A shrimp glycosylase protein, PmENGase, interacts with WSSV envelope protein VP41B and is involved in WSSV pathogenesis

Jiun Yan Huang, Hao Ching Wang, Yu Chun Chen, Po Sue Wang, Shin Jen Lin, Yun Shiang Chang, Kuan Fu Liu, Chu Fang Lo

Research output: Contribution to journalArticle

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.

Original languageEnglish
Article number103667
JournalDevelopmental and Comparative Immunology
Volume108
DOIs
Publication statusPublished - Jul 2020

Keywords

  • Shrimp
  • Shrimp glycosylase protein
  • White spot syndrome virus

ASJC Scopus subject areas

  • Immunology
  • Developmental Biology

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