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Influenza virus hemagglutinin and neuraminidase cytoplasmic tails control particle shape

Identifieur interne : 001B77 ( Main/Exploration ); précédent : 001B76; suivant : 001B78

Influenza 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 :

RBID : ISTEX:865FDCEC9DBB4422CD028782FAF98CB82633F697

English descriptors

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:
DOI: 10.1093/emboj/16.6.1236


Affiliations:


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Le document en format XML

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<term>Average diameter</term>
<term>Cdna</term>
<term>Cell biol</term>
<term>Colloidal gold</term>
<term>Control virus</term>
<term>Cytoplasmic</term>
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<term>Genetic background</term>
<term>Glycoprotein</term>
<term>Gold particles</term>
<term>Grid</term>
<term>Hemagglutinin</term>
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<term>Immunoelectron microscopy</term>
<term>Infectious diseases</term>
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<term>Lower infectivity</term>
<term>Lower panel</term>
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<term>Matrix protein</term>
<term>Mdck</term>
<term>Mdck cells</term>
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<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>
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<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>
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