Actin Mediates the Nanoscale Membrane Organization of the Clustered Membrane Protein Influenza Hemagglutinin

The influenza viral membrane protein hemagglutinin (HA) is required at high concentrations on virion and host-cell membranes for infectivity. Because the role of actin in membrane organization is not completely understood, we quantified the relationship between HA and host-cell actin at the nanoscal...

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Bibliographic Details
Published in:Biophysical journal 2013-05, Vol.104 (10), p.2182-2192
Main Authors: Gudheti, Manasa V., Curthoys, Nikki M., Gould, Travis J., Kim, Dahan, Gunewardene, Mudalige S., Gabor, Kristin A., Gosse, Julie A., Kim, Carol H., Zimmerberg, Joshua, Hess, Samuel T.
Format: Article
Language:English
Subjects:
actin
Actin Cytoskeleton - metabolism
Actin Depolymerizing Factors - metabolism
Actins - metabolism
Animals
Biochemistry
Biophysics
Cell Membrane - metabolism
Cell Membrane - ultrastructure
Cytoskeleton
fluorescence
Hemagglutinin Glycoproteins, Influenza Virus - chemistry
Hemagglutinin Glycoproteins, Influenza Virus - metabolism
Hemagglutinin Glycoproteins, Influenza Virus - ultrastructure
hemagglutinins
image analysis
Influenza
Influenza A Virus, H2N2 Subtype - chemistry
Influenza A Virus, H2N2 Subtype - metabolism
Membrane
membrane glycoproteins
Membranes
Mice
microfilaments
Microscopy
NIH 3T3 Cells
pathogenicity
Protein Multimerization
Proteins
virion
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Summary:The influenza viral membrane protein hemagglutinin (HA) is required at high concentrations on virion and host-cell membranes for infectivity. Because the role of actin in membrane organization is not completely understood, we quantified the relationship between HA and host-cell actin at the nanoscale. Results obtained using superresolution fluorescence photoactivation localization microscopy (FPALM) in nonpolarized cells show that HA clusters colocalize with actin-rich membrane regions (ARMRs). Individual molecular trajectories in live cells indicate restricted HA mobility in ARMRs, and actin disruption caused specific changes to HA clustering. Surprisingly, the actin-binding protein cofilin was excluded from some regions within several hundred nanometers of HA clusters, suggesting that HA clusters or adjacent proteins within the same clusters influence local actin structure. Thus, with the use of imaging, we demonstrate a dynamic relationship between glycoprotein membrane organization and the actin cytoskeleton at the nanoscale.
ISSN:0006-3495
1542-0086
DOI:10.1016/j.bpj.2013.03.054