A Pacifastacus leniusculus serine protease interacts with WSSV

Fish Shellfish Immunol. 2017 Sep:68:211-219. doi: 10.1016/j.fsi.2017.07.026. Epub 2017 Jul 10.

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.

Keywords: Hematopoietic tissue; Invertebrate; Serine protease; Virus; WSSV.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Arthropod Proteins / chemistry
  • Arthropod Proteins / genetics
  • Arthropod Proteins / metabolism*
  • Astacoidea / enzymology*
  • Astacoidea / genetics
  • Astacoidea / immunology
  • Astacoidea / virology*
  • Base Sequence
  • Gene Expression Regulation, Enzymologic
  • Gene Knockdown Techniques
  • Hemocytes / enzymology
  • Hemocytes / virology
  • Immunity, Innate*
  • Sequence Alignment
  • Serine Proteases / chemistry
  • Serine Proteases / genetics
  • Serine Proteases / metabolism*
  • Viral Envelope Proteins / metabolism
  • White spot syndrome virus 1 / physiology*

Substances

  • Arthropod Proteins
  • Viral Envelope Proteins
  • Serine Proteases