The inner tegument promotes herpes simplex virus capsid motility along microtubules in vitro

Traffic. 2006 Feb;7(2):227-37. doi: 10.1111/j.1600-0854.2005.00379.x.


After viral fusion, capsids of the neurotropic herpes simplex virus are transported along microtubules (MT) to the nuclear pores for viral genome uncoating, nuclear transcription and replication. After assembly and egress from the nucleus, cytosolic capsids are transported to host membranes for secondary envelopment or to the axon terminal for further viral spread. Using GFP-tagged capsids, Cy3-labelled MT and cytosol, we have reconstituted viral capsid transport in vitro. In the presence of ATP, capsids moved along MT up to 30 microm. Blocking the function of dynactin, a cofactor of dynein and kinesin-2, inhibited the transport. Removing outer tegument proteins from the capsids increased in vitro motility. In contrast, capsids isolated from infected nuclei that were devoid of inner as well as outer tegument proteins showed little interaction with dynein and its cofactor dynactin. Our data suggest that the inner tegument of alphaherpesviruses contains viral receptors for MT motors.

MeSH terms

  • Adenosine Triphosphate / physiology
  • Animals
  • Capsid / physiology
  • Capsid Proteins / metabolism
  • Cell Line
  • Cell Nucleus / virology
  • Cricetinae
  • Cytosol / virology
  • Dynactin Complex
  • Dyneins / physiology
  • Female
  • Green Fluorescent Proteins / metabolism
  • Herpesvirus 1, Human / physiology*
  • In Vitro Techniques
  • Microtubule-Associated Proteins / physiology
  • Microtubules / virology*
  • Molecular Motor Proteins / physiology
  • Movement
  • Oocytes / virology
  • Recombinant Fusion Proteins / metabolism
  • Xenopus laevis


  • Capsid Proteins
  • Dynactin Complex
  • Microtubule-Associated Proteins
  • Molecular Motor Proteins
  • Recombinant Fusion Proteins
  • capsid protein VP26, herpes simplex virus type 1
  • Green Fluorescent Proteins
  • Adenosine Triphosphate
  • Dyneins