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Journal of Virology, July 2009, p. 6978-6986, Vol. 83, No. 14
0022-538X/09/$08.00+0 doi:10.1128/JVI.00598-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

M. P. Taylor, and
L. W. Enquist*
Department of Molecular Biology, Princeton University, Princeton, New Jersey 08544
Received 23 March 2009/ Accepted 24 April 2009
Pseudorabies virus (PRV) Us9 is a small, tail-anchored (TA) membrane protein that is essential for axonal sorting of viral structural proteins and is highly conserved among other members of the alphaherpesvirus subfamily. We cloned the Us9 homologs from two human pathogens, varicella-zoster virus (VZV) and herpes simplex virus type 1 (HSV-1), as well as two veterinary pathogens, equine herpesvirus type 1 (EHV-1) and bovine herpesvirus type 1 (BHV-1), and fused them to enhanced green fluorescent protein to examine their subcellular localization and membrane topology. Akin to PRV Us9, all of the Us9 homologs localized to the trans-Golgi network and had a type II membrane topology (typical of TA proteins). Furthermore, we examined whether any of the Us9 homologs could compensate for the loss of PRV Us9 in anterograde, neuron-to-cell spread of infection in a compartmented chamber system. EHV-1 and BHV-1 Us9 were able to fully compensate for the loss of PRV Us9, whereas VZV and HSV-1 Us9 proteins were unable to functionally replace PRV Us9 when they were expressed in a PRV background.
Published ahead of print on 6 May 2009.
Present address: Department of Surgery, The Johns Hopkins Hospital, Baltimore, MD 21287.
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