IHB OpenIR  > 鱼类生物学及渔业生物技术研究中心  > 期刊论文
Fish herpesvirus protein (CaHV-138L) can target to mitochondrial protein FoF1 ATPase
Zhao, Yu-Han1; Zeng, Xiao-Tao1; Zhang, Qi-Ya1,2
2020-01-02
Source PublicationVIRUS RESEARCH
ISSN0168-1702
Volume275Issue:1Pages:7
Abstract

Herpesvirus infection usually relies on the interaction between viral protein and host protein to enhance replication of the enveloped virus. Fish Carassius auratus herpesvirus (CaHV) is highly pathogenic pathogen causing gill acute hemorrhages of crucian carp (Carassius auratus) and high moritality rates among those infected fish. The protein of CaHV (CaHV-138 L) containing two transmembrane (TM) domains and an immunoglobulin C-2 Type (IGc2) domain was predicted as a viral membrane protein. In this investigation, fluorescence observation showed that full-length CaHV-138 L mainly localized on the plasma membrane or around nuclear membrane of fish fathead minnow (FHM) cells in a punctate pattern. The TM domain deletion mutants of CaHV-138 L (Delta TM1, Delta TM2, and Delta TM1 &Delta TM2) diffusely distributed in both the cytoplasm and the nucleus, mainly presented patchy fashion in the cytoplasm, and mainly presented both in the nucleus and in the cytoplasm, respectively. Obviously, the TM domain deletion mutants significantly affected CaHV-138 L subcellular localization. Meanwhile, colocalization assay showed that the full-length viral protein colocalized with mitochondria. Furthermore, the interaction between CaHV-138 L and host protein was identified by yeast two-hybrid (Y2H) and co-immunoprecipitation (co-IP) assays. The host mitochondrial protein FoF1 ATP synthase (FoF1-ATPase) that interacts with this viral protein was screened. The data indicated that CaHV-138 L can target to mitochondrial protein FoF1-ATPase, which might provide energy for virus replication through mediating mitochondrial ATP synthesis. This study has provided valuable information for better understanding of the links of herpesvirus proteins with aquaculture animal proteins.

KeywordCarassius auratus herpesvirus (CaHV) Viral protein Mitochondrial FoF1-ATPase Virus-host interaction Yeast two hybrid (Y2H) Co-immunoprecipitation (co-IP) assays
DOI10.1016/j.virusres.2019.197754
Indexed BySCI
Language英语
WOS Research AreaVirology
WOS SubjectVirology
WOS IDWOS:000500373700003
WOS KeywordCARASSIUS-AURATUS HERPESVIRUS ; MOLECULAR-BASIS ; MEMBRANE ; SYNTHASE ; REVEALS
PublisherELSEVIER
Citation statistics
Document Type期刊论文
Identifierhttp://ir.ihb.ac.cn/handle/342005/34807
Collection鱼类生物学及渔业生物技术研究中心_期刊论文
Corresponding AuthorZhang, Qi-Ya
Affiliation1.Univ Chinese Acad Sci, Chinese Acad Sci, State Key Lab Freshwater Ecol & Biotechnol, Inst Hydrobiol, Wuhan 430072, Hubei, Peoples R China
2.Chinese Acad Sci, Innovat Acad Seed Design, Beijing 100101, Peoples R China
Recommended Citation
GB/T 7714
Zhao, Yu-Han,Zeng, Xiao-Tao,Zhang, Qi-Ya. Fish herpesvirus protein (CaHV-138L) can target to mitochondrial protein FoF1 ATPase[J]. VIRUS RESEARCH,2020,275(1):7.
APA Zhao, Yu-Han,Zeng, Xiao-Tao,&Zhang, Qi-Ya.(2020).Fish herpesvirus protein (CaHV-138L) can target to mitochondrial protein FoF1 ATPase.VIRUS RESEARCH,275(1),7.
MLA Zhao, Yu-Han,et al."Fish herpesvirus protein (CaHV-138L) can target to mitochondrial protein FoF1 ATPase".VIRUS RESEARCH 275.1(2020):7.
Files in This Item:
File Name/Size DocType Version Access License
1-s2.0-S016817021930(4720KB)期刊论文作者接受稿开放获取CC BY-NC-SAView Application Full Text
Related Services
Recommend this item
Bookmark
Usage statistics
Export to Endnote
Google Scholar
Similar articles in Google Scholar
[Zhao, Yu-Han]'s Articles
[Zeng, Xiao-Tao]'s Articles
[Zhang, Qi-Ya]'s Articles
Baidu academic
Similar articles in Baidu academic
[Zhao, Yu-Han]'s Articles
[Zeng, Xiao-Tao]'s Articles
[Zhang, Qi-Ya]'s Articles
Bing Scholar
Similar articles in Bing Scholar
[Zhao, Yu-Han]'s Articles
[Zeng, Xiao-Tao]'s Articles
[Zhang, Qi-Ya]'s Articles
Terms of Use
No data!
Social Bookmark/Share
File name: 1-s2.0-S0168170219304241-main.pdf
Format: Adobe PDF
All comments (0)
No comment.
 

Items in the repository are protected by copyright, with all rights reserved, unless otherwise indicated.