A functional link between the actin cytoskeleton and lipid rafts during budding of filamentous influenza virions

Martha Simpson-Holley, Darren Ellis, Dawn Fisher, Debra Elton, John McCauley, Paul Digard

Research output: Contribution to journalArticlepeer-review


Morphogenesis of influenza virus is a poorly understood process that produces two types of enveloped virion: approximately 100-nm spheres and similar diameter filaments that reach 20 microm in length. Spherical particles assemble at plasma membrane lipid rafts in a process independent of microfilaments. The budding site of filamentous virions is hitherto uncharacterised but their formation involves the actin cytoskeleton. We confirm microfilament involvement in filamentous budding and show that after disruption of cortical actin by jasplakinolide, HA, NP, and M1 redistributed around beta-actin clusters to form novel annular membrane structures. HA in filamentous virions and jasplakinolide-induced annuli was detergent insoluble at 4 degrees C. Furthermore, in both cases HA partitioned into low buoyant density detergent-insoluble glycolipid domains, indicating that filamentous virions and annuli contain reorganised lipid rafts. We propose that the actin cytoskeleton is required to maintain the correct organisation of lipid rafts for incorporation into budding viral filaments.
Original languageEnglish
Pages (from-to)212-25
Number of pages14
Issue number2
Publication statusPublished - 30 Sep 2002


  • Actins/metabolism
  • Animals
  • Cell Line
  • Cytochalasin D/pharmacology
  • Cytoskeleton/drug effects
  • Cytoskeleton/metabolism
  • Depsipeptides
  • Dogs
  • Hemagglutinin Glycoproteins, Influenza Virus
  • Humans
  • Influenza A virus
  • Intracellular Fluid
  • Membrane Microdomains/metabolism
  • Nucleoproteins/metabolism
  • Peptides, Cyclic/pharmacology
  • RNA-Binding Proteins
  • Viral Core Proteins/metabolism
  • Viral Matrix Proteins/metabolism
  • Virion/physiology
  • Virus Assembly


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