Partial fusion activity of influenza virus toward liposomes and erythrocyte ghosts is distinct from viral inactivation

Detalhes bibliográficos
Autor(a) principal: Ramalho-Santos, João
Data de Publicação: 1996
Outros Autores: Lima, Maria C. Pedroso de, Nir, Shlomo
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: http://hdl.handle.net/10316/12629
https://doi.org/10.1074/jbc.271.39.23902
Resumo: Final extents of fusion of influenza virus (A/PR/8/34 strain) with neutral and partially acidic liposomes were monitored with (i) a fluorescence resonance energy-transfer assay in which the liposomes were labeled and (ii) by the dequenching of octadecylrhodamine, initially incorporated in the viral membrane. The latter assay was also employed in the fusion of influenza virus and Sendai virus with erythrocyte ghosts. In all cases, a phenomenon of partial fusion activity of the virus was observed, which is distinct from low pH inactivation. The unfused influenza or Sendai virions, which were separated by sucrose gradient centrifugation from liposomes or erythrocyte ghosts exhibited again partial fusion activity toward freshly added liposomes or ghosts, respectively. The conclusion is that the fraction of initially bound and unfused virions does not consist of defective particles, but rather of particles bound to the target membranes via inactive sites on the virus (or on cellular membranes), or else, partial fusion activity is a manifestation of a certain probability of production of fusion inactive sites by irreversible association of viral glycoproteins or peptides in the target membrane
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spelling Partial fusion activity of influenza virus toward liposomes and erythrocyte ghosts is distinct from viral inactivationFinal extents of fusion of influenza virus (A/PR/8/34 strain) with neutral and partially acidic liposomes were monitored with (i) a fluorescence resonance energy-transfer assay in which the liposomes were labeled and (ii) by the dequenching of octadecylrhodamine, initially incorporated in the viral membrane. The latter assay was also employed in the fusion of influenza virus and Sendai virus with erythrocyte ghosts. In all cases, a phenomenon of partial fusion activity of the virus was observed, which is distinct from low pH inactivation. The unfused influenza or Sendai virions, which were separated by sucrose gradient centrifugation from liposomes or erythrocyte ghosts exhibited again partial fusion activity toward freshly added liposomes or ghosts, respectively. The conclusion is that the fraction of initially bound and unfused virions does not consist of defective particles, but rather of particles bound to the target membranes via inactive sites on the virus (or on cellular membranes), or else, partial fusion activity is a manifestation of a certain probability of production of fusion inactive sites by irreversible association of viral glycoproteins or peptides in the target membraneThe American Society for Biochemistry and Molecular Biology1996-09-27info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articlehttp://hdl.handle.net/10316/12629http://hdl.handle.net/10316/12629https://doi.org/10.1074/jbc.271.39.23902engThe Journal of Biological Chemistry. 271:39 (1996) 23902-239060021-9258Ramalho-Santos, JoãoLima, Maria C. Pedroso deNir, Shlomoinfo:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2021-09-17T11:05:01Zoai:estudogeral.uc.pt:10316/12629Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T20:55:40.833951Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse
dc.title.none.fl_str_mv Partial fusion activity of influenza virus toward liposomes and erythrocyte ghosts is distinct from viral inactivation
title Partial fusion activity of influenza virus toward liposomes and erythrocyte ghosts is distinct from viral inactivation
spellingShingle Partial fusion activity of influenza virus toward liposomes and erythrocyte ghosts is distinct from viral inactivation
Ramalho-Santos, João
title_short Partial fusion activity of influenza virus toward liposomes and erythrocyte ghosts is distinct from viral inactivation
title_full Partial fusion activity of influenza virus toward liposomes and erythrocyte ghosts is distinct from viral inactivation
title_fullStr Partial fusion activity of influenza virus toward liposomes and erythrocyte ghosts is distinct from viral inactivation
title_full_unstemmed Partial fusion activity of influenza virus toward liposomes and erythrocyte ghosts is distinct from viral inactivation
title_sort Partial fusion activity of influenza virus toward liposomes and erythrocyte ghosts is distinct from viral inactivation
author Ramalho-Santos, João
author_facet Ramalho-Santos, João
Lima, Maria C. Pedroso de
Nir, Shlomo
author_role author
author2 Lima, Maria C. Pedroso de
Nir, Shlomo
author2_role author
author
dc.contributor.author.fl_str_mv Ramalho-Santos, João
Lima, Maria C. Pedroso de
Nir, Shlomo
description Final extents of fusion of influenza virus (A/PR/8/34 strain) with neutral and partially acidic liposomes were monitored with (i) a fluorescence resonance energy-transfer assay in which the liposomes were labeled and (ii) by the dequenching of octadecylrhodamine, initially incorporated in the viral membrane. The latter assay was also employed in the fusion of influenza virus and Sendai virus with erythrocyte ghosts. In all cases, a phenomenon of partial fusion activity of the virus was observed, which is distinct from low pH inactivation. The unfused influenza or Sendai virions, which were separated by sucrose gradient centrifugation from liposomes or erythrocyte ghosts exhibited again partial fusion activity toward freshly added liposomes or ghosts, respectively. The conclusion is that the fraction of initially bound and unfused virions does not consist of defective particles, but rather of particles bound to the target membranes via inactive sites on the virus (or on cellular membranes), or else, partial fusion activity is a manifestation of a certain probability of production of fusion inactive sites by irreversible association of viral glycoproteins or peptides in the target membrane
publishDate 1996
dc.date.none.fl_str_mv 1996-09-27
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
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status_str publishedVersion
dc.identifier.uri.fl_str_mv http://hdl.handle.net/10316/12629
http://hdl.handle.net/10316/12629
https://doi.org/10.1074/jbc.271.39.23902
url http://hdl.handle.net/10316/12629
https://doi.org/10.1074/jbc.271.39.23902
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv The Journal of Biological Chemistry. 271:39 (1996) 23902-23906
0021-9258
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dc.publisher.none.fl_str_mv The American Society for Biochemistry and Molecular Biology
publisher.none.fl_str_mv The American Society for Biochemistry and Molecular Biology
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