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Title: Actin-myosin network is required for proper assembly of influenza virus particles

Abstract

Actin filaments are known to play a central role in cellular dynamics. After polymerization of actin, various actin-crosslinking proteins including non-muscle myosin II facilitate the formation of spatially organized actin filament networks. The actin-myosin network is highly expanded beneath plasma membrane. The genome of influenza virus (vRNA) replicates in the cell nucleus. Then, newly synthesized vRNAs are nuclear-exported to the cytoplasm as ribonucleoprotein complexes (vRNPs), followed by transport to the beneath plasma membrane where virus particles assemble. Here, we found that, by inhibiting actin-myosin network formation, the virus titer tends to be reduced and HA viral spike protein is aggregated on the plasma membrane. These results indicate that the actin-myosin network plays an important role in the virus formation. - Highlights: • Actin-myosin network is important for the influenza virus production. • HA forms aggregations at the plasma membrane in the presence of blebbistatin. • M1 is recruited to the budding site through the actin-myosin network.

Authors:
; ;
Publication Date:
OSTI Identifier:
22470150
Resource Type:
Journal Article
Resource Relation:
Journal Name: Virology; Journal Volume: 476; Other Information: Copyright (c) 2014 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved.; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United States
Language:
English
Subject:
60 APPLIED LIFE SCIENCES; ACTIN; AGGLOMERATION; CELL NUCLEI; CROSS-LINKING; CYTOPLASM; FILAMENTS; INFLUENZA VIRUSES; MEMBRANES; MUSCLES; MYOSIN; PARTICLES

Citation Formats

Kumakura, Michiko, Kawaguchi, Atsushi, E-mail: ats-kawaguchi@md.tsukuba.ac.jp, and Nagata, Kyosuke, E-mail: knagata@md.tsukuba.ac.jp. Actin-myosin network is required for proper assembly of influenza virus particles. United States: N. p., 2015. Web. doi:10.1016/J.VIROL.2014.12.016.
Kumakura, Michiko, Kawaguchi, Atsushi, E-mail: ats-kawaguchi@md.tsukuba.ac.jp, & Nagata, Kyosuke, E-mail: knagata@md.tsukuba.ac.jp. Actin-myosin network is required for proper assembly of influenza virus particles. United States. doi:10.1016/J.VIROL.2014.12.016.
Kumakura, Michiko, Kawaguchi, Atsushi, E-mail: ats-kawaguchi@md.tsukuba.ac.jp, and Nagata, Kyosuke, E-mail: knagata@md.tsukuba.ac.jp. Sun . "Actin-myosin network is required for proper assembly of influenza virus particles". United States. doi:10.1016/J.VIROL.2014.12.016.
@article{osti_22470150,
title = {Actin-myosin network is required for proper assembly of influenza virus particles},
author = {Kumakura, Michiko and Kawaguchi, Atsushi, E-mail: ats-kawaguchi@md.tsukuba.ac.jp and Nagata, Kyosuke, E-mail: knagata@md.tsukuba.ac.jp},
abstractNote = {Actin filaments are known to play a central role in cellular dynamics. After polymerization of actin, various actin-crosslinking proteins including non-muscle myosin II facilitate the formation of spatially organized actin filament networks. The actin-myosin network is highly expanded beneath plasma membrane. The genome of influenza virus (vRNA) replicates in the cell nucleus. Then, newly synthesized vRNAs are nuclear-exported to the cytoplasm as ribonucleoprotein complexes (vRNPs), followed by transport to the beneath plasma membrane where virus particles assemble. Here, we found that, by inhibiting actin-myosin network formation, the virus titer tends to be reduced and HA viral spike protein is aggregated on the plasma membrane. These results indicate that the actin-myosin network plays an important role in the virus formation. - Highlights: • Actin-myosin network is important for the influenza virus production. • HA forms aggregations at the plasma membrane in the presence of blebbistatin. • M1 is recruited to the budding site through the actin-myosin network.},
doi = {10.1016/J.VIROL.2014.12.016},
journal = {Virology},
number = ,
volume = 476,
place = {United States},
year = {Sun Feb 15 00:00:00 EST 2015},
month = {Sun Feb 15 00:00:00 EST 2015}
}