Herpes Simplex Virus Tegument Protein US11 Interacts with Conventional Kinesin Heavy Chain

• DOI: 10.1128/jvi.76.7.3282-3291.2002
• Publication Date: 2002-07-27T09:58:35Z
• Authors: Russell J. Diefen...; Monica Miranda-Sa...; Eve Diefenbach; David J. Holland; Ross A. Boadle; Patricia J. Armati; Anthony L. Cunnin...
• Keywords: Viral tegument; Axoplasmic transport; Kinesin; Immunoelectron microscopy

ABSTRACT Little is known about the mechanisms of transport neurotropic herpesviruses, such as herpes simplex virus (HSV), varicella-zoster virus, and pseudorabies within neurons. For these viruses, which replicate in nucleus, anterograde from cell body dorsal root ganglion (DRG) neurons to axon terminus occurs over long distances. In case HSV, unenveloped nucleocapsids human DRG cocultured with autologous skin were observed by immunoelectron microscopy colocalize conventional ubiquitous kinesin, a microtubule-dependent motor protein, during axonal transport. Subsequently, four candidate kinesin-binding structural HSV proteins identified (VP5, VP16, VP22, US11) using oligohistidine-tagged kinesin heavy chain (uKHC) bait. Of viral proteins, direct interaction between uKHC US11 was identified. vitro studies residues 867 894 US11-binding site located proposed heptad repeat cargo-binding domain uKHC. addition, uKHC-binding maps C-terminal RNA-binding domain. consistently cotransported kinetics similar those capsid protein VP5 into axons dissociated rat neurons, unlike other tegument VP16 VP22. These observations suggest major role for uKHC-US11 axons.