In vivo interaction of the hepatitis delta virus small antigen with the ELAV-like protein HuR

Detalhes bibliográficos
Autor(a) principal: Casaca, Ana
Data de Publicação: 2011
Outros Autores: Fardilha, Margarida, Silva, Edgar da Cruz e, Cunha, Celso
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: http://hdl.handle.net/10773/29317
Resumo: The small and large delta antigens (S-HDAg and L-HDAg, respectively) represent two forms of the only protein encoded by the hepatitis delta virus (HDV) RNA genome. Consequently, HDV relies, at a large extent, on the host cell machinery for replication and transcription. Until now, only a limited number of cellular proteins were identified as S-HDAg or L-HDAg partners being involved in the modulation of the virus life cycle. In an attempt to identify cellular S-HDAg-binding proteins we made use of a yeast two-hybrid approach to screen a human liver cDNA library. We were able to identify HuR, a ubiquitously expressed protein involved in RNA stabilization, as an S-HDAg partner both in vitro and in vivo. HuR was found to be overexpressed and colocalize with HDAg in human hepatoma cells. siRNA knockdown of HuR mRNA resulted in inhibition of S-HDAg and L-HDAg expression.
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spelling In vivo interaction of the hepatitis delta virus small antigen with the ELAV-like protein HuRHepatitis delta virusDelta antigenYeast two-hybridHuRThe small and large delta antigens (S-HDAg and L-HDAg, respectively) represent two forms of the only protein encoded by the hepatitis delta virus (HDV) RNA genome. Consequently, HDV relies, at a large extent, on the host cell machinery for replication and transcription. Until now, only a limited number of cellular proteins were identified as S-HDAg or L-HDAg partners being involved in the modulation of the virus life cycle. In an attempt to identify cellular S-HDAg-binding proteins we made use of a yeast two-hybrid approach to screen a human liver cDNA library. We were able to identify HuR, a ubiquitously expressed protein involved in RNA stabilization, as an S-HDAg partner both in vitro and in vivo. HuR was found to be overexpressed and colocalize with HDAg in human hepatoma cells. siRNA knockdown of HuR mRNA resulted in inhibition of S-HDAg and L-HDAg expression.Bentham Open2020-09-29T14:25:48Z2011-01-01T00:00:00Z2011info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10773/29317eng1874-357910.2174/1874357901105010012Casaca, AnaFardilha, MargaridaSilva, Edgar da Cruz eCunha, Celsoinfo: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:RCAAP2024-02-22T11:56:43Zoai:ria.ua.pt:10773/29317Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-20T03:01:41.184825Repositório 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 In vivo interaction of the hepatitis delta virus small antigen with the ELAV-like protein HuR
title In vivo interaction of the hepatitis delta virus small antigen with the ELAV-like protein HuR
spellingShingle In vivo interaction of the hepatitis delta virus small antigen with the ELAV-like protein HuR
Casaca, Ana
Hepatitis delta virus
Delta antigen
Yeast two-hybrid
HuR
title_short In vivo interaction of the hepatitis delta virus small antigen with the ELAV-like protein HuR
title_full In vivo interaction of the hepatitis delta virus small antigen with the ELAV-like protein HuR
title_fullStr In vivo interaction of the hepatitis delta virus small antigen with the ELAV-like protein HuR
title_full_unstemmed In vivo interaction of the hepatitis delta virus small antigen with the ELAV-like protein HuR
title_sort In vivo interaction of the hepatitis delta virus small antigen with the ELAV-like protein HuR
author Casaca, Ana
author_facet Casaca, Ana
Fardilha, Margarida
Silva, Edgar da Cruz e
Cunha, Celso
author_role author
author2 Fardilha, Margarida
Silva, Edgar da Cruz e
Cunha, Celso
author2_role author
author
author
dc.contributor.author.fl_str_mv Casaca, Ana
Fardilha, Margarida
Silva, Edgar da Cruz e
Cunha, Celso
dc.subject.por.fl_str_mv Hepatitis delta virus
Delta antigen
Yeast two-hybrid
HuR
topic Hepatitis delta virus
Delta antigen
Yeast two-hybrid
HuR
description The small and large delta antigens (S-HDAg and L-HDAg, respectively) represent two forms of the only protein encoded by the hepatitis delta virus (HDV) RNA genome. Consequently, HDV relies, at a large extent, on the host cell machinery for replication and transcription. Until now, only a limited number of cellular proteins were identified as S-HDAg or L-HDAg partners being involved in the modulation of the virus life cycle. In an attempt to identify cellular S-HDAg-binding proteins we made use of a yeast two-hybrid approach to screen a human liver cDNA library. We were able to identify HuR, a ubiquitously expressed protein involved in RNA stabilization, as an S-HDAg partner both in vitro and in vivo. HuR was found to be overexpressed and colocalize with HDAg in human hepatoma cells. siRNA knockdown of HuR mRNA resulted in inhibition of S-HDAg and L-HDAg expression.
publishDate 2011
dc.date.none.fl_str_mv 2011-01-01T00:00:00Z
2011
2020-09-29T14:25:48Z
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/10773/29317
url http://hdl.handle.net/10773/29317
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 1874-3579
10.2174/1874357901105010012
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dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Bentham Open
publisher.none.fl_str_mv Bentham Open
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instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
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reponame_str Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
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