Characterization of a gC1qR homolog from sea cucumber Apostichopus japonicus.

gC1qR is a multifunctional and multiligand binding protein that plays important roles in inflammation and infection. In this study, a novel gC1qR homolog called AjgC1qR from the invertebrate sea cucumber Apostichopus japonicus was cloned and characterized. The open reading frame of AjgC1qR encoded 292 amino acid residues with a conserved mitochondrial targeting sequence and MAM33 domain. Multiple sequence alignment and phylogenetic analyses proved that AjgC1qR is a homolog of the gC1qR family. Spatial mRNA transcription in five tissues revealed the ubiquitous expression of AjgC1qR. The highest and lowest levels of expression were found in the tentacle and muscle, respectively, and AjgC1qR expression was remarkably up-regulated in coelomocytes after Vibrio splendidus challenge. Moreover, the recombinant rAjgC1qR protein exhibited high binding activity toward pathogen-associated molecules, such as lipopolysaccharides, peptidoglycan, and mannan. These findings demonstrate that AjgC1qR may play important roles in innate immunity and function as a pathogen recognition receptor.