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Open AccessJournal ArticleDOI

Influenza Virus M2 Ion Channel Protein Is Necessary for Filamentous Virion Formation

TLDR
It is found that an amphipathic helix located within the M2 cytoplasmic tail is able to bind cholesterol, and it is speculated that M2 cholesterol binding is essential for both filament formation and the stability of existing viral filaments.
Abstract
Influenza A virus buds from cells as spherical (∼100-nm diameter) and filamentous (∼100 nm × 2 to 20 μm) virions. Previous work has determined that the matrix protein (M1) confers the ability of the virus to form filaments; however, additional work has suggested that the influenza virus M2 integral membrane protein also plays a role in viral filament formation. In examining the role of the M2 protein in filament formation, we observed that the cytoplasmic tail of M2 contains several sites that are essential for filament formation. Additionally, whereas M2 is a nonraft protein, expression of other viral proteins in the context of influenza virus infection leads to the colocalization of M2 with sites of virus budding and lipid raft domains. We found that an amphipathic helix located within the M2 cytoplasmic tail is able to bind cholesterol, and we speculate that M2 cholesterol binding is essential for both filament formation and the stability of existing viral filaments.

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Meta- and Orthogonal Integration of Influenza “OMICs” Data Defines a Role for UBR4 in Virus Budding

TL;DR: A meta-analysis of data from eight published RNAi screens and integrated with three protein interaction datasets revealed a functionally validated biochemical landscape of the influenza-host interface, which illuminates a viral-host network of high-confidence human proteins that are essential for influenza A virus replication.
Journal ArticleDOI

Influenza virus assembly and budding.

TL;DR: This review investigates the latest research on influenza virus budding in an attempt to provide a step-by-step analysis of the assembly and budding processes for influenza viruses.
Journal ArticleDOI

Influenza Virus M2 Protein Mediates ESCRT-Independent Membrane Scission

TL;DR: It is shown that M2 localizes to the neck of budding virions and that mutation of the M2 amphipathic helix results in failure of the virus to undergo membrane scission and virion release, suggesting that M1 mediates the final steps of budding for influenza viruses, bypassing the need for host ESCRT proteins.
Journal ArticleDOI

M2e-based universal influenza A vaccine.

TL;DR: Experiments in animal models have demonstrated that M2e-based vaccines induce protection against a lethal challenge with various influenza A virus subtypes, and the production and use of an effective M 2e-vaccine could be implemented at any time regardless of seasonality, both in an epidemic as well as in a pandemic preparedness program.
Journal ArticleDOI

Identification of a novel splice variant form of the influenza A virus M2 ion channel with an antigenically distinct ectodomain.

TL;DR: In identifying a 14th influenza A polypeptide, the data reinforce the unexpectedly high coding capacity of the viral genome and have implications for virus evolution, as well as for understanding the role of M2 in the virus life cycle.
References
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Journal ArticleDOI

Emergence and pandemic potential of swine-origin H1N1 influenza virus.

TL;DR: Efforts to control these outbreaks and real-time monitoring of the evolution of this virus should provide invaluable information to direct infectious disease control programmes and to improve understanding of the factors that determine viral pathogenicity and/or transmissibility.
Journal ArticleDOI

Generation of influenza A viruses entirely from cloned cDNAs

TL;DR: A new reverse-genetics system that allows one to efficiently generate influenza A viruses entirely from cloned cDNAs is described, which should be useful in viral mutagenesis studies and in the production of vaccines and gene therapy vectors.
Journal ArticleDOI

Influenza virus M2 protein has ion channel activity.

TL;DR: Analysis of the currents of altered M2 proteins suggests that the channel pore is formed by the transmembrane domain of the M2 protein, which is proposed to have a pivotal role in the biology of influenza virus infection.
Journal ArticleDOI

Structure and Mechanism of the M2 Proton Channel of Influenza A Virus

TL;DR: The structure of the tetrameric M2 channel in complex with rimantadine, determined by NMR is presented and predicted to counter the effect of drug binding by either increasing the hydrophilicity of the pore or weakening helix–helix packing, thus facilitating channel opening.
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