An alternative function of C-type lectin comprising low-density lipoprotein receptor domain from Fenneropenaeus merguiensis to act as a binding receptor for viral protein and vitellogenin.

A diversity of C-type lectins (CTLs) was coming reported and they are known to participate in invertebrate innate immunity by act as pattern recognition receptor (PRR). In the present study, a unique CTL containing low-density lipoprotein receptor (LDLR) domain from Fenneropenaeus merguiensis (designated as FmLdlr) was cloned. Its sequence contained a single LDLR domain and one carbohydrate recognition domain (CRD) with a QAP motif putative for galactose-specific binding. The expression of FmLdlr was detected only in hemocytes of healthy shrimp. Its expression was significantly up-regulated by Vibrio parahaemolyticus or white spot syndrome virus (WSSV) challenge. The knockdown by FmLdlr dsRNA resulted in severe gene down-regulation. The gene silencing with pathogenic co-inoculation led to reduction of the median lethal time and increasing in the cumulative mortality including the remained WSSV in WSSV co-challenge group. Recombinant proteins of FmLdlr and two domains could agglutinate various bacterial strains which LDLR domain revealed the lowest activity. Only FmLdlr and CRD could enhance phagocytosis and encapsulation by hemocytes. Both FmLdlr and CRD except LDLR domain exhibited the antibacterial activity by inhibiting the growth of pathogenic V. parahaemolyticus in cultured medium and disk diffusion assay. Only FmLdlr and CRD could bind to WSSV proteins, envelope VP28, tegument VP39A and also capsid VP15, which FmLdlr had the higher binding affinity than that of CRD. Altogether, we concluded that FmLdlr contributed in shrimp immune defense through the main action of CRD in capable of bacterial agglutination, enhancing the phagocytosis and encapsulation, antimicrobial activity and binding to viral proteins. Interestingly, ELISA approach revealed that LDLR domain displayed the highest binding affinity to vitellogenin than whole molecule and CRD. We signified a new function of FmLdlr that it might presumably act as a receptor for vitellogenin transportation in hemolymph during vitellogenesis of shrimp.