A novel pathogen-binding gC1qR homolog, FcgC1qR, in the Chinese white shrimp, Fenneropenaeus chinensis.

In vertebrates, the globular "head" of complement component C1q receptor (gC1qR) is a versatile, multiligand binding protein. However, research on its function in invertebrates is limited. In the present study, a full-length cDNA sequence of a novel gC1qR homolog, FcgC1qR, from the Chinese white shrimp Fenneropenaeus chinensis was cloned. Semi-quantitative polymerase chain reaction (PCR) detected FcgC1qR in all examined tissues, with the highest level detected in the intestine. Western blot assay further revealed that the FcgC1qR protein was distributed in all tested tissues except the cell-free hemolymph of normal Chinese white shrimp. In the expression pattern study, quantitative real-time PCR demonstrated that the transcripts of FcgC1qR were up-regulated when challenged with bacteria (Vibrio anguillarum or Staphylococcus aureus) and white spot syndrome virus. Subsequently, FcgC1qR was over-expressed in Escherichia coli, and the polyclonal antibody was prepared with the purified recombinant protein. Microorganism binding was examined using Western blot assay, and revealed that FcgC1qR could bind to Bacillus cereus, Bacillus thuringiensis, S. aureus, V. anguillarum, Vibrioharveyi, and Candida albicans. FcgC1qR was also proven able to bind to S. aureus in a concentration-dependent manner, and this binding activity was partly inhibited by the polyclonal antibody. These results suggest that FcgC1qR may be involved in defending against bacterial infections in the Chinese white shrimp.