Influenza A virus ribonucleoproteins modulate host recycling by competing with Rab11 effectors.
Identifieur interne : 000549 ( PubMed/Corpus ); précédent : 000548; suivant : 000550Influenza A virus ribonucleoproteins modulate host recycling by competing with Rab11 effectors.
Auteurs : Sílvia Vale-Costa ; Marta Alenquer ; Ana Laura Sousa ; Bárbara Kellen ; José Ramalho ; Erin M. Tranfield ; Maria João AmorimSource :
- Journal of cell science [ 1477-9137 ] ; 2016.
English descriptors
- KwdEn :
- MESH :
- chemical , metabolism : Upstream Stimulatory Factors, Vault Ribonucleoprotein Particles, rab GTP-Binding Proteins.
- metabolism : Endosomes.
- physiology : Influenza A virus.
- HEK293 Cells, HeLa Cells, Host-Pathogen Interactions, Humans, Protein Binding, Protein Transport, Virus Assembly.
Abstract
Influenza A virus assembly is an unclear process, whereby individual virion components form an infectious particle. The segmented nature of the influenza A genome imposes a problem to assembly because it requires packaging of eight distinct RNA particles (vRNPs). It also allows genome mixing from distinct parental strains, events associated with influenza pandemic outbreaks. It is important to public health to understand how segmented genomes assemble, a process that is dependent on the transport of components to assembly sites. Previously, it has been shown that vRNPs are carried by recycling endosome vesicles, resulting in a change of Rab11 distribution. Here, we describe that vRNP binding to recycling endosomes impairs recycling endosome function, by competing for Rab11 binding with family-interacting proteins, and that there is a causal relationship between Rab11 ability to recruit family-interacting proteins and Rab11 redistribution. This competition reduces recycling sorting at an unclear step, resulting in clustering of single- and double-membraned vesicles. These morphological changes in Rab11 membranes are indicative of alterations in protein and lipid homeostasis during infection. Vesicular clustering creates hotspots of the vRNPs that need to interact to form an infectious particle.
DOI: 10.1242/jcs.188409
PubMed: 26940915
Links to Exploration step
pubmed:26940915Le document en format XML
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Tranfield</name><affiliation><nlm:affiliation>Electron Microscopy Facility, Instituto Gulbenkian de Ciência, Rua da Quinta Grande, 6, Oeiras 2780-156, Portugal.</nlm:affiliation></affiliation></author><author><name sortKey="Amorim, Maria Joao" sort="Amorim, Maria Joao" uniqKey="Amorim M" first="Maria João" last="Amorim">Maria João Amorim</name><affiliation><nlm:affiliation>Cell Biology of Viral Infection Lab, Instituto Gulbenkian de Ciência, Rua da Quinta Grande, 6, Oeiras 2780-156, Portugal mjamorim@igc.gulbenkian.pt.</nlm:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2016">2016</date><idno type="RBID">pubmed:26940915</idno><idno type="pmid">26940915</idno><idno type="doi">10.1242/jcs.188409</idno><idno type="wicri:Area/PubMed/Corpus">000549</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000549</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Influenza A virus ribonucleoproteins modulate host recycling by competing with Rab11 effectors.</title><author><name sortKey="Vale Costa, Silvia" sort="Vale Costa, Silvia" uniqKey="Vale Costa S" first="Sílvia" last="Vale-Costa">Sílvia Vale-Costa</name><affiliation><nlm:affiliation>Cell Biology of Viral Infection Lab, Instituto Gulbenkian de Ciência, Rua da Quinta Grande, 6, Oeiras 2780-156, Portugal.</nlm:affiliation></affiliation></author><author><name sortKey="Alenquer, Marta" sort="Alenquer, Marta" uniqKey="Alenquer M" first="Marta" last="Alenquer">Marta Alenquer</name><affiliation><nlm:affiliation>Cell Biology of Viral Infection Lab, Instituto Gulbenkian de Ciência, Rua da Quinta Grande, 6, Oeiras 2780-156, Portugal.</nlm:affiliation></affiliation></author><author><name sortKey="Sousa, Ana Laura" sort="Sousa, Ana Laura" uniqKey="Sousa A" first="Ana Laura" last="Sousa">Ana Laura Sousa</name><affiliation><nlm:affiliation>Electron Microscopy Facility, Instituto Gulbenkian de Ciência, Rua da Quinta Grande, 6, Oeiras 2780-156, Portugal.</nlm:affiliation></affiliation></author><author><name sortKey="Kellen, Barbara" sort="Kellen, Barbara" uniqKey="Kellen B" first="Bárbara" last="Kellen">Bárbara Kellen</name><affiliation><nlm:affiliation>Cell Biology of Viral Infection Lab, Instituto Gulbenkian de Ciência, Rua da Quinta Grande, 6, Oeiras 2780-156, Portugal.</nlm:affiliation></affiliation></author><author><name sortKey="Ramalho, Jose" sort="Ramalho, Jose" uniqKey="Ramalho J" first="José" last="Ramalho">José Ramalho</name><affiliation><nlm:affiliation>Centro de Estudos de Doenças Crónicas (CEDOC), Faculdade de Ciências Médicas, Universidade Nova de Lisboa, Lisboa, Portugal.</nlm:affiliation></affiliation></author><author><name sortKey="Tranfield, Erin M" sort="Tranfield, Erin M" uniqKey="Tranfield E" first="Erin M" last="Tranfield">Erin M. Tranfield</name><affiliation><nlm:affiliation>Electron Microscopy Facility, Instituto Gulbenkian de Ciência, Rua da Quinta Grande, 6, Oeiras 2780-156, Portugal.</nlm:affiliation></affiliation></author><author><name sortKey="Amorim, Maria Joao" sort="Amorim, Maria Joao" uniqKey="Amorim M" first="Maria João" last="Amorim">Maria João Amorim</name><affiliation><nlm:affiliation>Cell Biology of Viral Infection Lab, Instituto Gulbenkian de Ciência, Rua da Quinta Grande, 6, Oeiras 2780-156, Portugal mjamorim@igc.gulbenkian.pt.</nlm:affiliation></affiliation></author></analytic><series><title level="j">Journal of cell science</title><idno type="eISSN">1477-9137</idno><imprint><date when="2016" type="published">2016</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Endosomes (metabolism)</term><term>HEK293 Cells</term><term>HeLa Cells</term><term>Host-Pathogen Interactions</term><term>Humans</term><term>Influenza A virus (physiology)</term><term>Protein Binding</term><term>Protein Transport</term><term>Upstream Stimulatory Factors (metabolism)</term><term>Vault Ribonucleoprotein Particles (metabolism)</term><term>Virus Assembly</term><term>rab GTP-Binding Proteins (metabolism)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Upstream Stimulatory Factors</term><term>Vault Ribonucleoprotein Particles</term><term>rab GTP-Binding Proteins</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Endosomes</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Influenza A virus</term></keywords><keywords scheme="MESH" xml:lang="en"><term>HEK293 Cells</term><term>HeLa Cells</term><term>Host-Pathogen Interactions</term><term>Humans</term><term>Protein Binding</term><term>Protein Transport</term><term>Virus Assembly</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Influenza A virus assembly is an unclear process, whereby individual virion components form an infectious particle. The segmented nature of the influenza A genome imposes a problem to assembly because it requires packaging of eight distinct RNA particles (vRNPs). It also allows genome mixing from distinct parental strains, events associated with influenza pandemic outbreaks. It is important to public health to understand how segmented genomes assemble, a process that is dependent on the transport of components to assembly sites. Previously, it has been shown that vRNPs are carried by recycling endosome vesicles, resulting in a change of Rab11 distribution. Here, we describe that vRNP binding to recycling endosomes impairs recycling endosome function, by competing for Rab11 binding with family-interacting proteins, and that there is a causal relationship between Rab11 ability to recruit family-interacting proteins and Rab11 redistribution. This competition reduces recycling sorting at an unclear step, resulting in clustering of single- and double-membraned vesicles. These morphological changes in Rab11 membranes are indicative of alterations in protein and lipid homeostasis during infection. Vesicular clustering creates hotspots of the vRNPs that need to interact to form an infectious particle.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">26940915</PMID><DateCompleted><Year>2017</Year><Month>01</Month><Day>06</Day></DateCompleted><DateRevised><Year>2017</Year><Month>01</Month><Day>07</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1477-9137</ISSN><JournalIssue CitedMedium="Internet"><Volume>129</Volume><Issue>8</Issue><PubDate><Year>2016</Year><Month>Apr</Month><Day>15</Day></PubDate></JournalIssue><Title>Journal of cell science</Title><ISOAbbreviation>J. Cell. Sci.</ISOAbbreviation></Journal><ArticleTitle>Influenza A virus ribonucleoproteins modulate host recycling by competing with Rab11 effectors.</ArticleTitle><Pagination><MedlinePgn>1697-710</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1242/jcs.188409</ELocationID><Abstract><AbstractText>Influenza A virus assembly is an unclear process, whereby individual virion components form an infectious particle. The segmented nature of the influenza A genome imposes a problem to assembly because it requires packaging of eight distinct RNA particles (vRNPs). It also allows genome mixing from distinct parental strains, events associated with influenza pandemic outbreaks. It is important to public health to understand how segmented genomes assemble, a process that is dependent on the transport of components to assembly sites. Previously, it has been shown that vRNPs are carried by recycling endosome vesicles, resulting in a change of Rab11 distribution. Here, we describe that vRNP binding to recycling endosomes impairs recycling endosome function, by competing for Rab11 binding with family-interacting proteins, and that there is a causal relationship between Rab11 ability to recruit family-interacting proteins and Rab11 redistribution. This competition reduces recycling sorting at an unclear step, resulting in clustering of single- and double-membraned vesicles. These morphological changes in Rab11 membranes are indicative of alterations in protein and lipid homeostasis during infection. Vesicular clustering creates hotspots of the vRNPs that need to interact to form an infectious particle.</AbstractText><CopyrightInformation>© 2016. Published by The Company of Biologists Ltd.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Vale-Costa</LastName><ForeName>Sílvia</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Cell Biology of Viral Infection Lab, Instituto Gulbenkian de Ciência, Rua da Quinta Grande, 6, Oeiras 2780-156, Portugal.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Alenquer</LastName><ForeName>Marta</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Cell Biology of Viral Infection Lab, Instituto Gulbenkian de Ciência, Rua da Quinta Grande, 6, Oeiras 2780-156, Portugal.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Sousa</LastName><ForeName>Ana Laura</ForeName><Initials>AL</Initials><AffiliationInfo><Affiliation>Electron Microscopy Facility, Instituto Gulbenkian de Ciência, Rua da Quinta Grande, 6, Oeiras 2780-156, Portugal.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kellen</LastName><ForeName>Bárbara</ForeName><Initials>B</Initials><AffiliationInfo><Affiliation>Cell Biology of Viral Infection Lab, Instituto Gulbenkian de Ciência, Rua da Quinta Grande, 6, Oeiras 2780-156, Portugal.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ramalho</LastName><ForeName>José</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Centro de Estudos de Doenças Crónicas (CEDOC), Faculdade de Ciências Médicas, Universidade Nova de Lisboa, Lisboa, Portugal.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Tranfield</LastName><ForeName>Erin M</ForeName><Initials>EM</Initials><AffiliationInfo><Affiliation>Electron Microscopy Facility, Instituto Gulbenkian de Ciência, Rua da Quinta Grande, 6, Oeiras 2780-156, Portugal.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Amorim</LastName><ForeName>Maria João</ForeName><Initials>MJ</Initials><Identifier Source="ORCID">http://orcid.org/0000-0002-4129-6659</Identifier><AffiliationInfo><Affiliation>Cell Biology of Viral Infection Lab, Instituto Gulbenkian de Ciência, Rua da Quinta Grande, 6, Oeiras 2780-156, Portugal mjamorim@igc.gulbenkian.pt.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2016</Year><Month>03</Month><Day>03</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>J Cell Sci</MedlineTA><NlmUniqueID>0052457</NlmUniqueID><ISSNLinking>0021-9533</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C497184">USF2 protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D051720">Upstream Stimulatory Factors</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D020394">Vault Ribonucleoprotein Particles</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.6.1.-</RegistryNumber><NameOfSubstance UI="C088986">rab11 protein</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.6.5.2</RegistryNumber><NameOfSubstance UI="D020691">rab GTP-Binding Proteins</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D011992" MajorTopicYN="N">Endosomes</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D057809" MajorTopicYN="N">HEK293 Cells</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006367" MajorTopicYN="N">HeLa Cells</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D054884" MajorTopicYN="N">Host-Pathogen Interactions</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009980" MajorTopicYN="N">Influenza A virus</DescriptorName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D021381" MajorTopicYN="N">Protein Transport</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D051720" MajorTopicYN="N">Upstream Stimulatory Factors</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020394" MajorTopicYN="N">Vault Ribonucleoprotein Particles</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D019065" MajorTopicYN="N">Virus Assembly</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020691" MajorTopicYN="N">rab GTP-Binding Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Correlative light and electron microscopy</Keyword><Keyword MajorTopicYN="N">Influenza A virus assembly</Keyword><Keyword MajorTopicYN="N">Membrane trafficking</Keyword><Keyword MajorTopicYN="N">Rab11</Keyword><Keyword MajorTopicYN="N">Recycling endosome</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2016</Year><Month>02</Month><Day>22</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2016</Year><Month>02</Month><Day>29</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2016</Year><Month>3</Month><Day>5</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2016</Year><Month>3</Month><Day>5</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2017</Year><Month>1</Month><Day>7</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">26940915</ArticleId><ArticleId IdType="pii">jcs.188409</ArticleId><ArticleId IdType="doi">10.1242/jcs.188409</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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