Abstract:Rab proteins are the largest subfamily in small GTP binding proteins, which play important roles in vesicle formation, transportation, adhesion, anchoring,and fusion. As a member of this family, Rab7 protein is in charge of the delivery of internalised materials into degradative compartments and the acquisition of lysosomal hydrolases. Evidence from the previous studies showed that VP28 of white spot syndrome virus (WSSV) can bind with Rab7 in Penaeus monodon (PmRab7). By rapid amplification of cDNA ends (RACE) method, the full length gene of Fenneropenaeus chinensis Rab7 gene (fcrab7) was obtained. The total cDNA consists of a 615bp open reading frame (ORF), which encoded 205 amino acids with a predicted molecular mass of 23.2 kDa . The deduced amino acid sequence contained many conserved motifs and regions, and the entire protein has 100% homology with Rab7 of Litopenaeus vannamei and P. monodon. The recombined vector of pBAD/gIIIA-fcrab7 was constructed and transformed into E. coli. The fusion protein was successfully expressed by induction, which was tested by SDS-PAGE and Western blot analysis. These results laid a basis for further studies on interaction between WSSV and FcRab7.
