A nuclear localization of the infectious haematopoietic necrosis virus NV protein is necessary for optimal viral growth
2011
Choi , Myeong Kyu (University of Ulsan, Seoul(Corée (République)). Department of Biological Sciences) | Moon , Chang Hoon (University of Ulsan, Seoul(Corée (République)). Department of Biological Sciences) | Ko , Myoung Seok (University of Ulsan, Seoul(Corée (République)). Department of Biological Sciences) | Lee , Unn-Hwa (University of Ulsan, Seoul(Corée (République)). Department of Biological Sciences) | Cho , Wha Ja (University of Ulsan, Seoul(Corée (République)). Biomedical Research Center) | Cha , Seung Ju (University of Ulsan, Seoul(Corée (République)). Biomedical Research Center) | Do , Jeong Wan (University of Ulsan, Seoul(Corée (République)). South and West Sea Fisheries Research Institute) | Heo , Gang Joon (Chungbuk National University, Cheongju(Corée (République)). College of Veterinary Medicine) | Jeong , Soo Geun (Ulsan Institute of Health and Environment, Ulsan(Corée (République)). Labo/service de l'auteur) | Hahm , Yoo Sik (Ulsan Institute of Health and Environment, Ulsan(Corée (République)). Labo/service de l'auteur) | Harmache , Abdallah (INRA , Nouzilly (France). UMR 1282 Infectiologie et Santé Publique) | Bremont-Deletang , Michel (INRA (France). ) | Kurath , Gael (US Geological Survey, Seattle / Washington(Etats-Unis). Western Fisheries Research Center) | Park , Jeong Woo(auteur de correspondance) (University of Ulsan, Seoul(Corée (République)). Department of Biological Sciences)
The nonvirion (NV) protein of infectious hematopoietic necrosis virus (IHNV) has been previously reported to be essential for efficient growth and pathogenicity of IHNV. However, little is known about the mechanism by which the NV supports the viral growth. In this study, cellular localization of NV and its role in IHNV growth in host cells was investigated. Through transient transfection in RTG-2 cells of NV fused to green fluorescent protein (GFP), a nuclear localization of NV was demonstrated. Deletion analyses showed that the 32EGDL 35 residues were essential for nuclear localization of NV protein, and fusion of these 4 amino acids to GFP directed its transport to the nucleus. We generated a recombinant IHNV, rIHNVNV-DEGDLin which the 32EGDL 35 was deleted from the NV. rIHNVs with wild-type NV (rIHNV-NV) or with the NV gene replaced with GFP (rIHNV-DNV-GFP) were used as controls. RTG-2 cells infected with rIHNV-DNV-GFP and rIHNV-NV-DEGDL yielded 12- and 5-fold less infectious virion, respectively, than wild type rIHNV-infected cells at 48 h post-infection (p.i.). While treatment with poly I:C at 24 h p.i. did not inhibit replication of wild-type rIHNVs, replication rates of rIHNV-DNV-GFP and rIHNV-NV-DEGDL were inhibited by poly I:C. In addition, both rIHNV-DNV and rIHNV-NV-DEGDL induced higher levels of expressions of both IFN1 and Mx1 than wild-type rIHNV. These data suggest that the IHNV NV may support the growth of IHNV through inhibition of the INF system and the amino acid residues of 32EGDL 35 responsible for nuclear localization are important for the inhibitory activity of NV.
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