Abstract:Fructose-1,6-bisphosphate aldolase (FBA) is a key glycolytic enzyme involved in both the glycolytic and gluconeogenic pathways. In the present study, fructose-1,6-bisphosphate aldolase from Chinese shrimp Fenneropenaeus chinensis (FcFBA) was cloned and sequenced. The full-length complementary DNA (cDNA) sequence of FcFBA is 2496 bp long, which contains a 79-bp 5¢-untranslated region (UTR), 1319-bp 3¢-UTR, and 1098-bp open reading frame, encoding a polypeptide of 365 amino acids with a molecular mass of 39.8 kDa and a theoretical isoelectric point of 6.6. Multiple sequence alignments showed the high similarity of FcFBA with the aldolases of other arthropods. Phylogenetic analysis showed that FcFBA of shrimp belonged to the same class as that of other arthropod aldolases. The transcript of FcFBA showed the highest expression in the muscle and lowest expression in the hepatopancreas, which indicates that FcFBA is similar to the muscle type (type A) aldolase that acts in the glycolytic pathway. The expression profile of FcFBA in the hepatopancreas, gills, and muscle was modulated when the shrimp were stimulated by white spot syndrome virus (WSSV), which resulted in differential expression of FcFBA. Further, RNA interference (RNAi) was used to analyze the role of FcFBA. After RNAi, the mortality of shrimp after WSSV infection was altered compared with that after phosphate-buffered saline injection. Within 24 h of RNAi, the expression level of FcFBA was significantly down regulated. These results show that FcFBA is inducible and might be involved in the immune response of shrimp.
