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Virology v.513, 2018년, pp.188 - 194   SCI SCIE
본 등재정보는 저널의 등재정보를 참고하여 보여주는 베타서비스로 정확한 논문의 등재여부는 등재기관에 확인하시기 바랍니다.

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

Sun, Fenfen (Division of Avian Infectious Diseases, State Key Laboratory of Veterinary Biotechnology, Harbin Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Harbin 150001, China ) ; Pan, Wei (Division of Avian Infectious Diseases, State Key Laboratory of Veterinary Biotechnology, Harbin Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Harbin 150001, China ) ; Gao, Honglei (Division of Avian Infectious Diseases, State Key Laboratory of Veterinary Biotechnology, Harbin Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Harbin 150001, China ) ; Qi, Xiaole (Division of Avian Infectious Diseases, State Key Laboratory of Veterinary Biotechnology, Harbin Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Harbin 150001, China ) ; Qin, Liting (Division of Avian Infectious Diseases, State Key Laboratory of Veterinary Biotechnology, Harbin Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Harbin 150001, China ) ; Wang, Yongqiang (Division of Avian Infectious Diseases, S ) ; Gao, Yulong ; Wang, Xiaomei ;
  • 초록  

    Abstract 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. Highlights This study firstly demonstrated the direct interplay between VP3 and VP2 of CAV. Multiple independent interactive domains existed within the two proteins. The NLS2, but not the LRS in VP3, contributed to the interaction with the full-length VP2.


  • 주제어

    Chicken anemia virus .   VP2 .   VP3 .   Interaction .   Interaction domains.  

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