WhiteSpot Disease (WSD), which is caused by a double-stranded DNA virus White spot
syndrome virus (WSSV) has become the major threat to global crustacean aquaculture
industries. To date nearly 100 potential host species for WSD have been
identified, including shrimp, crabs, lobsters, prawns, crayfishes, and copepods.
However, despite growing understanding of the underlying molecular biology,
cost-effective vaccinations or treatments for the disease remain elusive.
Molecularchaperones from the family of 70kDa heat shock proteins (Hsp70s) are conserved
among many kinds of organisms. The constitutively expressed members of this
family, heat shock cognate proteins (Hsc70s), have been shown to be involved in
protein folding in the cytoplasm, protein import into the endoplasmic reticulum,
mitochondria and chloroplasts, and trafficking of receptors and coated vesicles.
In the case of animal viruses, interactions with Hsc70 appear to be involved in
cell entry, virion assembly and disassembly, cell transformation, and DNA
replication. Our previous studies showed shrimp Heat shock protein Hsc70 play
key roles in WSSV infection, immune evasion, host cell apoptosis and virus
package. However, its regulatory mechanism remains unclear.
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