Identification of the interaction and interaction domains of chicken anemia virus VP2 and VP3 proteins

被引:10
作者
Sun, Fenfen [1 ,2 ]
Pan, Wei [1 ,2 ]
Gao, Honglei [1 ]
Qi, Xiaole [1 ]
Qin, Liting [1 ]
Wang, Yongqiang [1 ]
Gao, Yulong [1 ]
Wang, Xiaomei [1 ]
机构
[1] Chinese Acad Agr Sci, Harbin Vet Res Inst, State Key Lab Vet Biotechnol, Div Avian Infect Dis, Harbin 150001, Heilongjiang, Peoples R China
[2] Xuzhou Med Univ, Expt Teaching Ctr Morphol, Xuzhou 221004, Jiangsu, Peoples R China
关键词
Chicken anemia virus; VP2; VP3; Interaction; Interaction domains; APOPTIN PROTEIN; APOPTOSIS; LOCALIZATION; REPLICATION; EXPRESSION; INDUCTION; SYSTEM; CELLS;
D O I
10.1016/j.virol.2017.09.014
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
Chicken anemia virus (CAV) is a small, single-stranded DNA virus of Anelloviridae family. Its genome segments encode three proteins, VP1, VP2, and VP3. This study identified an interaction between VP2 and VP3 and mapped the interaction domains. Through the yeast two-hybrid (Y2H) system, VP2 was found to interact with VP3. The presence of the VP2 VP3 complex in CAV-infected chicken cells was confirmed by co-immunoprecipitation. Confocal microscopy showed that VP2 and VP3 were expressed in the cytoplasm in cotransfected Vero cells. In the Y2H system, the interaction domains were identified as being within the N-terminal aa 1-30 and C-terminal aa 17-60 for VP2 and the N-terminal aa 46-60 and C-terminal aa 1-7 for VP3. This study showed the interaction between VP2 and VP3 of CAV and identified multiple independent interactive domains within the two proteins. This provides novel information for investigating the biological functions of these proteins.
引用
收藏
页码:188 / 194
页数:7
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