Rab7 is a member of the
Rab GTPases protein family, and it plays an essential role in regulating trafficking organelles in higher animals. However, recent studies showed that it also participated in the immune response and cytophagy against pathogens in invertebrates. In the present study, the full-length of Rab7 from Procambarus clarkii (PcRab7) was cloned, and its function during pathogen
infection and phagocytosis of haemocytes was also explored. The results showed that the full-length of PcRab7 was 3639 bp, containing a 618 bp open reading frame encoding 155
amino acids. The predicted molecular weight and isoelectric point of PcRab7 were 23.2 kDa and 5.77, respectively. PcRab7 was widely expressed in various tissues including haemocytes, intestine, muscle, gill, and hepatopancreas, and the highest expression level was in haemocytes. The
mRNA transcripts of PcRab7 in the main organs (gill, intestine, and hepatopancreas, and haemocytes) were significantly affected by white spot syndrome virus (WSSV) and Aeromonas veronii
infection. Subsequently, the prokaryotic and eukaryotic expression vectors were successfully constructed, and polyclonal
antibodies, which could specifically recognize the endogenous Rab7
protein, were also obtained. Furthermore, the phagocytosis rate of haemocytes against
FITC-labeled A. veronii was significantly decreased when the PcRab7 was silenced, while the over-expression of Rab7 increased the phagocytosis rate of haemocytes. The abnormal expression of Rab7
protein could also affect the survival rate of P. clarkii infected with WSSV or A. veronii. These results could provide a basis for further study on the immunological function of PcRab7.