Base de dados : LILACS
Pesquisa : D12.776.543.512.500 [Categoria DeCS]
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Texto completo
Id: lil-634520
Autor: Peralta, A.; Molinari, M. P.; Taboga, O..
Título: Baculovirus recombinantes como inmunógenos
Fonte: Rev. argent. microbiol;38(2):74-74, ene.-abr. 2006. ilus.
Idioma: es.
Descritores: Baculoviridae/imunologia
Moléculas de Adesão Celular/imunologia
Glicoproteínas de Membrana/imunologia
Proteínas Recombinantes de Fusão/imunologia
Proteínas Virais/imunologia
Vacinas Virais/imunologia
-Anticorpos Antivirais
Proteínas Virais de Fusão
Responsável: AR1.2 - Instituto de Investigaciónes Epidemiológicas

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Texto completo SciELO Brasil
Texto completo
Id: lil-402669
Autor: Da Poian, A. T; Carneiro, F. A; Stauffer, F.
Título: Viral membrane fusion: is glycoprotein G of rhabdoviruses a representative of a new class of viral fusion proteins?
Fonte: Braz. j. med. biol. res = Rev. bras. pesqui. méd. biol;38(6):813-823, June 2005. ilus, tab.
Idioma: en.
Conferência: Apresentado em: Congresso Brasileiro de Biologia Celular, 11, Campinas, July 15-18, 2004.
Resumo: Enveloped viruses always gain entry into the cytoplasm by fusion of their lipid envelope with a cell membrane. Some enveloped viruses fuse directly with the host cell plasma membrane after virus binding to the cell receptor. Other enveloped viruses enter the cells by the endocytic pathway, and fusion depends on the acidification of the endosomal compartment. In both cases, virus-induced membrane fusion is triggered by conformational changes in viral envelope glycoproteins. Two different classes of viral fusion proteins have been described on the basis of their molecular architecture. Several structural data permitted the elucidation of the mechanisms of membrane fusion mediated by class I and class II fusion proteins. In this article, we review a number of results obtained by our laboratory and by others that suggest that the mechanisms involved in rhabdovirus fusion are different from those used by the two well-studied classes of viral glycoproteins. We focus our discussion on the electrostatic nature of virus binding and interaction with membranes, especially through phosphatidylserine, and on the reversibility of the conformational changes of the rhabdovirus glycoprotein involved in fusion. Taken together, these data suggest the existence of a third class of fusion proteins and support the idea that new insights should emerge from studies of membrane fusion mediated by the G protein of rhabdoviruses. In particular, the elucidation of the three-dimensional structure of the G protein or even of the fusion peptide at different pH's might provide valuable information for understanding the fusion mechanism of this new class of fusion proteins.
Descritores: Glicoproteínas/fisiologia
Fusão de Membrana/fisiologia
Proteínas Virais de Fusão/fisiologia
-Proteínas de Ligação ao GTP/fisiologia
Glicoproteínas de Membrana/fisiologia
Limites: Animais
Tipo de Publ: Revisão
Responsável: BR1.1 - BIREME

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Id: lil-245445
Autor: Volberding, Paul.
Título: Resistencia del virus de inmunodeficiencia humana a los fármacos antiretrovirales: cómo enfrentarla / Antiretroviral resistance of HIV: how to deal with it
Fonte: Rev. chil. infectol;15(3):149-53, 1998.
Idioma: es.
Descritores: Fármacos Anti-HIV/administração & dosagem
Resistência a Medicamentos
HIV/efeitos dos fármacos
Combinação de Medicamentos
Hidroxiureia/uso terapêutico
Inibidores de Integrase/uso terapêutico
Inibidores de Proteases/farmacocinética
Inibidores da Transcriptase Reversa/uso terapêutico
Proteínas Virais de Fusão/antagonistas & inibidores
Limites: Humanos
Tipo de Publ: Aula
Responsável: CL1.1 - Biblioteca Central

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Texto completo SciELO Brasil
Couceiro, J. N. S. S
Texto completo
Id: lil-212584
Autor: Barbosa, A. T. C; Luiz, M. O; Gusmäo, N. P; Couceiro, J. N. S. S.
Título: Analysis of viral and cellular parameters which affect the fusion process of influenza viruses
Fonte: Braz. j. med. biol. res = Rev. bras. pesqui. méd. biol;30(12):1415-20, Dec. 1997. tab, graf.
Idioma: en.
Resumo: In the present investigation we studied the fusogenic process developed by influenza A, B and C viruses on cell surfaces and different factors associated with virus and cell membrane structures. The biological activity of purified virus strains was evaluated in hemagglutination, sialidase and fusion assays. Hemolysis by influenza A, B and C viruses ranging from 77.4 to 97.2 percent, from 20.0 to 65.0 percent, from 0.2 to 93.7 percent and from 9.0 to 76.1 percent was observed when human, chicken, rabbit and monkey erythrocytes, respectively, were tested at pH 5.5. At this pH, low hemolysis indexes for influenza A, B and C viruses were observed if horse erythrocytes were used as target cells for the fusion process, which could be explained by an inefficient receptor binding activity of influenza on N-glycolyl sialic acids. Differences in hemaglutinin receptor binding activity due to its specificity to N-acetyl or N-glycolyl cell surface oligosaccharides, density of these cellular receptors and level of negative charges on the cell surface may possibly explain these results, showing influence on the sialidase activity and the fusogenic process. Comparative analysis showed a lack of dependence between the sialidase and fusion activities developed by influenza B viruses. Influenza A viruses at low sialidase titers (<2) also exhibited clearly low hemolysis at pH 5.5 (15.8 percent), while influenza B viruses with similarly low sialidase titers showed highly variable hemolysis indexes (0.2 to 78.0 percent). These results support the idea that different virus and cell-associated factors such as those presented above have a significant effect on the multifactorial fusion process.
Descritores: Vírus da Influenza A/patogenicidade
Vírus da Influenza B/patogenicidade
Influenzavirus C/patogenicidade
Fusão de Membrana/imunologia
Glicoproteínas de Membrana
Vírus da Parainfluenza 1 Humana/patogenicidade
Proteínas Virais de Fusão
Membrana Eritrocítica
Influenza Humana/fisiopatologia
Ácido N-Acetilneuramínico
Ácidos Siálicos
Limites: Coelhos
Tipo de Publ: Estudo Comparativo
Research Support, Non-U.S. Gov't
Responsável: BR1.1 - BIREME

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Rossetti, M. L. R
Zaha, A
Id: lil-148711
Autor: Rossetti, M. L. R; Raupp, R. M; Farias, S. E; Ferreira, L. F. C; Zaha, A.
Título: Expression of the VP3-VP1 sequence of foot-and-mouth disease virus in Escherichia coli
Fonte: Braz. j. med. biol. res = Rev. bras. pesqui. méd. biol;26(6):591-603, Jun. 1993. ilus.
Idioma: en.
Resumo: 1. cDNA recombinants containing the VP3 and VP1 sequences of foot-and-mouth disease virus were isolated and the VP3-VP1 sequence was reconstructed. 2. The reconstructed VP3-VP1 sequence was subcloned into expression vector pEX31b and a fusion protein of about 62,000 Da was expressed. 3. When injected into mice, the fusion protein was able to elicit the production of antibodies that recognized viral VP1 and VP3. 4. Antibodies present in sera from mice immunized with VP3-VP1 protein did not neutralize the foot-and-mouth disease virus in vitro
Descritores: Anticorpos Antivirais/biossíntese
Escherichia coli/genética
Proteínas Virais de Fusão/isolamento & purificação
Western Blotting
Capsídeo/isolamento & purificação
Ensaio de Imunoadsorção Enzimática
Testes de Neutralização
Proteínas Virais de Fusão/genética
Proteínas Virais de Fusão/imunologia
Limites: Animais
Responsável: BR1.1 - BIREME

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