Intracellular localization of Equine herpesvirus type 1 tegument protein VP22

被引:8
|
作者
Okada, Ayaka [1 ]
Kodaira, Akari [1 ]
Hanyu, Sachiko [1 ]
Izume, Satoko [1 ]
Ohya, Kenji [1 ,2 ]
Fukushi, Hideto [1 ,2 ]
机构
[1] Gifu Univ, United Grad Sch Vet Sci, Dept Appl Vet Sci, Gifu 5011193, Japan
[2] Gifu Univ, Fac Appl Biol Sci, Lab Vet Microbiol, Gifu 5011193, Japan
关键词
Equine herpesvirus 1; Tegument; VP22; Localization; SIMPLEX-VIRUS; BOVINE HERPESVIRUS-1; NUCLEAR-LOCALIZATION; UL49; HOMOLOG; GENE; INFECTION; MUTANTS; ABSENCE; GROWTH; CELLS;
D O I
10.1016/j.virusres.2014.08.006
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
Intracellular localization of Equine herpesvirus type 1 (EHV-1) tegument protein VP22 was examined by using a plasmid that expressed VP22 fused with an enhanced green fluorescent protein (EGFP). Also a recombinant EHV-1 expressing VP22 fused with a red fluorescent protein (mCherry) was constructed to observe the localization of VP22 in infected cells. When EGFP-fused VP22 was overexpressed in the cells, VP22 localized in the cytoplasm and nucleus. Live cell imaging suggested that the fluorescently tagged VP22 also localized in the cytoplasm and nucleus. These results show that VP22 localizes in the cytoplasm and nucleus independently of other viral proteins. Experiments with truncation mutants of pEGFP-VP22 suggested that 154-188 aa might be the nuclear localization signal of EHV-1 VP22. (C) 2014 Elsevier B.V. All rights reserved.
引用
收藏
页码:103 / 113
页数:11
相关论文
共 50 条
  • [1] Bovine herpesvirus 1 tegument protein VP22 interacts with histones, and the carboxyl terminus of VP22 is required for nuclear localization
    Ren, XD
    Harms, JS
    Splitter, GA
    JOURNAL OF VIROLOGY, 2001, 75 (17) : 8251 - 8258
  • [2] Tyrosine phosphorylation of bovine herpesvirus 1 tegument protein VP22 correlates with the incorporation of VP22 into virions
    Ren, XD
    Harms, JS
    Splitter, GA
    JOURNAL OF VIROLOGY, 2001, 75 (19) : 9010 - 9017
  • [3] Decreased expression of the immediate early protein, ICP4, by deletion of the tegument protein VP22 of equine herpesvirus type 1
    Okada, Ayaka
    Suganuma, Shota
    Badr, Yassien
    Omatsu, Tsutomu
    Mizutani, Tetsuya
    Ohya, Kenji
    Fukushi, Hideto
    JOURNAL OF VETERINARY MEDICAL SCIENCE, 2018, 80 (02): : 311 - 315
  • [4] Nuclear and mitochondrial localization signals overlap within bovine herpesvirus 1 tegument protein VP22
    ZhuO, J
    Qiu, ZH
    Wiese, C
    Ishii, Y
    Friedrichsen, J
    Rajashekara, G
    Splitter, GA
    JOURNAL OF BIOLOGICAL CHEMISTRY, 2005, 280 (16) : 16038 - 16044
  • [5] Equine herpesvirus type 1 tegument protein VP22 is not essential for pathogenicity in a hamster model, but is required for efficient viral growth in cultured cells
    Okada, Ayaka
    Izume, Satoko
    Ohya, Kenji
    Fukushi, Hideto
    JOURNAL OF VETERINARY MEDICAL SCIENCE, 2015, 77 (10): : 1293 - 1297
  • [6] Distinctions between bovine herpesvirus 1 and herpes simplex virus type 1 VP22 tegument protein subcellular associations
    Harms, JS
    Ren, XD
    Oliveira, SC
    Splitter, GA
    JOURNAL OF VIROLOGY, 2000, 74 (07) : 3301 - 3312
  • [8] Membrane association of VP22, a herpes simplex virus type 1 tegument protein
    Brignati, MJ
    Loomis, JS
    Wills, JW
    Courtney, RJ
    JOURNAL OF VIROLOGY, 2003, 77 (08) : 4888 - 4898
  • [9] Conformational lability of herpesvirus protein VP22
    Kueltzo, LA
    Normand, N
    O'Hare, P
    Middaugh, CR
    JOURNAL OF BIOLOGICAL CHEMISTRY, 2000, 275 (43) : 33213 - 33221
  • [10] Phosphorylation of the herpes simplex virus type I tegument protein VP22
    Elliott, G
    OReilly, D
    OHare, P
    VIROLOGY, 1996, 226 (01) : 140 - 145