H2N2V1, Main, Exploration, bibRecord, 000520

Structural Analysis of the Roles of Influenza A Virus Membrane-Associated Proteins in Assembly and Morphology.

Identifieur interne : 000520 ( Main/Exploration ); précédent : 000519; suivant : 000521

Structural Analysis of the Roles of Influenza A Virus Membrane-Associated Proteins in Assembly and Morphology.

Auteurs : Petr Chlanda [Allemagne] ; Oliver Schraidt [Allemagne] ; Susann Kummer [Allemagne] ; James Riches [Allemagne] ; Heike Oberwinkler [Allemagne] ; Simone Prinz [Allemagne] ; Hans-Georg Kr Usslich [Allemagne] ; John A G. Briggs [Allemagne]

Source :

Journal of virology [ 1098-5514 ] ; 2015.

RBID : pubmed:26085153

Descripteurs français

English descriptors

KwdEn :
- Cell Line, Cryoelectron Microscopy, Electron Microscope Tomography, HEK293 Cells, Hemagglutinin Glycoproteins, Influenza Virus (biosynthesis), Hemagglutinin Glycoproteins, Influenza Virus (genetics), Hemagglutinin Glycoproteins, Influenza Virus (metabolism), Humans, Influenza A Virus, H2N2 Subtype (metabolism), Influenza A Virus, H3N2 Subtype (metabolism), Neuraminidase (biosynthesis), Neuraminidase (genetics), Neuraminidase (metabolism), Viral Matrix Proteins (biosynthesis), Viral Matrix Proteins (genetics), Viral Matrix Proteins (metabolism), Virus Assembly (genetics), Virus Release (genetics).
MESH :
- chemical , biosynthesis : Hemagglutinin Glycoproteins, Influenza Virus, Neuraminidase, Viral Matrix Proteins.
- chemical , genetics : Hemagglutinin Glycoproteins, Influenza Virus, Neuraminidase, Viral Matrix Proteins.
- chemical , metabolism : Hemagglutinin Glycoproteins, Influenza Virus, Neuraminidase, Viral Matrix Proteins.
- genetics : Virus Assembly, Virus Release.
- metabolism : Influenza A Virus, H2N2 Subtype, Influenza A Virus, H3N2 Subtype.
- Cell Line, Cryoelectron Microscopy, Electron Microscope Tomography, HEK293 Cells, Humans.

Abstract

The assembly of influenza A virus at the plasma membrane of infected cells leads to release of enveloped virions that are typically round in tissue culture-adapted strains but filamentous in strains isolated from patients. The viral proteins hemagglutinin (HA), neuraminidase (NA), matrix protein 1 (M1), and M2 ion channel all contribute to virus assembly. When expressed individually or in combination in cells, they can all, under certain conditions, mediate release of membrane-enveloped particles, but their relative roles in virus assembly, release, and morphology remain unclear. To investigate these roles, we produced membrane-enveloped particles by plasmid-derived expression of combinations of HA, NA, and M proteins (M1 and M2) or by infection with influenza A virus. We monitored particle release, particle morphology, and plasma membrane morphology by using biochemical methods, electron microscopy, electron tomography, and cryo-electron tomography. Our data suggest that HA, NA, or HANA (HA plus NA) expression leads to particle release through nonspecific induction of membrane curvature. In contrast, coexpression with the M proteins clusters the glycoproteins into filamentous membrane protrusions, which can be released as particles by formation of a constricted neck at the base. HA and NA are preferentially distributed to differently curved membranes within these particles. Both the budding intermediates and the released particles are morphologically similar to those produced during infection with influenza A virus. Together, our data provide new insights into influenza virus assembly and show that the M segment together with either of the glycoproteins is the minimal requirement to assemble and release membrane-enveloped particles that are truly virus-like.

DOI: 10.1128/JVI.00592-15
PubMed: 26085153

Affiliations:

Le document en format XML

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<term>Electron Microscope Tomography</term>
<term>HEK293 Cells</term>
<term>Hemagglutinin Glycoproteins, Influenza Virus (biosynthesis)</term>
<term>Hemagglutinin Glycoproteins, Influenza Virus (genetics)</term>
<term>Hemagglutinin Glycoproteins, Influenza Virus (metabolism)</term>
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<term>Neuraminidase (genetics)</term>
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<term>Viral Matrix Proteins (genetics)</term>
<term>Viral Matrix Proteins (metabolism)</term>
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<term>Virus Release (genetics)</term>
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<term>Cellules HEK293</term>
<term>Cryomicroscopie électronique</term>
<term>Glycoprotéine hémagglutinine du virus influenza (biosynthèse)</term>
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<term>Neuraminidase</term>
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<keywords scheme="MESH" qualifier="biosynthèse" xml:lang="fr"><term>Glycoprotéine hémagglutinine du virus influenza</term>
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<term>Protéines de la matrice virale</term>
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<front><div type="abstract" xml:lang="en">The assembly of influenza A virus at the plasma membrane of infected cells leads to release of enveloped virions that are typically round in tissue culture-adapted strains but filamentous in strains isolated from patients. The viral proteins hemagglutinin (HA), neuraminidase (NA), matrix protein 1 (M1), and M2 ion channel all contribute to virus assembly. When expressed individually or in combination in cells, they can all, under certain conditions, mediate release of membrane-enveloped particles, but their relative roles in virus assembly, release, and morphology remain unclear. To investigate these roles, we produced membrane-enveloped particles by plasmid-derived expression of combinations of HA, NA, and M proteins (M1 and M2) or by infection with influenza A virus. We monitored particle release, particle morphology, and plasma membrane morphology by using biochemical methods, electron microscopy, electron tomography, and cryo-electron tomography. Our data suggest that HA, NA, or HANA (HA plus NA) expression leads to particle release through nonspecific induction of membrane curvature. In contrast, coexpression with the M proteins clusters the glycoproteins into filamentous membrane protrusions, which can be released as particles by formation of a constricted neck at the base. HA and NA are preferentially distributed to differently curved membranes within these particles. Both the budding intermediates and the released particles are morphologically similar to those produced during infection with influenza A virus. Together, our data provide new insights into influenza virus assembly and show that the M segment together with either of the glycoproteins is the minimal requirement to assemble and release membrane-enveloped particles that are truly virus-like.</div>
</front>
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Structural Analysis of the Roles of Influenza A Virus Membrane-Associated Proteins in Assembly and Morphology.

Structural Analysis of the Roles of Influenza A Virus Membrane-Associated Proteins in Assembly and Morphology.

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