The shift from low to high non-structural protein 1 expression in rotavirus-infected MA-104 cells

Detalhes bibliográficos
Autor(a) principal: Martinez-Alvarez,Laura
Data de Publicação: 2013
Outros Autores: Pina-Vazquez,Carolina, Zarco,Wilbert, Padilla-Noriega,Luis
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Memórias do Instituto Oswaldo Cruz
Texto Completo: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0074-02762013000400421
Resumo: A hallmark of group/species A rotavirus (RVA) replication in MA-104 cells is the logarithmic increase in viral mRNAs that occurs four-12 h post-infection. Viral protein synthesis typically lags closely behind mRNA synthesis but continues after mRNA levels plateau. However, RVA non-structural protein 1 (NSP1) is present at very low levels throughout viral replication despite showing robust protein synthesis. NSP1 has the contrasting properties of being susceptible to proteasomal degradation, but being stabilised against proteasomal degradation by viral proteins and/or viral mRNAs. We aimed to determine the kinetics of the accumulation and intracellular distribution of NSP1 in MA-104 cells infected with rhesus rotavirus (RRV). NSP1 preferentially localises to the perinuclear region of the cytoplasm of infected cells, forming abundant granules that are heterogeneous in size. Late in infection, large NSP1 granules predominate, coincident with a shift from low to high NSP1 expression levels. Our results indicate that rotavirus NSP1 is a late viral protein in MA-104 cells infected with RRV, presumably as a result of altered protein turnover.
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spelling The shift from low to high non-structural protein 1 expression in rotavirus-infected MA-104 cellsrotavirusgene expressioninterferons type 1proteasome endopeptidase complexubiquitin protein ligasesA hallmark of group/species A rotavirus (RVA) replication in MA-104 cells is the logarithmic increase in viral mRNAs that occurs four-12 h post-infection. Viral protein synthesis typically lags closely behind mRNA synthesis but continues after mRNA levels plateau. However, RVA non-structural protein 1 (NSP1) is present at very low levels throughout viral replication despite showing robust protein synthesis. NSP1 has the contrasting properties of being susceptible to proteasomal degradation, but being stabilised against proteasomal degradation by viral proteins and/or viral mRNAs. We aimed to determine the kinetics of the accumulation and intracellular distribution of NSP1 in MA-104 cells infected with rhesus rotavirus (RRV). NSP1 preferentially localises to the perinuclear region of the cytoplasm of infected cells, forming abundant granules that are heterogeneous in size. Late in infection, large NSP1 granules predominate, coincident with a shift from low to high NSP1 expression levels. Our results indicate that rotavirus NSP1 is a late viral protein in MA-104 cells infected with RRV, presumably as a result of altered protein turnover.Instituto Oswaldo Cruz, Ministério da Saúde2013-06-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://www.scielo.br/scielo.php?script=sci_arttext&pid=S0074-02762013000400421Memórias do Instituto Oswaldo Cruz v.108 n.4 2013reponame:Memórias do Instituto Oswaldo Cruzinstname:Fundação Oswaldo Cruzinstacron:FIOCRUZ10.1590/S0074-0276108042013005info:eu-repo/semantics/openAccessMartinez-Alvarez,LauraPina-Vazquez,CarolinaZarco,WilbertPadilla-Noriega,Luiseng2020-04-25T17:51:32Zhttp://www.scielo.br/oai/scielo-oai.php0074-02761678-8060opendoar:null2020-04-26 02:19:00.858Memórias do Instituto Oswaldo Cruz - Fundação Oswaldo Cruztrue
dc.title.none.fl_str_mv The shift from low to high non-structural protein 1 expression in rotavirus-infected MA-104 cells
title The shift from low to high non-structural protein 1 expression in rotavirus-infected MA-104 cells
spellingShingle The shift from low to high non-structural protein 1 expression in rotavirus-infected MA-104 cells
Martinez-Alvarez,Laura
rotavirus
gene expression
interferons type 1
proteasome endopeptidase complex
ubiquitin protein ligases
title_short The shift from low to high non-structural protein 1 expression in rotavirus-infected MA-104 cells
title_full The shift from low to high non-structural protein 1 expression in rotavirus-infected MA-104 cells
title_fullStr The shift from low to high non-structural protein 1 expression in rotavirus-infected MA-104 cells
title_full_unstemmed The shift from low to high non-structural protein 1 expression in rotavirus-infected MA-104 cells
title_sort The shift from low to high non-structural protein 1 expression in rotavirus-infected MA-104 cells
author Martinez-Alvarez,Laura
author_facet Martinez-Alvarez,Laura
Pina-Vazquez,Carolina
Zarco,Wilbert
Padilla-Noriega,Luis
author_role author
author2 Pina-Vazquez,Carolina
Zarco,Wilbert
Padilla-Noriega,Luis
author2_role author
author
author
dc.contributor.author.fl_str_mv Martinez-Alvarez,Laura
Pina-Vazquez,Carolina
Zarco,Wilbert
Padilla-Noriega,Luis
dc.subject.por.fl_str_mv rotavirus
gene expression
interferons type 1
proteasome endopeptidase complex
ubiquitin protein ligases
topic rotavirus
gene expression
interferons type 1
proteasome endopeptidase complex
ubiquitin protein ligases
dc.description.none.fl_txt_mv A hallmark of group/species A rotavirus (RVA) replication in MA-104 cells is the logarithmic increase in viral mRNAs that occurs four-12 h post-infection. Viral protein synthesis typically lags closely behind mRNA synthesis but continues after mRNA levels plateau. However, RVA non-structural protein 1 (NSP1) is present at very low levels throughout viral replication despite showing robust protein synthesis. NSP1 has the contrasting properties of being susceptible to proteasomal degradation, but being stabilised against proteasomal degradation by viral proteins and/or viral mRNAs. We aimed to determine the kinetics of the accumulation and intracellular distribution of NSP1 in MA-104 cells infected with rhesus rotavirus (RRV). NSP1 preferentially localises to the perinuclear region of the cytoplasm of infected cells, forming abundant granules that are heterogeneous in size. Late in infection, large NSP1 granules predominate, coincident with a shift from low to high NSP1 expression levels. Our results indicate that rotavirus NSP1 is a late viral protein in MA-104 cells infected with RRV, presumably as a result of altered protein turnover.
description A hallmark of group/species A rotavirus (RVA) replication in MA-104 cells is the logarithmic increase in viral mRNAs that occurs four-12 h post-infection. Viral protein synthesis typically lags closely behind mRNA synthesis but continues after mRNA levels plateau. However, RVA non-structural protein 1 (NSP1) is present at very low levels throughout viral replication despite showing robust protein synthesis. NSP1 has the contrasting properties of being susceptible to proteasomal degradation, but being stabilised against proteasomal degradation by viral proteins and/or viral mRNAs. We aimed to determine the kinetics of the accumulation and intracellular distribution of NSP1 in MA-104 cells infected with rhesus rotavirus (RRV). NSP1 preferentially localises to the perinuclear region of the cytoplasm of infected cells, forming abundant granules that are heterogeneous in size. Late in infection, large NSP1 granules predominate, coincident with a shift from low to high NSP1 expression levels. Our results indicate that rotavirus NSP1 is a late viral protein in MA-104 cells infected with RRV, presumably as a result of altered protein turnover.
publishDate 2013
dc.date.none.fl_str_mv 2013-06-01
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://www.scielo.br/scielo.php?script=sci_arttext&pid=S0074-02762013000400421
url http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0074-02762013000400421
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 10.1590/S0074-0276108042013005
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 Instituto Oswaldo Cruz, Ministério da Saúde
publisher.none.fl_str_mv Instituto Oswaldo Cruz, Ministério da Saúde
dc.source.none.fl_str_mv Memórias do Instituto Oswaldo Cruz v.108 n.4 2013
reponame:Memórias do Instituto Oswaldo Cruz
instname:Fundação Oswaldo Cruz
instacron:FIOCRUZ
reponame_str Memórias do Instituto Oswaldo Cruz
collection Memórias do Instituto Oswaldo Cruz
instname_str Fundação Oswaldo Cruz
instacron_str FIOCRUZ
institution FIOCRUZ
repository.name.fl_str_mv Memórias do Instituto Oswaldo Cruz - Fundação Oswaldo Cruz
repository.mail.fl_str_mv
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