The interaction of white spot syndrome virus envelope protein VP28 with shrimp Hsc70 is specific and ATP-dependent

Fish Shellfish Immunol. 2009 Mar;26(3):414-21. doi: 10.1016/j.fsi.2009.01.001. Epub 2009 Jan 10.

Abstract

White spot syndrome virus (WSSV) is one of the most devastating pathogens of shrimps and other crustaceans. In a previous study, we demonstrated that the major envelope protein VP28 of WSSV was involved in the attachment and penetration into shrimp cells. Here we showed that heat-shock cognate protein 70 (Hsc70) of shrimp was a binding partner of VP28 during virus infection. Hsc70 expression was enhanced by WSSV infection at the early stage and peaked at 12h post-infection and decreased drastically at the late stage. In shrimp haemocytes, both VP28 and Hsc70 proteins localized in the cytoplasm and their association was specific, ATP-dependent and Hsc70 concentration dependent. Moreover, direct VP28-Hsc70 association required both ATPase domain and peptide binding domain of Hsc70. The data obtained will help elucidate the role of VP28 protein in the process of virus infection.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Triphosphate / metabolism*
  • Animals
  • Cytoplasm / metabolism
  • Cytoplasm / virology
  • Gene Expression Profiling
  • Gene Expression Regulation
  • HSC70 Heat-Shock Proteins / metabolism*
  • Hemocytes / metabolism
  • Penaeidae / virology*
  • Protein Binding
  • Recombinant Proteins / metabolism
  • Time Factors
  • Viral Envelope Proteins / metabolism*
  • Viral Proteins / genetics
  • Viral Proteins / metabolism
  • White spot syndrome virus 1 / physiology*

Substances

  • HSC70 Heat-Shock Proteins
  • Recombinant Proteins
  • Viral Envelope Proteins
  • Viral Proteins
  • Adenosine Triphosphate