Influenza virus hemagglutinin and neuraminidase cytoplasmic tails control particle shape
Identifieur interne : 001B77 ( Main/Exploration ); précédent : 001B76; suivant : 001B78Influenza virus hemagglutinin and neuraminidase cytoplasmic tails control particle shape
Auteurs : Hong Jin [États-Unis] ; George P. Leser [États-Unis] ; Jie Zhang [États-Unis] ; Robert A. Lamb [États-Unis]Source :
- The EMBO Journal [ 0261-4189 ] ; 1997-03-15.
English descriptors
- Teeft :
- Allantoic, Assay, Average diameter, Cdna, Cell biol, Colloidal gold, Control virus, Cytoplasmic, Cytoplasmic domain, Cytoplasmic domains, Cytoplasmic tail, Cytoplasmic tail deletion, Cytoplasmic tail deletion viruses, Cytoplasmic tails, Deletion, Electron microscope, Embryonated, Embryonated chicken eggs, Embryonated eggs, Genetic background, Glycoprotein, Gold particles, Grid, Hemagglutinin, Immunoblotting, Immunoelectron microscopy, Infectious diseases, Infectivity, Integral membrane proteins, Irregular shapes, Lamentous, Lower infectivity, Lower panel, Matrix, Matrix protein, Mdck, Mdck cells, Membrane association, Morphology, Mutation, Natl acad, Neuraminidase, Neuraminidase activity, Nucleotide sequence, Palese, Phosphotungstic acid, Polypeptide, Protein cytoplasmic tail, Reassortant, Reassortant viruses, Small plaques, Spherical particles, Spike, Sucrose, Sucrose density gradients, Tissue culture, Transfectant, Transfectant virus, Transmembrane, Transmembrane domain, Viral, Viral protein, Virion, Virol, Virology, Virus, Virus assembly, Virus envelope, Virus hemagglutinin, Virus morphology, Virus transfectant.
Abstract
The cytoplasmic tails of the influenza virus glycoproteins hemagglutinin (HA) and neuraminidase (NA) are highly conserved in sequence for all virus subtypes and it is believed that assembly of this enveloped virus depends on interactions of these domains with cytoplasmic viral components. However, it is possible to rescue altered influenza viruses lacking either the HA or NA cytoplasmic tails. We have obtained an influenza virus that lacks both the cytoplasmic tail of HA and NA. Particle production is reduced ∼10‐fold but these particles, although having a fairly normal protein composition, are greatly elongated and of extended irregular shape. We propose a model in which the interactions of the cytoplasmic tails of HA and NA with an internal viral component are so important for spherical virion shape that there is dual redundancy in the interactions.
Url:
- https://api.istex.fr/ark:/67375/WNG-N1QPLF7S-H/fulltext.pdf
- http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1169722
DOI: 10.1093/emboj/16.6.1236
Affiliations:
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Le document en format XML
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<term>Assay</term>
<term>Average diameter</term>
<term>Cdna</term>
<term>Cell biol</term>
<term>Colloidal gold</term>
<term>Control virus</term>
<term>Cytoplasmic</term>
<term>Cytoplasmic domain</term>
<term>Cytoplasmic domains</term>
<term>Cytoplasmic tail</term>
<term>Cytoplasmic tail deletion</term>
<term>Cytoplasmic tail deletion viruses</term>
<term>Cytoplasmic tails</term>
<term>Deletion</term>
<term>Electron microscope</term>
<term>Embryonated</term>
<term>Embryonated chicken eggs</term>
<term>Embryonated eggs</term>
<term>Genetic background</term>
<term>Glycoprotein</term>
<term>Gold particles</term>
<term>Grid</term>
<term>Hemagglutinin</term>
<term>Immunoblotting</term>
<term>Immunoelectron microscopy</term>
<term>Infectious diseases</term>
<term>Infectivity</term>
<term>Integral membrane proteins</term>
<term>Irregular shapes</term>
<term>Lamentous</term>
<term>Lower infectivity</term>
<term>Lower panel</term>
<term>Matrix</term>
<term>Matrix protein</term>
<term>Mdck</term>
<term>Mdck cells</term>
<term>Membrane association</term>
<term>Morphology</term>
<term>Mutation</term>
<term>Natl acad</term>
<term>Neuraminidase</term>
<term>Neuraminidase activity</term>
<term>Nucleotide sequence</term>
<term>Palese</term>
<term>Phosphotungstic acid</term>
<term>Polypeptide</term>
<term>Protein cytoplasmic tail</term>
<term>Reassortant</term>
<term>Reassortant viruses</term>
<term>Small plaques</term>
<term>Spherical particles</term>
<term>Spike</term>
<term>Sucrose</term>
<term>Sucrose density gradients</term>
<term>Tissue culture</term>
<term>Transfectant</term>
<term>Transfectant virus</term>
<term>Transmembrane</term>
<term>Transmembrane domain</term>
<term>Viral</term>
<term>Viral protein</term>
<term>Virion</term>
<term>Virol</term>
<term>Virology</term>
<term>Virus</term>
<term>Virus assembly</term>
<term>Virus envelope</term>
<term>Virus hemagglutinin</term>
<term>Virus morphology</term>
<term>Virus transfectant</term>
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<front><div type="abstract">The cytoplasmic tails of the influenza virus glycoproteins hemagglutinin (HA) and neuraminidase (NA) are highly conserved in sequence for all virus subtypes and it is believed that assembly of this enveloped virus depends on interactions of these domains with cytoplasmic viral components. However, it is possible to rescue altered influenza viruses lacking either the HA or NA cytoplasmic tails. We have obtained an influenza virus that lacks both the cytoplasmic tail of HA and NA. Particle production is reduced ∼10‐fold but these particles, although having a fairly normal protein composition, are greatly elongated and of extended irregular shape. We propose a model in which the interactions of the cytoplasmic tails of HA and NA with an internal viral component are so important for spherical virion shape that there is dual redundancy in the interactions.</div>
</front>
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<name sortKey="Jin, Hong" sort="Jin, Hong" uniqKey="Jin H" first="Hong" last="Jin">Hong Jin</name>
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