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The Inner Tegument Promotes Herpes Simplex Virus Capsid Motility Along Microtubules in vitro
Author(s) -
Wolfstein André,
Nagel ClausHenning,
Radtke Kerstin,
Döhner Katinka,
Allan Victoria J.,
Sodeik Beate
Publication year - 2006
Publication title -
traffic
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.677
H-Index - 130
eISSN - 1600-0854
pISSN - 1398-9219
DOI - 10.1111/j.1600-0854.2005.00379.x
Subject(s) - viral tegument , capsid , biology , dynactin , microbiology and biotechnology , microtubule , dynein , herpes simplex virus , cytosol , axoplasmic transport , lipid bilayer fusion , viral envelope , nocodazole , virology , biophysics , virus , cytoskeleton , biochemistry , cell , enzyme
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 µm. 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.