmacologia
Paramyxoviridae/genética
Biossíntese de Proteínas/genética
RNA Mensageiro/genética
Rubulavirus/genética
[Mh] Termos MeSH secundário: Células A549
Linhagem Celular Tumoral
Seres Humanos
Interferon-alfa/metabolismo
Metilação
Vírus da Caxumba/genética
Vírus da Parainfluenza 5/genética
Capuzes de RNA/genética
RNA Viral/genética
Vírus Sendai/genética
Replicação Viral/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Carrier Proteins); 0 (IFIT1 protein, human); 0 (Interferon-alpha); 0 (RNA Caps); 0 (RNA, Messenger); 0 (RNA, Viral)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170922
[Lr] Data última revisão:
170922
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160812
[St] Status:MEDLINE
[do] DOI:10.1128/JVI.01056-16


  4 / 78 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:27505156
[Au] Autor:Li Y; Johnson JB; Parks GD
[Ad] Endereço:Burnett School of Biomedical Sciences, University of Central Florida, College of Medicine, Orlando, FL 32827, USA.
[Ti] Título:Parainfluenza virus 5 upregulates CD55 expression to produce virions with enhanced resistance to complement-mediated neutralization.
[So] Source:Virology;497:305-313, 2016 Oct.
[Is] ISSN:1096-0341
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Many enveloped RNA viruses recruit host cell proteins during assembly as a mechanism to limit antiviral effects of complement. Using viruses which incorporated CD46 alone, CD55 alone or both CD46 and CD55, we addressed the role of these two host cell regulators in limiting complement-mediated neutralization of Parainfluenza virus 5 (PIV5). PIV5 incorporated functional forms of both CD55 and CD46 into virions. PIV5 containing CD55 was highly resistant to complement-mediated neutralization, whereas CD46-containing PIV5 was as sensitive to neutralization as virus lacking both regulators. PIV5 infected cells had increased levels of cell surface CD55, which was further upregulated by exogenous treatment with tumor necrosis factor alpha. PIV5 derived from cells with higher CD55 levels was more resistant to complement-mediated neutralization in vitro than virus from control cells. We propose a role for virus induction of host cell complement inhibitors in defining virus growth and tissue tropism.
[Mh] Termos MeSH primário: Antígenos CD55/genética
Proteínas do Sistema Complemento/imunologia
Regulação da Expressão Gênica
Vírus da Parainfluenza 5/fisiologia
Infecções por Rubulavirus/genética
Infecções por Rubulavirus/virologia
Replicação Viral
[Mh] Termos MeSH secundário: Animais
Antígenos CD55/metabolismo
Células CHO
Linhagem Celular
Ativação do Complemento/imunologia
Cricetinae
Cricetulus
Seres Humanos
Proteína Cofatora de Membrana/genética
Proteína Cofatora de Membrana/metabolismo
Testes de Neutralização
Infecções por Rubulavirus/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (CD55 Antigens); 0 (Membrane Cofactor Protein); 9007-36-7 (Complement System Proteins)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160810
[St] Status:MEDLINE


  5 / 78 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:27489276
[Au] Autor:Adu-Gyamfi E; Kim LS; Jardetzky TS; Lamb RA
[Ad] Endereço:Department of Molecular Biosciences, Northwestern University, Evanston, Illinois, USA.
[Ti] Título:Flexibility of the Head-Stalk Linker Domain of Paramyxovirus HN Glycoprotein Is Essential for Triggering Virus Fusion.
[So] Source:J Virol;90(20):9172-81, 2016 Oct 15.
[Is] ISSN:1098-5514
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:UNLABELLED: The Paramyxoviridae comprise a large family of enveloped, negative-sense, single-stranded RNA viruses with significant economic and public health implications. For nearly all paramyxoviruses, infection is initiated by fusion of the viral and host cell plasma membranes in a pH-independent fashion. Fusion is orchestrated by the receptor binding protein hemagglutinin-neuraminidase (HN; also called H or G depending on the virus type) protein and a fusion (F) protein, the latter undergoing a major refolding process to merge the two membranes. Mechanistic details regarding the coupling of receptor binding to F activation are not fully understood. Here, we have identified the flexible loop region connecting the bulky enzymatically active head and the four-helix bundle stalk to be essential for fusion promotion. Proline substitution in this region of HN of parainfluenza virus 5 (PIV5) and Newcastle disease virus HN abolishes cell-cell fusion, whereas HN retains receptor binding and neuraminidase activity. By using reverse genetics, we engineered recombinant PIV5-EGFP viruses with mutations in the head-stalk linker region of HN. Mutations in this region abolished virus recovery and infectivity. In sum, our data suggest that the loop region acts as a "hinge" around which the bulky head of HN swings to-and-fro to facilitate timely HN-mediate F-triggering, a notion consistent with the stalk-mediated activation model of paramyxovirus fusion. IMPORTANCE: Paramyxovirus fusion with the host cell plasma membrane is essential for virus infection. Membrane fusion is orchestrated via interaction of the receptor binding protein (HN, H, or G) with the viral fusion glycoprotein (F). Two distinct models have been suggested to describe the mechanism of fusion: these include "the clamp" and the "provocateur" model of activation. By using biochemical and reverse genetics tools, we have obtained strong evidence in favor of the HN stalk-mediated activation of paramyxovirus fusion. Specifically, our data strongly support the notion that the short linker between the head and stalk plays a role in "conformational switching" of the head group to facilitate F-HN interaction and triggering.
[Mh] Termos MeSH primário: Proteína HN/metabolismo
Vírus da Doença de Newcastle/fisiologia
Vírus da Parainfluenza 5/fisiologia
Ligação Viral
Internalização do Vírus
[Mh] Termos MeSH secundário: Animais
Linhagem Celular
Análise Mutacional de DNA
Proteína HN/genética
Seres Humanos
Mutagênese Sítio-Dirigida
Vírus da Doença de Newcastle/genética
Vírus da Parainfluenza 5/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (HN Protein)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170510
[Lr] Data última revisão:
170510
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160805
[St] Status:MEDLINE
[do] DOI:10.1128/JVI.01187-16


  6 / 78 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:27335462
[Au] Autor:Song AS; Poor TA; Abriata LA; Jardetzky TS; Dal Peraro M; Lamb RA
[Ad] Endereço:Department of Molecular Biosciences, Northwestern University, Evanston, IL 60208-3500;
[Ti] Título:Immobilization of the N-terminal helix stabilizes prefusion paramyxovirus fusion proteins.
[So] Source:Proc Natl Acad Sci U S A;113(27):E3844-51, 2016 07 05.
[Is] ISSN:1091-6490
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Parainfluenza virus 5 (PIV5) is an enveloped, single-stranded, negative-sense RNA virus of the Paramyxoviridae family. PIV5 fusion and entry are mediated by the coordinated action of the receptor-binding protein, hemagglutinin-neuraminidase (HN), and the fusion protein (F). Upon triggering by HN, F undergoes an irreversible ATP- and pH-independent conformational change, going down an energy gradient from a metastable prefusion state to a highly stable postfusion state. Previous studies have highlighted key conformational changes in the F-protein refolding pathway, but a detailed understanding of prefusion F-protein metastability remains elusive. Here, using two previously described F-protein mutations (S443D or P22L), we examine the capacity to modulate PIV5 F stability and the mechanisms by which these point mutants act. The S443D mutation destabilizes prefusion F proteins by disrupting a hydrogen bond network at the base of the F-protein globular head. The introduction of a P22L mutation robustly rescues destabilized F proteins through a local hydrophobic interaction between the N-terminal helix and a hydrophobic pocket. Prefusion stabilization conferred by a P22L-homologous mutation is demonstrated in the F protein of Newcastle disease virus, a paramyxovirus of a different genus, suggesting a conserved stabilizing structural element within the paramyxovirus family. Taken together, the available data suggest that movement of the N-terminal helix is a necessary early step for paramyxovirus F-protein refolding and presents a novel target for structure-based drug design.
[Mh] Termos MeSH primário: Vírus da Parainfluenza 5/metabolismo
Proteínas Virais de Fusão/metabolismo
[Mh] Termos MeSH secundário: Substituição de Aminoácidos
Animais
Cercopithecus aethiops
Conformação Molecular
Mutação
Estabilidade Proteica
Células Vero
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Viral Fusion Proteins)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170807
[Lr] Data última revisão:
170807
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160624
[St] Status:MEDLINE
[do] DOI:10.1073/pnas.1608349113


  7 / 78 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:27072881
[Au] Autor:Matsumoto Y; Ohta K; Goto H; Nishio M
[Ad] Endereço:Department of Microbiology, School of Medicine, Wakayama Medical University, 811-1 Kimiidera, Wakayama, 641-8509, Japan.
[Ti] Título:Parainfluenza virus chimeric mini-replicons indicate a novel regulatory element in the leader promoter.
[So] Source:J Gen Virol;97(7):1520-30, 2016 Jul.
[Is] ISSN:1465-2099
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Gene expression of paramyxoviruses is regulated by genome-encoded cis-acting elements; however, whether all the required elements for viral growth have been identified is not clear. Using a mini-replicon system, it has been shown that human parainfluenza virus type 2 (hPIV2) polymerase can recognize the promoter elements of parainfluenza virus type 5 (PIV5), but reporter activity is lower in this case. We constructed a series of luciferase-encoding chimeric PIV2/5 mini-genomes that are basically hPIV2, but whose leader (le), mRNA start signal and trailer sequence are partially replaced with those of PIV5. Studies of the chimeric PIV2/5 mini-replicons demonstrated that replacement of hPIV2 le with PIV5 le results in remarkably weak luciferase expression. Further mutagenesis identified the responsible region as positions 25-30 of the PIV5 le. Using recombinant hPIV2, the impact of this region on viral life cycles was assessed. Insertion of the mutation at this region facilitated viral growth, genomic replication and mRNA transcription at the early stage of infection, which elicited severe cell damage. In contrast, at the late infection stage it caused a reduction in viral transcription. Here, we identify a novel cis-acting element in the internal region of an le sequence that is involved in the regulation of polymerase, and which contributes to maintaining a balance between viral growth and cytotoxicity.
[Mh] Termos MeSH primário: Regiões 5´ não Traduzidas/genética
Quimera/genética
Vírus da Parainfluenza 2 Humana/genética
Vírus da Parainfluenza 5/genética
Regiões Promotoras Genéticas/genética
RNA Replicase/genética
Sequências Reguladoras de Ácido Nucleico/genética
[Mh] Termos MeSH secundário: Sequência de Bases
Linhagem Celular Tumoral
Genoma Viral/genética
Células HeLa
Seres Humanos
Vírus da Parainfluenza 2 Humana/crescimento & desenvolvimento
Vírus da Parainfluenza 5/crescimento & desenvolvimento
Infecções por Paramyxoviridae/virologia
RNA Viral/genética
Replicon/genética
Transcrição Genética/genética
Replicação Viral/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (5' Untranslated Regions); 0 (RNA, Viral); EC 2.7.7.48 (RNA Replicase)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170519
[Lr] Data última revisão:
170519
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160414
[St] Status:MEDLINE
[do] DOI:10.1099/jgv.0.000479


  8 / 78 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
PubMed Central Texto completo
Texto completo
[PMID]:26792745
[Au] Autor:Ray G; Schmitt PT; Schmitt AP
[Ad] Endereço:Department of Veterinary and Biomedical Sciences, The Pennsylvania State University, University Park, Pennsylvania, USA.
[Ti] Título:C-Terminal DxD-Containing Sequences within Paramyxovirus Nucleocapsid Proteins Determine Matrix Protein Compatibility and Can Direct Foreign Proteins into Budding Particles.
[So] Source:J Virol;90(7):3650-60, 2016 Jan 20.
[Is] ISSN:1098-5514
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:UNLABELLED: Paramyxovirus particles are formed by a budding process coordinated by viral matrix (M) proteins. M proteins coalesce at sites underlying infected cell membranes and induce other viral components, including viral glycoproteins and viral ribonucleoprotein complexes (vRNPs), to assemble at these locations from which particles bud. M proteins interact with the nucleocapsid (NP or N) components of vRNPs, and these interactions enable production of infectious, genome-containing virions. For the paramyxoviruses parainfluenza virus 5 (PIV5) and mumps virus, M-NP interaction also contributes to efficient production of virus-like particles (VLPs) in transfected cells. A DLD sequence near the C-terminal end of PIV5 NP protein was previously found to be necessary for M-NP interaction and efficient VLP production. Here, we demonstrate that 15-residue-long, DLD-containing sequences derived from either the PIV5 or Nipah virus nucleocapsid protein C-terminal ends are sufficient to direct packaging of a foreign protein, Renilla luciferase, into budding VLPs. Mumps virus NP protein harbors DWD in place of the DLD sequence found in PIV5 NP protein, and consequently, PIV5 NP protein is incompatible with mumps virus M protein. A single amino acid change converting DLD to DWD within PIV5 NP protein induced compatibility between these proteins and allowed efficient production of mumps VLPs. Our data suggest a model in which paramyxoviruses share an overall common strategy for directing M-NP interactions but with important variations contained within DLD-like sequences that play key roles in defining M/NP protein compatibilities. IMPORTANCE: Paramyxoviruses are responsible for a wide range of diseases that affect both humans and animals. Paramyxovirus pathogens include measles virus, mumps virus, human respiratory syncytial virus, and the zoonotic paramyxoviruses Nipah virus and Hendra virus. Infectivity of paramyxovirus particles depends on matrix-nucleocapsid protein interactions which enable efficient packaging of encapsidated viral RNA genomes into budding virions. In this study, we have defined regions near the C-terminal ends of paramyxovirus nucleocapsid proteins that are important for matrix protein interaction and that are sufficient to direct a foreign protein into budding particles. These results advance our basic understanding of paramyxovirus genome packaging interactions and also have implications for the potential use of virus-like particles as protein delivery tools.
[Mh] Termos MeSH primário: Motivos de Aminoácidos
Vírus da Caxumba/fisiologia
Vírus Nipah/fisiologia
Proteínas do Nucleocapsídeo/metabolismo
Vírus da Parainfluenza 5/fisiologia
Proteínas da Matriz Viral/metabolismo
Montagem de Vírus
[Mh] Termos MeSH secundário: Linhagem Celular
Seres Humanos
Luciferases de Renilla/metabolismo
Vírus da Caxumba/genética
Vírus Nipah/genética
Proteínas do Nucleocapsídeo/química
Proteínas do Nucleocapsídeo/genética
Vírus da Parainfluenza 5/genética
Ligação Proteica
Mapeamento de Interação de Proteínas
Proteínas da Matriz Viral/química
Virossomos/metabolismo
Liberação de Vírus
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Nucleocapsid Proteins); 0 (Viral Matrix Proteins); 0 (Virosomes); EC 1.13.12.5 (Luciferases, Renilla)
[Em] Mês de entrada:1607
[Cu] Atualização por classe:161019
[Lr] Data última revisão:
161019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160122
[St] Status:MEDLINE
[do] DOI:10.1128/JVI.02673-15


  9 / 78 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
PubMed Central Texto completo
Texto completo
[PMID]:26583313
[Au] Autor:Liu Y; Li N; Zhang S; Zhang F; Lian H; Hu R
[Ti] Título:Parainfluenza Virus 5 as Possible Cause of Severe Respiratory Disease in Calves, China.
[So] Source:Emerg Infect Dis;21(12):2242-4, 2015 Dec.
[Is] ISSN:1080-6059
[Cp] País de publicação:United States
[La] Idioma:eng
[Mh] Termos MeSH primário: Bovinos/virologia
Vírus da Parainfluenza 5/genética
Vírus da Parainfluenza 5/patogenicidade
Infecções por Respirovirus
[Mh] Termos MeSH secundário: Animais
Bovinos/genética
China
[Pt] Tipo de publicação:LETTER; RESEARCH SUPPORT, NON-U.S. GOV'T
[Em] Mês de entrada:1607
[Cu] Atualização por classe:151209
[Lr] Data última revisão:
151209
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151120
[St] Status:MEDLINE
[do] DOI:10.3201/eid2112.141111


  10 / 78 MEDLINE  
              first record previous record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:26552000
[Au] Autor:Chen Z; Gupta T; Xu P; Phan S; Pickar A; Yau W; Karls RK; Quinn FD; Sakamoto K; He B
[Ad] Endereço:Department of Infectious Diseases, University of Georgia College of Veterinary Medicine, Athens, GA, USA.
[Ti] Título:Efficacy of parainfluenza virus 5 (PIV5)-based tuberculosis vaccines in mice.
[So] Source:Vaccine;33(51):7217-7224, 2015 Dec 16.
[Is] ISSN:1873-2518
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Mycobacterium tuberculosis, the etiological agent of tuberculosis (TB), is an important human pathogen. Bacillus Calmette-Guérin (BCG), a live, attenuated variant of Mycobacterium bovis, is currently the only available TB vaccine despite its low efficacy against the infectious pulmonary form of the disease in adults. Thus, a more-effective TB vaccine is needed. Parainfluenza virus 5 (PIV5), a paramyxovirus, has several characteristics that make it an attractive vaccine vector. It is safe, inexpensive to produce, and has been previously shown to be efficacious as the backbone of vaccines for influenza, rabies, and respiratory syncytial virus. In this work, recombinant PIV5 expressing M. tuberculosis antigens 85A (PIV5-85A) and 85B (PIV5-85B) have been generated and their immunogenicity and protective efficacy evaluated in a mouse aerosol infection model. In a long-term protection study, a single dose of PIV5-85A was found to be most effective in reducing M. tuberculosis colony forming units (CFU) in lungs when compared to unvaccinated, whereas the BCG vaccinated animals had similar numbers of CFUs to unvaccinated animals. BCG-prime followed by a PIV5-85A or PIV5-85B boost produced better outcomes highlighted by close to three-log units lower lung CFUs compared to PBS. The results indicate that PIV5-based M. tuberculosis vaccines are promising candidates for further development.
[Mh] Termos MeSH primário: Aciltransferases/imunologia
Antígenos de Bactérias/imunologia
Proteínas de Bactérias/imunologia
Portadores de Fármacos
Vírus da Parainfluenza 5/genética
Vacinas contra a Tuberculose/imunologia
Tuberculose/prevenção & controle
[Mh] Termos MeSH secundário: Aciltransferases/genética
Animais
Antígenos de Bactérias/genética
Proteínas de Bactérias/genética
Contagem de Colônia Microbiana
Modelos Animais de Doenças
Feminino
Pulmão/microbiologia
Camundongos Endogâmicos BALB C
Resultado do Tratamento
Vacinas contra a Tuberculose/administração & dosagem
Vacinas contra a Tuberculose/genética
Vacinas Sintéticas/administração & dosagem
Vacinas Sintéticas/genética
Vacinas Sintéticas/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antigens, Bacterial); 0 (Bacterial Proteins); 0 (Drug Carriers); 0 (Tuberculosis Vaccines); 0 (Vaccines, Synthetic); EC 2.3.- (Acyltransferases); EC 2.3.1.- (antigen 85A, Mycobacterium tuberculosis); EC 2.3.1.- (antigen 85B, Mycobacterium tuberculosis)
[Em] Mês de entrada:1610
[Cu] Atualização por classe:171021
[Lr] Data última revisão:
171021
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151110
[St] Status:MEDLINE



página 1 de 8 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