Cloning of an orange-spotted grouper Epinephelus coioides heat shock protein 90AB (HSP90AB) and characterization of its expression in response to nodavirus

Fish Shellfish Immunol. 2010 May-Jun;28(5-6):895-904. doi: 10.1016/j.fsi.2010.02.004. Epub 2010 Feb 11.

Abstract

The heat shock proteins (HSPs) family which consists of HSP90, HSP70, and low molecular mass HSPs are involved in chaperone activity. Here, we report the cloning and characterization of HSP90AB gene from orange-spotted grouper, Epinephelus coioides. The full-length of grouper HSP90AB was 727 amino acids and possessed an ATPase domain as well as an evolutionarily conserved molecular chaperone. The HSP90AB-green fluorescent protein fusion protein was evenly distributed in the cytoplasm. Immunohistochemistry (IHC) and real-time polymerase chain reaction (PCR) analyses indicated that the expression of grouper HSP90AB was marginally increased following nodavirus infection. Grouper E. coioides that received HSP90 inhibitor geldanamycin (GA) showed an increase in HSP90AB expression and growth of nodavirus supporting nodavirus replication.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Antibiotics, Antineoplastic / pharmacology
  • Base Sequence
  • Bass / genetics*
  • Bass / immunology*
  • Benzoquinones / pharmacology
  • Capsid Proteins / metabolism
  • Cell Line
  • Cloning, Molecular
  • Fish Diseases / immunology*
  • Gene Expression Profiling
  • Gene Expression Regulation / drug effects
  • Heat-Shock Proteins / genetics*
  • Heat-Shock Proteins / immunology*
  • Lactams, Macrocyclic / pharmacology
  • Molecular Sequence Data
  • Nodaviridae
  • Phylogeny
  • RNA Virus Infections / immunology
  • RNA Virus Infections / veterinary*
  • Time Factors

Substances

  • Antibiotics, Antineoplastic
  • Benzoquinones
  • Capsid Proteins
  • Heat-Shock Proteins
  • Lactams, Macrocyclic
  • geldanamycin

Associated data

  • GENBANK/FJ644278