INHIBITION OF MAYARO VIRUS REPLICATION BY PROSTAGLANDIN A1 IN Aedes albopictus CELLS
Autor(a) principal: | |
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Data de Publicação: | 1998 |
Outros Autores: | |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Revista de Microbiologia |
Texto Completo: | http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0001-37141998000300013 |
Resumo: | Prostaglandin A1 (PGA1) inhibits Mayaro virus replication in Aedes albopictus cells at nontoxic doses to uninfected cells. At 10 µg/ml, PGA1 decreases virus production by 90%. The presence of PGA1 during virus adsorption, with no treatment after infection, reduces virus yield by 41%. Antiviral activity is observed even when treatment starts at one or two hours post-infection. However, in cells pre-treated with PGA1 during 24 hours, virus replication is not impaired. Thus, events ocurring during initial stages of infection and after virus adsorption and penetration must be the target of PGA1 action. SDS-PAGE analysis of 35S-methionine labelled proteins shows that PGA1 inhibits the synthesis of viral proteins and induces the synthesis of polypeptides with molecular weight of 70 kDa, 57 kDa and 23 kDa. In cells pre-treated with actinomycin D the induction of those proteins is suppressed. In addition, actinomycin D treatment prevents PGA1antiviral activity, indicating that PGA1-induced stress proteins are probably involved in this mechanism. |
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INHIBITION OF MAYARO VIRUS REPLICATION BY PROSTAGLANDIN A1 IN Aedes albopictus CELLSMayaro virusProstaglandinAedes albopictus cellsHeat-shock proteinsActinomycin DProstaglandin A1 (PGA1) inhibits Mayaro virus replication in Aedes albopictus cells at nontoxic doses to uninfected cells. At 10 µg/ml, PGA1 decreases virus production by 90%. The presence of PGA1 during virus adsorption, with no treatment after infection, reduces virus yield by 41%. Antiviral activity is observed even when treatment starts at one or two hours post-infection. However, in cells pre-treated with PGA1 during 24 hours, virus replication is not impaired. Thus, events ocurring during initial stages of infection and after virus adsorption and penetration must be the target of PGA1 action. SDS-PAGE analysis of 35S-methionine labelled proteins shows that PGA1 inhibits the synthesis of viral proteins and induces the synthesis of polypeptides with molecular weight of 70 kDa, 57 kDa and 23 kDa. In cells pre-treated with actinomycin D the induction of those proteins is suppressed. In addition, actinomycin D treatment prevents PGA1antiviral activity, indicating that PGA1-induced stress proteins are probably involved in this mechanism.Sociedade Brasileira de Microbiologia1998-09-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S0001-37141998000300013Revista de Microbiologia v.29 n.3 1998reponame:Revista de Microbiologiainstname:Sociedade Brasileira de Microbiologia (SBM)instacron:SBM10.1590/S0001-37141998000300013info:eu-repo/semantics/openAccessBarbosa,Joel AntonioRebello,Moacyr Alcoforadoeng1999-02-26T00:00:00Zoai:scielo:S0001-37141998000300013Revistahttps://www.scielo.br/j/rm/ONGhttps://old.scielo.br/oai/scielo-oai.phpbjm@sbmicrobiologia.org.br||revmicro@icb.usp.br0001-37140001-3714opendoar:1999-02-26T00:00Revista de Microbiologia - Sociedade Brasileira de Microbiologia (SBM)false |
dc.title.none.fl_str_mv |
INHIBITION OF MAYARO VIRUS REPLICATION BY PROSTAGLANDIN A1 IN Aedes albopictus CELLS |
title |
INHIBITION OF MAYARO VIRUS REPLICATION BY PROSTAGLANDIN A1 IN Aedes albopictus CELLS |
spellingShingle |
INHIBITION OF MAYARO VIRUS REPLICATION BY PROSTAGLANDIN A1 IN Aedes albopictus CELLS Barbosa,Joel Antonio Mayaro virus Prostaglandin Aedes albopictus cells Heat-shock proteins Actinomycin D |
title_short |
INHIBITION OF MAYARO VIRUS REPLICATION BY PROSTAGLANDIN A1 IN Aedes albopictus CELLS |
title_full |
INHIBITION OF MAYARO VIRUS REPLICATION BY PROSTAGLANDIN A1 IN Aedes albopictus CELLS |
title_fullStr |
INHIBITION OF MAYARO VIRUS REPLICATION BY PROSTAGLANDIN A1 IN Aedes albopictus CELLS |
title_full_unstemmed |
INHIBITION OF MAYARO VIRUS REPLICATION BY PROSTAGLANDIN A1 IN Aedes albopictus CELLS |
title_sort |
INHIBITION OF MAYARO VIRUS REPLICATION BY PROSTAGLANDIN A1 IN Aedes albopictus CELLS |
author |
Barbosa,Joel Antonio |
author_facet |
Barbosa,Joel Antonio Rebello,Moacyr Alcoforado |
author_role |
author |
author2 |
Rebello,Moacyr Alcoforado |
author2_role |
author |
dc.contributor.author.fl_str_mv |
Barbosa,Joel Antonio Rebello,Moacyr Alcoforado |
dc.subject.por.fl_str_mv |
Mayaro virus Prostaglandin Aedes albopictus cells Heat-shock proteins Actinomycin D |
topic |
Mayaro virus Prostaglandin Aedes albopictus cells Heat-shock proteins Actinomycin D |
description |
Prostaglandin A1 (PGA1) inhibits Mayaro virus replication in Aedes albopictus cells at nontoxic doses to uninfected cells. At 10 µg/ml, PGA1 decreases virus production by 90%. The presence of PGA1 during virus adsorption, with no treatment after infection, reduces virus yield by 41%. Antiviral activity is observed even when treatment starts at one or two hours post-infection. However, in cells pre-treated with PGA1 during 24 hours, virus replication is not impaired. Thus, events ocurring during initial stages of infection and after virus adsorption and penetration must be the target of PGA1 action. SDS-PAGE analysis of 35S-methionine labelled proteins shows that PGA1 inhibits the synthesis of viral proteins and induces the synthesis of polypeptides with molecular weight of 70 kDa, 57 kDa and 23 kDa. In cells pre-treated with actinomycin D the induction of those proteins is suppressed. In addition, actinomycin D treatment prevents PGA1antiviral activity, indicating that PGA1-induced stress proteins are probably involved in this mechanism. |
publishDate |
1998 |
dc.date.none.fl_str_mv |
1998-09-01 |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0001-37141998000300013 |
url |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0001-37141998000300013 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
10.1590/S0001-37141998000300013 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
text/html |
dc.publisher.none.fl_str_mv |
Sociedade Brasileira de Microbiologia |
publisher.none.fl_str_mv |
Sociedade Brasileira de Microbiologia |
dc.source.none.fl_str_mv |
Revista de Microbiologia v.29 n.3 1998 reponame:Revista de Microbiologia instname:Sociedade Brasileira de Microbiologia (SBM) instacron:SBM |
instname_str |
Sociedade Brasileira de Microbiologia (SBM) |
instacron_str |
SBM |
institution |
SBM |
reponame_str |
Revista de Microbiologia |
collection |
Revista de Microbiologia |
repository.name.fl_str_mv |
Revista de Microbiologia - Sociedade Brasileira de Microbiologia (SBM) |
repository.mail.fl_str_mv |
bjm@sbmicrobiologia.org.br||revmicro@icb.usp.br |
_version_ |
1754821030142017536 |