Skip to main navigation Skip to search Skip to main content

A Pacifastacus leniusculus serine protease interacts with WSSV

  • Enen Guo
  • , Gül Gizem Korkut
  • , Phattarunda Jaree
  • , Irene Söderhäll
  • , Kenneth Söderhäll
  • Uppsala University

Research output: Contribution to journalArticlepeer-review

11 Citations (Scopus)

Abstract

Serine proteases are involved in many critical physiological processes including virus spread and replication. In the present study, we identified a new clip-domain serine protease (PlcSP) in the crayfish Pacifastacus leniusculus hemocytes, which can interact with the White Spot Syndrome Virus (WSSV) envelope protein VP28. It was characterized by a classic clip domain with six strictly conserved Cys residues, and contained the conserved His-Asp-Ser (H-D-S) motif in the catalytic domain. Furthermore, signal peptide prediction revealed that it has a 16-residue secretion signal peptide. Tissue distribution showed that it was mainly located in P. leniusculus hemocytes, and its expression was increased in hemocytes upon WSSV challenge. In vitro knock down of PlcSP decreased both the expression of VP28 and the WSSV copy number in hematopoietic stem (HPT) cells. Accordingly, these data suggest that the new serine protease may be of importance for WSSV infection into hematopoietic cells.

Original languageEnglish
Pages (from-to)211-219
Number of pages9
JournalFish and Shellfish Immunology
Volume68
DOIs
Publication statusPublished - Sept 2017
Externally publishedYes

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

  1. SDG 3 - Good Health and Well-being
    SDG 3 Good Health and Well-being

Keywords

  • Hematopoietic tissue
  • Invertebrate
  • Serine protease
  • Virus
  • WSSV

Fingerprint

Dive into the research topics of 'A Pacifastacus leniusculus serine protease interacts with WSSV'. Together they form a unique fingerprint.

Cite this