This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Guggemoos, S.
Right arrow Articles by Neubauer, A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Guggemoos, S.
Right arrow Articles by Neubauer, A.

 Previous Article  |  Next Article 

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,{dagger} Frank T. Just,2 and Antonie Neubauer1*

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 Mrs 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 Mr 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.

* Corresponding author. Mailing address: Antonie Neubauer Institute for Medical Microbiology, Infectious and Epidemic Diseases, Ludwig-Maximilians-University Munich, Veterinaerstr. 13, D-80539 Munich, Germany. Phone: 49-89-2180-2509. Fax: 49-89-2180-5905. E-mail: toni.neubauer{at}micro.vetmed.uni-muenchen.de.

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

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.



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]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»