Modulation of nuclear localization of the influenza virus nucleoprotein through interaction with actin filaments.
Identifieur interne : 002E93 ( Main/Exploration ); précédent : 002E92; suivant : 002E94Modulation of nuclear localization of the influenza virus nucleoprotein through interaction with actin filaments.
Auteurs : P. Digard [Royaume-Uni] ; D. Elton ; K. Bishop ; E. Medcalf ; A. Weeds ; B. PopeSource :
- Journal of virology [ 0022-538X ] ; 1999.
Descripteurs français
- KwdFr :
- MESH :
- génétique : Orthomyxoviridae.
- métabolisme : ARN viral, Actines, Noyau de la cellule, Protéines du core viral.
- Animaux, Cellules HeLa, Cellules cultivées, Cricetinae, Humains, Mutation, Nucléoprotéines, Protéines nucléocapside, Transcription génétique.
English descriptors
- KwdEn :
- MESH :
- chemical , metabolism : Actins, RNA, Viral, Viral Core Proteins.
- genetics : Orthomyxoviridae.
- metabolism : Cell Nucleus.
- Animals, Cells, Cultured, Cricetinae, HeLa Cells, Humans, Mutation, Nucleocapsid Proteins, Nucleoproteins, Transcription, Genetic.
Abstract
The influenza virus genome is transcribed in the nuclei of infected cells but assembled into progeny virions in the cytoplasm. This is reflected in the cellular distribution of the virus nucleoprotein (NP), a protein which encapsidates genomic RNA to form ribonucleoprotein structures. At early times postinfection NP is found in the nucleus, but at later times it is found predominantly in the cytoplasm. NP contains several sequences proposed to act as nuclear localization signals (NLSs), and it is not clear how these are overridden to allow cytoplasmic accumulation of the protein. We find that NP binds tightly to filamentous actin in vitro and have identified a cluster of residues in NP essential for the interaction. Complexes containing RNA, NP, and actin could be formed, suggesting that viral ribonucleoproteins also bind actin. In cells, exogenously expressed NP when expressed at a high level partitioned to the cytoplasm, where it associated with F-actin stress fibers. In contrast, mutants unable to bind F-actin efficiently were imported into the nucleus even under conditions of high-level expression. Similarly, nuclear import of NLS-deficient NP molecules was restored by concomitant disruption of F-actin binding. We propose that the interaction of NP with F-actin causes the cytoplasmic retention of influenza virus ribonucleoproteins.
PubMed: 9971805
Affiliations:
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Digard</name><affiliation wicri:level="4"><nlm:affiliation>Division of Virology, Department of Pathology, University of Cambridge, Cambridge CB2 1QP, United Kingdom. pd1@mole.bio.cam.ac.uk</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>Division of Virology, Department of Pathology, University of Cambridge, Cambridge CB2 1QP</wicri:regionArea><orgName type="university">Université de Cambridge</orgName><placeName><settlement type="city">Cambridge</settlement><region type="country">Angleterre</region><region type="région" nuts="1">Angleterre de l'Est</region></placeName></affiliation></author><author><name sortKey="Elton, D" sort="Elton, D" uniqKey="Elton D" first="D" last="Elton">D. Elton</name></author><author><name sortKey="Bishop, K" sort="Bishop, K" uniqKey="Bishop K" first="K" last="Bishop">K. Bishop</name></author><author><name sortKey="Medcalf, E" sort="Medcalf, E" uniqKey="Medcalf E" first="E" last="Medcalf">E. Medcalf</name></author><author><name sortKey="Weeds, A" sort="Weeds, A" uniqKey="Weeds A" first="A" last="Weeds">A. Weeds</name></author><author><name sortKey="Pope, B" sort="Pope, B" uniqKey="Pope B" first="B" last="Pope">B. 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Digard</name><affiliation wicri:level="4"><nlm:affiliation>Division of Virology, Department of Pathology, University of Cambridge, Cambridge CB2 1QP, United Kingdom. pd1@mole.bio.cam.ac.uk</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>Division of Virology, Department of Pathology, University of Cambridge, Cambridge CB2 1QP</wicri:regionArea><orgName type="university">Université de Cambridge</orgName><placeName><settlement type="city">Cambridge</settlement><region type="country">Angleterre</region><region type="région" nuts="1">Angleterre de l'Est</region></placeName></affiliation></author><author><name sortKey="Elton, D" sort="Elton, D" uniqKey="Elton D" first="D" last="Elton">D. Elton</name></author><author><name sortKey="Bishop, K" sort="Bishop, K" uniqKey="Bishop K" first="K" last="Bishop">K. Bishop</name></author><author><name sortKey="Medcalf, E" sort="Medcalf, E" uniqKey="Medcalf E" first="E" last="Medcalf">E. Medcalf</name></author><author><name sortKey="Weeds, A" sort="Weeds, A" uniqKey="Weeds A" first="A" last="Weeds">A. Weeds</name></author><author><name sortKey="Pope, B" sort="Pope, B" uniqKey="Pope B" first="B" last="Pope">B. Pope</name></author></analytic><series><title level="j">Journal of virology</title><idno type="ISSN">0022-538X</idno><imprint><date when="1999" type="published">1999</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Actins (metabolism)</term><term>Animals</term><term>Cell Nucleus (metabolism)</term><term>Cells, Cultured</term><term>Cricetinae</term><term>HeLa Cells</term><term>Humans</term><term>Mutation</term><term>Nucleocapsid Proteins</term><term>Nucleoproteins</term><term>Orthomyxoviridae (genetics)</term><term>RNA, Viral (metabolism)</term><term>Transcription, Genetic</term><term>Viral Core Proteins (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>ARN viral (métabolisme)</term><term>Actines (métabolisme)</term><term>Animaux</term><term>Cellules HeLa</term><term>Cellules cultivées</term><term>Cricetinae</term><term>Humains</term><term>Mutation</term><term>Noyau de la cellule (métabolisme)</term><term>Nucléoprotéines</term><term>Orthomyxoviridae (génétique)</term><term>Protéines du core viral (métabolisme)</term><term>Protéines nucléocapside</term><term>Transcription génétique</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Actins</term><term>RNA, Viral</term><term>Viral Core Proteins</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Orthomyxoviridae</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Orthomyxoviridae</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Cell Nucleus</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>ARN viral</term><term>Actines</term><term>Noyau de la cellule</term><term>Protéines du core viral</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Cells, Cultured</term><term>Cricetinae</term><term>HeLa Cells</term><term>Humans</term><term>Mutation</term><term>Nucleocapsid Proteins</term><term>Nucleoproteins</term><term>Transcription, Genetic</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Cellules HeLa</term><term>Cellules cultivées</term><term>Cricetinae</term><term>Humains</term><term>Mutation</term><term>Nucléoprotéines</term><term>Protéines nucléocapside</term><term>Transcription génétique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The influenza virus genome is transcribed in the nuclei of infected cells but assembled into progeny virions in the cytoplasm. This is reflected in the cellular distribution of the virus nucleoprotein (NP), a protein which encapsidates genomic RNA to form ribonucleoprotein structures. At early times postinfection NP is found in the nucleus, but at later times it is found predominantly in the cytoplasm. NP contains several sequences proposed to act as nuclear localization signals (NLSs), and it is not clear how these are overridden to allow cytoplasmic accumulation of the protein. We find that NP binds tightly to filamentous actin in vitro and have identified a cluster of residues in NP essential for the interaction. Complexes containing RNA, NP, and actin could be formed, suggesting that viral ribonucleoproteins also bind actin. In cells, exogenously expressed NP when expressed at a high level partitioned to the cytoplasm, where it associated with F-actin stress fibers. In contrast, mutants unable to bind F-actin efficiently were imported into the nucleus even under conditions of high-level expression. Similarly, nuclear import of NLS-deficient NP molecules was restored by concomitant disruption of F-actin binding. We propose that the interaction of NP with F-actin causes the cytoplasmic retention of influenza virus ribonucleoproteins.</div></front></TEI><affiliations><list><country><li>Royaume-Uni</li></country><region><li>Angleterre</li><li>Angleterre de l'Est</li></region><settlement><li>Cambridge</li></settlement><orgName><li>Université de Cambridge</li></orgName></list><tree><noCountry><name sortKey="Bishop, K" sort="Bishop, K" uniqKey="Bishop K" first="K" last="Bishop">K. Bishop</name><name sortKey="Elton, D" sort="Elton, D" uniqKey="Elton D" first="D" last="Elton">D. Elton</name><name sortKey="Medcalf, E" sort="Medcalf, E" uniqKey="Medcalf E" first="E" last="Medcalf">E. Medcalf</name><name sortKey="Pope, B" sort="Pope, B" uniqKey="Pope B" first="B" last="Pope">B. Pope</name><name sortKey="Weeds, A" sort="Weeds, A" uniqKey="Weeds A" first="A" last="Weeds">A. Weeds</name></noCountry><country name="Royaume-Uni"><region name="Angleterre"><name sortKey="Digard, P" sort="Digard, P" uniqKey="Digard P" first="P" last="Digard">P. Digard</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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