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DnaJC16, the molecular chaperone, is implicated in hemocyte apoptosis and facilitates of WSSV infection in shrimp.

Abstract
Chaperone proteins, including heat shock proteins (HSPs) and DnaJ proteins, are highly conserved and well known for their quick responses to environmental stresses and pathogen infections, especially viruses. However, how DnaJ, an HSP family member, in Penaeus vannamei responds to viral invasion has not been reported. In this research, the novel DnaJ homolog subfamily C member 16-like, or DnaJC16, was characterized in P. vannamei. It contains the DnaJ and thioredoxin domains. Phylogenetic tree analysis demonstrated the conservation of DnaJC16 among penaeid shrimp, where PvDnaJC16 was found to be closely related to DnaJC16 from Fenneropenaeus chinensis and Marsupenaeus japonicus. The transcripts of PvDnaJC16 were expressed in all the tissues tested, and the highest expression was in the lymphoid organs. As hemocytes are major immune tissue, we found significant upregulation of PvDnaJC16 in shrimp hemocytes after white spot syndrome virus (WSSV) infection. Furthermore, the suppression of PvDnaJC16 expression by RNA interference in WSSV-infected shrimp showed a decrease in replication and WSSV copy number. Interestingly, a dramatically high cumulative survival rate following the WSSV challenge (over 60%) was observed in PvDnaJC16-silenced shrimp. Meanwhile, the total hemocyte number was significantly increased in PvDnaJC16 knockdown. In addition, the expression of caspase-3 was reduced, as was the caspase-3/7 activity in PvDnaJC16 silencing. Additionally, the percentage of late apoptotic hemocytes diminished after PvDnaJC16 reduction, whereas the percentage of hemocyte viability increased. Our data reflect the fact that the upregulation of PvDnaJC16 expression upon WSSV infection enhances hemocyte apoptosis, which can accelerate viral spreading in shrimp.
AuthorsPhattarunda Jaree, Kunlaya Somboonwiwat
JournalFish & shellfish immunology (Fish Shellfish Immunol) Vol. 137 Pg. 108770 (Jun 2023) ISSN: 1095-9947 [Electronic] England
PMID37105425 (Publication Type: Journal Article)
CopyrightCopyright © 2023 Elsevier Ltd. All rights reserved.
Chemical References
  • Caspase 3
  • Molecular Chaperones
  • Arthropod Proteins
Topics
  • Animals
  • Hemocytes
  • Caspase 3 (genetics)
  • White spot syndrome virus 1 (physiology)
  • Phylogeny
  • Apoptosis (genetics)
  • Molecular Chaperones (genetics)
  • Penaeidae
  • Arthropod Proteins

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