Distinctions between bovine herpesvirus 1 and herpes simplex virus type 1 VP22 tegument protein subcellular associations

被引:62
作者
Harms, JS
Ren, XD
Oliveira, SC
Splitter, GA
机构
[1] Univ Wisconsin, Dept Anim Hlth & Biomed Sci, Madison, WI 53706 USA
[2] Univ Fed Minas Gerais, Dept Bioquim & Imunol, BR-30161970 Belo Horizonte, MG, Brazil
关键词
D O I
10.1128/JVI.74.7.3301-3312.2000
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
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,,vith 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.
引用
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页码:3301 / 3312
页数:12
相关论文
共 29 条
[21]   Phosphorylation of structural components promotes dissociation of the herpes simplex virus type 1 tegument [J].
Morrison, EE ;
Wang, YF ;
Meredith, DM .
JOURNAL OF VIROLOGY, 1998, 72 (09) :7108-7114
[22]   Intercellular delivery of functional p53 by the herpesvirus protein VP22 [J].
Phelan, A ;
Elliott, G ;
O'Hare, P .
NATURE BIOTECHNOLOGY, 1998, 16 (05) :440-443
[23]   Modified VP22 localizes to the cell nucleus during synchronized herpes simplex virus type 1 infection [J].
Pomeranz, LE ;
Blaho, JA .
JOURNAL OF VIROLOGY, 1999, 73 (08) :6769-6781
[24]   Molecular virology of ruminant herpesviruses [J].
Schwyzer, M ;
Ackermann, M .
VETERINARY MICROBIOLOGY, 1996, 53 (1-2) :17-29
[25]   Microtubule-mediated transport of incoming herpes simplex virus 1 capsids to the nucleus [J].
Sodeik, B ;
Ebersold, MW ;
Helenius, A .
JOURNAL OF CELL BIOLOGY, 1997, 136 (05) :1007-1021
[26]   Construction and characterization of a stably transformed HeLa cell line in which the expression of bovine herpesvirus 1 ICP0 (BICP0) is induced by tetracycline [J].
Steinmann, NA ;
Nuñez, R ;
Köppel, R ;
Ackermann, M .
ARCHIVES OF VIROLOGY, 1998, 143 (01) :35-48
[27]   Phosphorylation of histone H3 is required for proper chromosome condensation and segregation [J].
Wei, Y ;
Yu, LL ;
Bowen, J ;
Gorovsky, MA ;
Allis, CD .
CELL, 1999, 97 (01) :99-109
[28]  
Wybranietz WA, 1999, J GENE MED, V1, P265
[29]   ROLE OF HERPES-SIMPLEX VIRUS TYPE-1 UL46 AND UL47 IN ALPHA-TIF-MEDIATED TRANSCRIPTIONAL INDUCTION - CHARACTERIZATION OF 3 VIRAL DELETION MUTANTS [J].
ZHANG, Y ;
SIRKO, DA ;
MCKNIGHT, JLC .
JOURNAL OF VIROLOGY, 1991, 65 (02) :829-841