Partial fusion activity of influenza virus toward liposomes and erythrocyte ghosts is distinct from viral inactivation
Autor(a) principal: | |
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Data de Publicação: | 1996 |
Outros Autores: | , |
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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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 |
format |
article |
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 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
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 |
dc.source.none.fl_str_mv |
reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação instacron:RCAAP |
instname_str |
Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
instacron_str |
RCAAP |
institution |
RCAAP |
reponame_str |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
collection |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
repository.name.fl_str_mv |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
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1799133843276431360 |