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Journal of Virology, January 2006, p. 95-107, Vol. 80, No. 1
0022-538X/06/$08.00+0     doi:10.1128/JVI.80.1.95-107.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

The Equine Herpesvirus 1 UL20 Product Interacts with Glycoprotein K and Promotes Egress of Mature Particles

Simone Guggemoos,^1, Frank T. Just,² and Antonie Neubauer^1*

Institute for Medical Microbiology, Infectious and Epidemic Diseases, Ludwig-Maximilians-University Munich, Veterinaerstr. 13, D-80539 Munich, Germany,¹ Institute for Comparative Tropical Medicine and Parasitology, Ludwig-Maximilians-University Munich, Leopoldstrasse 5, D-80802 Munich, Germany²

Received 17 June 2005/ Accepted 3 October 2005

The aim of the present study was to identify and functionally characterize the equine herpesvirus 1 (EHV-1) UL20 protein (UL20p). Using a specific antiserum, UL20p was shown to be associated with membranes of infected cells, as well as with envelopes of purified virions. By Western blot analysis, UL20p was detected in two main forms exhibiting M_rs of 25,000 and 75,000. Both moieties did not enter the separating gel after heating of protein samples to 99°C. The slower-migrating form of UL20p contains N-linked carbohydrates, and its presence is dependent of that of other viral proteins. Infection of cells that either constitutively express UL20p or a gK-green fluorescent protein (GFP) fusion protein with various EHV-1 deletion mutants revealed a relatively stable hetero-oligomer containing gK and UL20p with an apparent M_r of 75,000. As demonstrated by confocal microscopy, UL20p distribution in Rk13 cells changed from a diffuse granular or netlike appearance to a pattern confined to the Golgi network when gK was coexpressed. Analysis of a UL20 deletion mutant of EHV-1 strain RacL11 indicated an involvement of UL20p in cell-to-cell spread, as well as in very late events in virus egress. Based on these and electron microscopic studies we suggest that the EHV-1 UL20 protein might be necessary to avoid fusion of mature virions with membranes of their transport vesicles.

Present address: GSF-National Research Center for Environment and Health, Institute of Molecular Immunology, CCG HCT, Marchioninistr. 25, D-81377 Munich, Germany.

This article has been cited by other articles:

• Foster, T. P., Chouljenko, V. N., Kousoulas, K. G. (2008). Functional and Physical Interactions of the Herpes Simplex Virus Type 1 UL20 Membrane Protein with Glycoprotein K. J. Virol. 82: 6310-6323 [Abstract] [Full Text]