Previous Article | Next Article 
Journal of Virology, April 2000, p. 3301-3312, Vol. 74, No. 7
0022-538X/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
Distinctions between Bovine Herpesvirus 1 and
Herpes Simplex Virus Type 1 VP22 Tegument Protein Subcellular
Associations
Jerome S.
Harms,1,*
Xiaodi
Ren,1
Sergio C.
Oliveira,2 and
Gary A.
Splitter1
Department of Animal Health and Biomedical Sciences,
University of Wisconsin-Madison, Madison, Wisconsin
53706-1581,1 and Departamento de
Bioquímica e Imunologia, Universidade Federal de Minas
Gerais, Belo Horizonte, MG, CP 486 CEP 30161-970, Brazil2
Received 27 October 1999/Accepted 4 January 2000
The alphaherpesvirus tegument protein VP22 has been characterized
with multiple traits including microtubule reorganization, nuclear
localization, and nonclassical intercellular trafficking. However, all
these data were derived from studies using herpes simplex virus type 1 (HSV-1) and may not apply to VP22 homologs of other alphaherpesviruses.
We compared subcellular attributes of HSV-1 VP22 (HVP22) with bovine
herpesvirus 1 (BHV-1) VP22 (BVP22) using green fluorescent protein
(GFP)-fused VP22 expression vectors. Fluorescence microscopy of cell
lines transfected with these constructs revealed differences as well as
similarities between the two VP22 homologs. Compared to that of HVP22,
the BVP22 microtubule interaction was much less pronounced. The VP22
nuclear interaction varied, with a marbled or halo appearance for BVP22
and a speckled or nucleolus-bound appearance for HVP22. Both VP22
homologs associated with chromatin at various stages of mitosis and
could traffic from expressing cells to the nuclei of nonexpressing
cells. However, distinct qualitative differences in microtubule,
nuclear, and chromatin association as well as trafficking were
observed. The differences in VP22 homolog characteristics revealed in
this study will help define VP22 function within HSV-1 and BHV-1 infection.
*
Corresponding author. Mailing address: AHABS, 1656 Linden Dr., Madison, WI 53706-1581. Phone: (608) 262-0359. Fax: (608)
262-7420. E-mail: harms{at}ahabs.wisc.edu.
Journal of Virology, April 2000, p. 3301-3312, Vol. 74, No. 7
0022-538X/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
This article has been cited by other articles:
-
Yao, W., Liu, S., Qu, X., Xiao, S., Liu, Y., Liu, J.
(2009). Enhanced immune response and protection efficacy of a DNA vaccine constructed by linkage of the Mycobacterium tuberculosis Ag85B-encoding gene with the BVP22-encoding gene. J Med Microbiol
58: 462-468
[Abstract]
[Full Text]
-
Kalthoff, D., Granzow, H., Trapp, S., Beer, M.
(2008). The UL49 gene product of BoHV-1: a major factor in efficient cell-to-cell spread. J. Gen. Virol.
89: 2269-2274
[Abstract]
[Full Text]
-
Cilloniz, C., Jackson, W., Grose, C., Czechowski, D., Hay, J., Ruyechan, W. T.
(2007). The Varicella-Zoster Virus (VZV) ORF9 Protein Interacts with the IE62 Major VZV Transactivator. J. Virol.
81: 761-774
[Abstract]
[Full Text]
-
Zheng, C., Brownlie, R., Babiuk, L. A., van Drunen Littel-van den Hurk, S.
(2005). Characterization of the Nuclear Localization and Nuclear Export Signals of Bovine Herpesvirus 1 VP22. J. Virol.
79: 11864-11872
[Abstract]
[Full Text]
-
Mwangi, W., Brown, W. C., Splitter, G. A., Zhuang, Y., Kegerreis, K., Palmer, G. H.
(2005). Enhancement of antigen acquisition by dendritic cells and MHC class II-restricted epitope presentation to CD4+ T cells using VP22 DNA vaccine vectors that promote intercellular spreading following initial transfection. J. Leukoc. Biol.
78: 401-411
[Abstract]
[Full Text]
-
Zhu, J., Qiu, Z., Wiese, C., Ishii, Y., Friedrichsen, J., Rajashekara, G., Splitter, G. A.
(2005). Nuclear and Mitochondrial Localization Signals Overlap within Bovine Herpesvirus 1 Tegument Protein VP22. J. Biol. Chem.
280: 16038-16044
[Abstract]
[Full Text]
-
Yedowitz, J. C., Kotsakis, A., Schlegel, E. F. M., Blaho, J. A.
(2005). Nuclear Localizations of the Herpes Simplex Virus Type 1 Tegument Proteins VP13/14, vhs, and VP16 Precede VP22-Dependent Microtubule Reorganization and VP22 Nuclear Import. J. Virol.
79: 4730-4743
[Abstract]
[Full Text]
-
Zheng, C., Babiuk, L. A., van Drunen Littel-van den Hurk, S.
(2005). Bovine Herpesvirus 1 VP22 Enhances the Efficacy of a DNA Vaccine in Cattle. J. Virol.
79: 1948-1953
[Abstract]
[Full Text]
-
Qiu, Z., Harms, J. S., Zhu, J., Splitter, G. A.
(2004). Bovine Herpesvirus Tegument Protein VP22 Enhances Thymidine Kinase/Ganciclovir Suicide Gene Therapy for Neuroblastomas Compared to Herpes Simplex Virus VP22. J. Virol.
78: 4224-4233
[Abstract]
[Full Text]
-
Fuchs, W., Klupp, B. G., Granzow, H., Hengartner, C., Brack, A., Mundt, A., Enquist, L. W., Mettenleiter, T. C.
(2002). Physical Interaction between Envelope Glycoproteins E and M of Pseudorabies Virus and the Major Tegument Protein UL49. J. Virol.
76: 8208-8217
[Abstract]
[Full Text]
-
Martin, A., O'Hare, P., McLauchlan, J., Elliott, G.
(2002). Herpes Simplex Virus Tegument Protein VP22 Contains Overlapping Domains for Cytoplasmic Localization, Microtubule Interaction, and Chromatin Binding. J. Virol.
76: 4961-4970
[Abstract]
[Full Text]
-
Mettenleiter, T. C.
(2002). Herpesvirus Assembly and Egress. J. Virol.
76: 1537-1547
[Full Text]
-
Dorange, F., Tischer, B. K., Vautherot, J.-F., Osterrieder, N.
(2002). Characterization of Marek's Disease Virus Serotype 1 (MDV-1) Deletion Mutants That Lack UL46 to UL49 Genes: MDV-1 UL49, Encoding VP22, Is Indispensable for Virus Growth. J. Virol.
76: 1959-1970
[Abstract]
[Full Text]
-
Ren, X., Harms, J. S., Splitter, G. A.
(2001). Tyrosine Phosphorylation of Bovine Herpesvirus 1 Tegument Protein VP22 Correlates with the Incorporation of VP22 into Virions. J. Virol.
75: 9010-9017
[Abstract]
[Full Text]
-
Kotsakis, A., Pomeranz, L. E., Blouin, A., Blaho, J. A.
(2001). Microtubule Reorganization during Herpes Simplex Virus Type 1 Infection Facilitates the Nuclear Localization of VP22, a Major Virion Tegument Protein. J. Virol.
75: 8697-8711
[Abstract]
[Full Text]
-
Ren, X., Harms, J. S., Splitter, G. A.
(2001). Bovine Herpesvirus 1 Tegument Protein VP22 Interacts with Histones, and the Carboxyl Terminus of VP22 Is Required for Nuclear Localization. J. Virol.
75: 8251-8258
[Abstract]
[Full Text]
-
Hung, C.-F., Cheng, W.-F., Chai, C.-Y., Hsu, K.-F., He, L., Ling, M., Wu, T.-C.
(2001). Improving Vaccine Potency Through Intercellular Spreading and Enhanced MHC Class I Presentation of Antigen. J. Immunol.
166: 5733-5740
[Abstract]
[Full Text]
-
Cheng, W.-F., Hung, C.-F., Chai, C.-Y., Hsu, K.-F., He, L., Ling, M., Wu, T.-C.
(2001). Enhancement of Sindbis Virus Self-Replicating RNA Vaccine Potency by Linkage of Herpes Simplex Virus Type 1 VP22 Protein to Antigen. J. Virol.
75: 2368-2376
[Abstract]
[Full Text]
-
Pomeranz, L. E., Blaho, J. A.
(2000). Assembly of Infectious Herpes Simplex Virus Type 1 Virions in the Absence of Full-Length VP22. J. Virol.
74: 10041-10054
[Abstract]
[Full Text]
-
Normand, N., van Leeuwen, H., O'Hare, P.
(2001). Particle Formation by a Conserved Domain of the Herpes Simplex Virus Protein VP22 Facilitating Protein and Nucleic Acid Delivery. J. Biol. Chem.
276: 15042-15050
[Abstract]
[Full Text]