Global profiling of megalocytivirus-induced proteins in tongue sole (Cynoglossus semilaevis) spleen identifies cellular processes essential to viral infection

Megalocytivirus is a DNA virus with a broad host range among farmed fish including tongue sole (Cynoglossus semilaevis). In this study, label-free proteomics was performed to examine protein expression in tongue sole spleen induced by megalocytivirus at 8 and 12 days post infection (dpi). Compared t...

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Bibliographic Details
Published in:Developmental & Comparative Immunology
Main Authors: Zhang, Jian, Sun, Li
Format: Report
Language:English
Published: ELSEVIER SCI LTD 2019
Subjects:
Cynoglossus semilaevis
Megalocytivirus
Viral infection
Immune defense
Ubiquitin proteasome system
Fisheries
Immunology
Zoology
FLOUNDER PARALICHTHYS-OLIVACEUS
TURBOT SCOPHTHALMUS-MAXIMUS
IRIDOVIRUS-LIKE AGENT
MANDARIN FISH
SINIPERCA-CHUATSI
JAPANESE FLOUNDER
NECROSIS VIRUS
ENDOSOMAL PROTEOLYSIS
MANNOSE RECEPTOR
CATHEPSIN-L
Scophthalmus maximus
Turbot
Online Access:http://ir.qdio.ac.cn/handle/337002/155594
https://doi.org/10.1016/j.dci.2018.11.006
Description
Summary:Megalocytivirus is a DNA virus with a broad host range among farmed fish including tongue sole (Cynoglossus semilaevis). In this study, label-free proteomics was performed to examine protein expression in tongue sole spleen induced by megalocytivirus at 8 and 12 days post infection (dpi). Compared to uninfected control fish, virus-infected fish displayed 315 up-regulated proteins and 111 down-regulated proteins at 8 dpi, and 48 up regulated proteins and 43 down-regulated proteins at 12 dpi. The expressions of five differentially expressed proteins were confirmed by Western blot. The differentially expressed proteins were enriched in the pathways and processes associated with innate immune response and viral infection. Interference with the expression of two up-regulated proteins of the ubiquitin proteasome system (UPS), i.e. proteasome assembly chaperone 2 and proteasome maturation protein, significantly reduced viral propagation in fish, whereas overexpression of these two proteins significantly enhanced viral propagation. Consistently, inhibition of the functioning of proteasome significantly impaired viral replication in vivo. This study provided the first global protein profile responsive to megalocytivirus in tongue sole, and revealed an essential role of UPS in viral infection.

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