1. A shrimp glycosylase protein, PmENGase, interacts with WSSV envelope protein VP41B and is involved in WSSV pathogenesis.
- Author
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Huang JY, Wang HC, Chen YC, Wang PS, Lin SJ, Chang YS, Liu KF, and Lo CF
- Subjects
- Animals, Aquaculture, Arthropod Proteins genetics, Arthropod Proteins isolation & purification, Cell Line, Host-Pathogen Interactions genetics, Host-Pathogen Interactions immunology, Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase genetics, Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase isolation & purification, Penaeidae immunology, Protein Binding immunology, RNA Interference, Recombinant Proteins genetics, Recombinant Proteins isolation & purification, Recombinant Proteins metabolism, Ribonucleases metabolism, Two-Hybrid System Techniques, Up-Regulation immunology, White spot syndrome virus 1 immunology, White spot syndrome virus 1 metabolism, Arthropod Proteins metabolism, Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase metabolism, Penaeidae virology, Viral Envelope Proteins metabolism, White spot syndrome virus 1 pathogenicity
- Abstract
Viral glycoproteins are expressed by many viruses, and during infection they usually play very important roles, such as receptor attachment or membrane fusion. The mature virion of the white spot syndrome virus (WSSV) is unusual in that it contains no glycosylated proteins, and there are currently no reports of any glycosylation mechanisms in the pathogenesis of this virus. In this study, we cloned a glycosylase, mannosyl-glycoprotein endo-β-N-acetylglucosaminidase (ENGase, EC 3.2.1.96), from Penaeus monodon and found that it was significantly up-regulated in WSSV-infected shrimp. A yeast two-hybrid assay showed that PmENGase interacted with both structural and non-structural proteins, and GST-pull down and co-immunoprecipitation (Co-IP) assays confirmed its interaction with the envelope protein VP41B. In the WSSV challenge tests, the cumulative mortality and viral copy number were significantly decreased in the PmEngase-silenced shrimp, from which we conclude that shrimp glycosylase interacts with WSSV in a way that benefits the virus. Lastly, we speculate that the deglycosylation activity of PmENGase might account for the absence of glycosylated proteins in the WSSV virion., (Copyright © 2020 Elsevier Ltd. All rights reserved.)
- Published
- 2020
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