Base de dados : MEDLINE
Pesquisa : G04.575 [Categoria DeCS]
Referências encontradas : 7544 [refinar]
Mostrando: 1 .. 10   no formato [Detalhado]

página 1 de 755 ir para página                         

  1 / 7544 MEDLINE  
              next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:29382836
[Au] Autor:Füzik T; Formanová P; Ruzek D; Yoshii K; Niedrig M; Plevka P
[Ad] Endereço:Structural Virology, Central European Institute of Technology, Masaryk University, Kamenice 753/5, 62500, Brno, Czech Republic.
[Ti] Título:Structure of tick-borne encephalitis virus and its neutralization by a monoclonal antibody.
[So] Source:Nat Commun;9(1):436, 2018 01 30.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Tick-borne encephalitis virus (TBEV) causes 13,000 cases of human meningitis and encephalitis annually. However, the structure of the TBEV virion and its interactions with antibodies are unknown. Here, we present cryo-EM structures of the native TBEV virion and its complex with Fab fragments of neutralizing antibody 19/1786. Flavivirus genome delivery depends on membrane fusion that is triggered at low pH. The virion structure indicates that the repulsive interactions of histidine side chains, which become protonated at low pH, may contribute to the disruption of heterotetramers of the TBEV envelope and membrane proteins and induce detachment of the envelope protein ectodomains from the virus membrane. The Fab fragments bind to 120 out of the 180 envelope glycoproteins of the TBEV virion. Unlike most of the previously studied flavivirus-neutralizing antibodies, the Fab fragments do not lock the E-proteins in the native-like arrangement, but interfere with the process of virus-induced membrane fusion.
[Mh] Termos MeSH primário: Anticorpos Neutralizantes/química
Anticorpos Antivirais/química
Vírus da Encefalite Transmitidos por Carrapatos/ultraestrutura
Fragmentos Fab das Imunoglobulinas/química
Proteínas Virais/química
Vírion/ultraestrutura
[Mh] Termos MeSH secundário: Anticorpos Neutralizantes/biossíntese
Anticorpos Antivirais/biossíntese
Linhagem Celular Tumoral
Microscopia Crioeletrônica
Vírus da Encefalite Transmitidos por Carrapatos/genética
Vírus da Encefalite Transmitidos por Carrapatos/metabolismo
Expressão Gênica
Seres Humanos
Concentração de Íons de Hidrogênio
Fragmentos Fab das Imunoglobulinas/biossíntese
Fusão de Membrana/genética
Neurônios/patologia
Neurônios/virologia
Domínios Proteicos
Multimerização Proteica
Proteínas Virais/genética
Proteínas Virais/metabolismo
Vírion/genética
Vírion/metabolismo
Internalização do Vírus
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antibodies, Neutralizing); 0 (Antibodies, Viral); 0 (Immunoglobulin Fab Fragments); 0 (Viral Proteins)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180307
[Lr] Data última revisão:
180307
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180201
[St] Status:MEDLINE
[do] DOI:10.1038/s41467-018-02882-0


  2 / 7544 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:29176784
[Au] Autor:Fu C; Heitman J
[Ad] Endereço:Department of Molecular Genetics and Microbiology, Duke University Medical Center, Durham, NC, United States of America.
[Ti] Título:PRM1 and KAR5 function in cell-cell fusion and karyogamy to drive distinct bisexual and unisexual cycles in the Cryptococcus pathogenic species complex.
[So] Source:PLoS Genet;13(11):e1007113, 2017 Nov.
[Is] ISSN:1553-7404
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Sexual reproduction is critical for successful evolution of eukaryotic organisms in adaptation to changing environments. In the opportunistic human fungal pathogens, the Cryptococcus pathogenic species complex, C. neoformans primarily undergoes bisexual reproduction, while C. deneoformans undergoes both unisexual and bisexual reproduction. During both unisexual and bisexual cycles, a common set of genetic circuits regulates a yeast-to-hyphal morphological transition, that produces either monokaryotic or dikaryotic hyphae. As such, both the unisexual and bisexual cycles can generate genotypic and phenotypic diversity de novo. Despite the similarities between these two cycles, genetic and morphological differences exist, such as the absence of an opposite mating-type partner and monokaryotic instead of dikaryotic hyphae during C. deneoformans unisexual cycle. To better understand the similarities and differences between these modes of sexual reproduction, we focused on two cellular processes involved in sexual reproduction: cell-cell fusion and karyogamy. We identified orthologs of the plasma membrane fusion protein Prm1 and the nuclear membrane fusion protein Kar5 in both Cryptococcus species, and demonstrated their conserved roles in cell fusion and karyogamy during C. deneoformans α-α unisexual reproduction and C. deneoformans and C. neoformans a-α bisexual reproduction. Notably, karyogamy occurs inside the basidum during bisexual reproduction in C. neoformans, but often occurs earlier following cell fusion during bisexual reproduction in C. deneoformans. Characterization of these two genes also showed that cell fusion is dispensable for solo unisexual reproduction in C. deneoformans. The blastospores produced along hyphae during C. deneoformans unisexual reproduction are diploid, suggesting that diploidization occurs early during hyphal development, possibly through either an endoreplication pathway or cell fusion-independent karyogamy events. Taken together, our findings suggest distinct mating mechanisms for unisexual and bisexual reproduction in Cryptococcus, exemplifying distinct evolutionary trajectories within this pathogenic species complex.
[Mh] Termos MeSH primário: Cryptococcus neoformans/genética
Proteínas Fúngicas/genética
Genes Fúngicos Tipo Acasalamento/genética
Reprodução Assexuada/genética
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Núcleo Celular/genética
Núcleo Celular/metabolismo
Cryptococcus neoformans/citologia
Cryptococcus neoformans/crescimento & desenvolvimento
Diploide
Regulação da Expressão Gênica no Desenvolvimento
Regulação Fúngica da Expressão Gênica
Hifas/genética
Hifas/crescimento & desenvolvimento
Fusão de Membrana/genética
Microscopia Confocal
Modelos Genéticos
Mutação
Homologia de Sequência de Aminoácidos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Fungal Proteins)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:180307
[Lr] Data última revisão:
180307
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171128
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pgen.1007113


  3 / 7544 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:29351320
[Au] Autor:Kumar P; van Son M; Zheng T; Valdink D; Raap J; Kros A; Huber M
[Ad] Endereço:Department of Physics, Huygens-Kamerlingh Onnes Laboratory, Leiden University, Leiden, The Netherlands.
[Ti] Título:Coiled-coil formation of the membrane-fusion K/E peptides viewed by electron paramagnetic resonance.
[So] Source:PLoS One;13(1):e0191197, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The interaction of the complementary K (Ac-(KIAALKE)3-GW-NH2) and E (Ac-(EIAALEK)3-GY-NH2) peptides, components of the zipper of an artificial membrane fusion system (Robson Marsden H. et al. Angew Chemie Int Ed. 2009) is investigated by electron paramagnetic resonance (EPR). By frozen solution continuous-wave EPR and double electron-electron resonance (DEER), the distance between spin labels attached to the K- and to the E-peptide is measured. Three constructs of spin-labelled K- and E-peptides are used in five combinations for low temperature investigations. The K/E heterodimers are found to be parallel, in agreement with previous studies. Also, K homodimers in parallel orientation were observed, a finding that was not reported before. Comparison to room-temperature, solution EPR shows that the latter method is less specific to detect this peptide-peptide interaction. Combining frozen solution cw-EPR for short distances (1.8 nm to 2.0 nm) and DEER for longer distances thus proves versatile to detect the zipper interaction in membrane fusion. As the methodology can be applied to membrane samples, the approach presented suggests itself for in-situ studies of the complete membrane fusion process, opening up new avenues for the study of membrane fusion.
[Mh] Termos MeSH primário: Proteínas de Fusão de Membrana/química
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Simulação por Computador
Espectroscopia de Ressonância de Spin Eletrônica
Fusão de Membrana/fisiologia
Proteínas de Fusão de Membrana/fisiologia
Modelos Moleculares
Oligopeptídeos/química
Domínios e Motivos de Interação entre Proteínas
Estrutura Quaternária de Proteína
Estrutura Secundária de Proteína
Marcadores de Spin
Temperatura Ambiente
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Membrane Fusion Proteins); 0 (Oligopeptides); 0 (Spin Labels)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180221
[Lr] Data última revisão:
180221
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180120
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0191197


  4 / 7544 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:29289693
[Au] Autor:Wang TY; Ma Z; Wang C; Liu C; Yan DY; Deng Y; Liu W; Xu ZF; Xu B
[Ad] Endereço:Department of Environmental Health, School of Public Health, China Medical University, People's Republic of China.
[Ti] Título:Manganese-induced alpha-synuclein overexpression impairs synaptic vesicle fusion by disrupting the Rab3 cycle in primary cultured neurons.
[So] Source:Toxicol Lett;285:34-42, 2018 Mar 15.
[Is] ISSN:1879-3169
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Overexposure to Manganese (Mn) has been known to disrupt neurotransmitter release in the brain. However, the underlying mechanisms of Mn exposure on neurotransmitter vesicle release are still unclear. The current study investigated whether Mn-induced alpha-synuclein protein overexpression could disrupt the Rab3 cycle leading to synaptic vesicle fusion dysfunction. After the neurons were exposed to Mn (100 µM) for 0, 6, 12, 24 h, [Ca ] , alpha-synuclein and Rab3A-GTP protein expression increased gradually. However, the interaction of synaptotagmin/Rab3-GAP and Rab3A-GTP/Rab3-GAP decreased significantly in response to Mn treatment for 12-24 h. Remarkably, the treatment with Mn caused an increase in the interaction of alpha-synuclein/Rab3A-GTP. To further validate that Mn-induced alpha-synuclein disrupted the proteins interactions of Rab3A-GTP/Rab3-GAP, the lentivirus vector of alpha-synuclein/negative shRNA was transfected in primary cultured neurons to knockdown the expression of alpha-synuclein. Our results showed that the interaction of Rab3A-GTP/Rab3-GAP in alpha-synuclein knockdown neurons treated with Mn for 24 h had a significant recovery. These results suggested that Mn-induced alpha-synuclein protein overexpression, which bound to Rab3A-GTP and inhibited the GTP hydrolysis of Rab3 protein, disrupted the Rab3 cycle leading to synaptic vesicle fusion dysfunction.
[Mh] Termos MeSH primário: Manganês/toxicidade
Fusão de Membrana/efeitos dos fármacos
Neurônios/efeitos dos fármacos
Vesículas Sinápticas/efeitos dos fármacos
alfa-Sinucleína/metabolismo
Proteínas rab3 de Ligação ao GTP/metabolismo
[Mh] Termos MeSH secundário: Animais
Animais Recém-Nascidos
Sobrevivência Celular/efeitos dos fármacos
Células Cultivadas
Técnicas de Silenciamento de Genes
Neurônios/metabolismo
Cultura Primária de Células
Ratos Wistar
Vesículas Sinápticas/metabolismo
alfa-Sinucleína/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (alpha-Synuclein); 42Z2K6ZL8P (Manganese); EC 3.6.5.2 (rab3 GTP-Binding Proteins)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180219
[Lr] Data última revisão:
180219
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180101
[St] Status:MEDLINE


  5 / 7544 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:29189794
[Ti] Título:A day in the life of a cell biologist.
[So] Source:Nature;551(7682):S182, 2017 11 30.
[Is] ISSN:1476-4687
[Cp] País de publicação:England
[La] Idioma:eng
[Mh] Termos MeSH primário: Biologia Celular
Pesquisadores
[Mh] Termos MeSH secundário: Pesquisa Interdisciplinar
Fusão de Membrana
Microscopia
Sinaptotagmina I/metabolismo
[Pt] Tipo de publicação:INTERVIEW
[Nm] Nome de substância:
0 (Synaptotagmin I)
[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:171201
[St] Status:MEDLINE
[do] DOI:10.1038/d41586-017-07563-4


  6 / 7544 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:29254991
[Au] Autor:Hernández JM; Podbilewicz B
[Ad] Endereço:Department of Structural Biochemistry, Max Planck Institute of Molecular Physiology, D-44227 Dortmund, Germany matias.hernandez@mpi-dortmund.mpg.de podbilew@technion.ac.il.
[Ti] Título:The hallmarks of cell-cell fusion.
[So] Source:Development;144(24):4481-4495, 2017 Dec 15.
[Is] ISSN:1477-9129
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Cell-cell fusion is essential for fertilization and organ development. Dedicated proteins known as fusogens are responsible for mediating membrane fusion. However, until recently, these proteins either remained unidentified or were poorly understood at the mechanistic level. Here, we review how fusogens surmount multiple energy barriers to mediate cell-cell fusion. We describe how early preparatory steps bring membranes to a distance of ∼10 nm, while fusogens act in the final approach between membranes. The mechanical force exerted by cell fusogens and the accompanying lipidic rearrangements constitute the hallmarks of cell-cell fusion. Finally, we discuss the relationship between viral and eukaryotic fusogens, highlight a classification scheme regrouping a superfamily of fusogens called Fusexins, and propose new questions and avenues of enquiry.
[Mh] Termos MeSH primário: Adesão Celular/fisiologia
Fusão Celular
Fusão de Membrana/fisiologia
[Mh] Termos MeSH secundário: Animais
Caenorhabditis elegans
Proteínas de Caenorhabditis elegans/metabolismo
Drosophila
Produtos do Gene env/metabolismo
Seres Humanos
Glicoproteínas de Membrana/metabolismo
Mioblastos/metabolismo
Proteínas da Gravidez/metabolismo
Proteínas SNARE/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (AFF-1 protein, C elegans); 0 (Caenorhabditis elegans Proteins); 0 (EFF-1 protein, C elegans); 0 (Gene Products, env); 0 (Membrane Glycoproteins); 0 (Pregnancy Proteins); 0 (SNARE Proteins); 0 (syncytin)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180102
[Lr] Data última revisão:
180102
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171220
[St] Status:MEDLINE
[do] DOI:10.1242/dev.155523


  7 / 7544 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:27773768
[Au] Autor:Kordyukova L
[Ad] Endereço:Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Leninskie Gory 1-40, Moscow 119991, Russian Federation. Electronic address: kord@belozersky.msu.ru.
[Ti] Título:Structural and functional specificity of Influenza virus haemagglutinin and paramyxovirus fusion protein anchoring peptides.
[So] Source:Virus Res;227:183-199, 2017 01 02.
[Is] ISSN:1872-7492
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Two enveloped virus families, Orthomyxoviridae and Paramyxoviridae, comprise a large number of dangerous pathogens that enter the host cell via fusion of their envelope with a target cell membrane at acidic or neutral pH. The Class I prototypic glycoproteins responsible for this reaction are the Influenza virus haemagglutinin (HA) protein or paramyxovirus fusion (F) protein. X-ray crystallography and cryoelectron microscopy data are available for the HA and F ectodomains in pre- and post-fusion conformations, revealing similar spiky architectures, albeit with clear differences in the details. In contrast, their anchoring segments, which possess a linker region, transmembrane domain and cytoplasmic tail that is specifically modified with long fatty acids (highly conserved in HA and occasional in F), are not resolved. Recent experimental, bioinformatics and molecular modelling data showing the primary, secondary and quaternary organization of the HA and F anchoring segments are summarized in this review. Some amino acid patterns that are crucial for protein thermal stability or lipid membrane order/cholesterol binding are addressed, and new achievements in vaccine practice using HA transmembrane domain chimaeras are discussed. The oligomerization properties of the transmembrane domains are considered in the context of Group-1 and Group-2 antigenic HA subtypes and various genera/subfamilies of paramyxoviruses. A specific focus is the late steps of fusion that are reportedly facilitated by (1) ß-sheet-promoting ß-branched amino acids (valine and isoleucine) that are enriched in the transmembrane domain of paramyxovirus F or (2) a post-translational modification of C-terminal cysteines with palmitate/stearate (differential S-acylation) that is highly conserved in Influenza virus HA.
[Mh] Termos MeSH primário: Glicoproteínas de Hemaglutininação de Vírus da Influenza/química
Glicoproteínas de Hemaglutininação de Vírus da Influenza/metabolismo
Peptídeos/química
Domínios e Motivos de Interação entre Proteínas
Proteínas Virais de Fusão/química
Proteínas Virais de Fusão/metabolismo
[Mh] Termos MeSH secundário: Motivos de Aminoácidos
Sequência de Aminoácidos
Animais
Membrana Celular
Sequência Conservada
Seres Humanos
Lipídeos/química
Fusão de Membrana
Modelos Moleculares
Peptídeos/metabolismo
Conformação Proteica
Multimerização Proteica
Processamento de Proteína Pós-Traducional
Estabilidade Proteica
Relação Estrutura-Atividade
Termodinâmica
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Hemagglutinin Glycoproteins, Influenza Virus); 0 (Lipids); 0 (Peptides); 0 (Viral Fusion Proteins)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171218
[Lr] Data última revisão:
171218
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161107
[St] Status:MEDLINE


  8 / 7544 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28463755
[Au] Autor:Yu S; Melia TJ
[Ad] Endereço:Department of Cell Biology, Yale University School of Medicine, New Haven, CT, United States.
[Ti] Título:The coordination of membrane fission and fusion at the end of autophagosome maturation.
[So] Source:Curr Opin Cell Biol;47:92-98, 2017 Aug.
[Is] ISSN:1879-0410
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The two major objectives of macroautophagy are to sequester cargo away from the cytoplasm and deliver this material for breakdown in the lysosome. Sequestration is complete when the autophagosome membrane undergoes fission to produce separate inner and outer membranes, while delivery into the lysosome requires fusion of the outer autophagosome membrane with the lysosome membrane. Thus, the merging of membranes through fission and fusion underlies each of the pivotal events in macroautophagic clearance. How these merging events are controlled in the cell is poorly understood. Several recent studies however suggest that the two events may be temporally coordinated and rely upon members of the classic membrane fusion SNARE family as well as the autophagy-specific family of Atg8 proteins.
[Mh] Termos MeSH primário: Autofagossomos/metabolismo
Membranas Intracelulares/metabolismo
Lisossomos/metabolismo
Proteínas SNARE/metabolismo
[Mh] Termos MeSH secundário: Animais
Autofagia
Família da Proteína 8 Relacionada à Autofagia/metabolismo
Fusão de Membrana
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Autophagy-Related Protein 8 Family); 0 (SNARE Proteins)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171128
[Lr] Data última revisão:
171128
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170503
[St] Status:MEDLINE


  9 / 7544 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:29065154
[Au] Autor:Bahrami AH; Lin MG; Ren X; Hurley JH; Hummer G
[Ad] Endereço:Department of Theoretical Biophysics, Max Planck Institute of Biophysics, Frankfurt am Main, Germany.
[Ti] Título:Scaffolding the cup-shaped double membrane in autophagy.
[So] Source:PLoS Comput Biol;13(10):e1005817, 2017 Oct.
[Is] ISSN:1553-7358
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Autophagy is a physiological process for the recycling and degradation of cellular materials. Forming the autophagosome from the phagophore, a cup-shaped double-membrane vesicle, is a critical step in autophagy. The origin of the cup shape of the phagophore is poorly understood. In yeast, fusion of a small number of Atg9-containing vesicles is considered a key step in autophagosome biogenesis, aided by Atg1 complexes (ULK1 in mammals) localized at the preautophagosomal structure (PAS). In particular, the S-shaped Atg17-Atg31-Atg29 subcomplex of Atg1 is critical for phagophore nucleation at the PAS. To study this process, we simulated membrane remodeling processes in the presence and absence of membrane associated Atg17. We show that at least three vesicles need to fuse to induce the phagophore shape, consistent with experimental observations. However, fusion alone is not sufficient. Interactions with 34-nm long, S-shaped Atg17 complexes are required to overcome a substantial kinetic barrier in the transition to the cup-shaped phagophore. Our finding rationalizes the recruitment of Atg17 complexes to the yeast PAS, and their unusual shape. In control simulations without Atg17, with weakly binding Atg17, or with straight instead of S-shaped Atg17, the membrane shape transition did not occur. We confirm the critical role of Atg17-membrane interactions experimentally by showing that mutations of putative membrane interaction sites result in reduction or loss of autophagic activity in yeast. Fusion of a small number of vesicles followed by Atg17-guided membrane shape-remodeling thus emerges as a viable route to phagophore formation.
[Mh] Termos MeSH primário: Autofagossomos/química
Autofagossomos/ultraestrutura
Proteínas Relacionadas à Autofagia/química
Proteínas Relacionadas à Autofagia/ultraestrutura
Autofagia
Membrana Celular/química
Membrana Celular/ultraestrutura
Proteínas de Saccharomyces cerevisiae/química
Proteínas de Saccharomyces cerevisiae/ultraestrutura
[Mh] Termos MeSH secundário: Sítios de Ligação
Simulação por Computador
Fluidez de Membrana
Fusão de Membrana
Modelos Químicos
Modelos Moleculares
Ligação Proteica
Conformação Proteica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Atg17 protein, S cerevisiae); 0 (Autophagy-Related Proteins); 0 (Saccharomyces cerevisiae Proteins)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171119
[Lr] Data última revisão:
171119
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171025
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pcbi.1005817


  10 / 7544 MEDLINE  
              first record previous record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28956592
[Au] Autor:Sousa IP; Carvalho CAM; Mendes YS; Weissmuller G; Oliveira AC; Gomes AMO
[Ad] Endereço:Instituto de Bioquímica Médica Leopoldo de Meis, Centro de Ciências da Saúde and ‡Instituto de Biofísica Carlos Chagas Filho, Centro de Ciências da Saúde, Universidade Federal do Rio de Janeiro , Rio de Janeiro, Rio de Janeiro 21941-902, Brazil.
[Ti] Título:Fusion of a New World Alphavirus with Membrane Microdomains Involving Partially Reversible Conformational Changes in the Viral Spike Proteins.
[So] Source:Biochemistry;56(43):5823-5830, 2017 Oct 31.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Alphaviruses are enveloped arboviruses mainly proposed to infect host cells by receptor-mediated endocytosis followed by fusion between the viral envelope and the endosomal membrane. The fusion reaction is triggered by low pH and requires the presence of both cholesterol and sphingolipids in the target membrane, suggesting the involvement of lipid rafts in the cell entry mechanism. In this study, we show for the first time the interaction of an enveloped virus with membrane microdomains isolated from living cells. Using Mayaro virus (MAYV), a New World alphavirus, we verified that virus fusion to these domains occurred to a significant extent upon acidification, although its kinetics was quite slow when compared to that of fusion with artificial liposomes demonstrated in a previous work. Surprisingly, when virus was previously exposed to acidic pH, a condition previously shown to inhibit alphavirus binding and fusion to target membranes as well as infectivity, and then reneutralized, its ability to fuse with membrane microdomains at low pH was retained. Interestingly, this observation correlated with a partial reversion of low pH-induced conformational changes in viral proteins and retention of virus infectivity upon reneutralization. Our results suggest that MAYV entry into host cells could alternatively involve internalization via lipid rafts and that the conformational changes triggered by low pH in the viral spike proteins during the entry process are partially reversible.
[Mh] Termos MeSH primário: Alphavirus/química
Lipossomos/química
Fusão de Membrana
Microdomínios da Membrana/química
Proteínas Virais de Fusão/química
Internalização do Vírus
[Mh] Termos MeSH secundário: Alphavirus/metabolismo
Concentração de Íons de Hidrogênio
Microdomínios da Membrana/metabolismo
Proteínas Virais de Fusão/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Liposomes); 0 (Viral Fusion Proteins)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171103
[Lr] Data última revisão:
171103
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170929
[St] Status:MEDLINE
[do] DOI:10.1021/acs.biochem.7b00650



página 1 de 755 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