A C1q domain containing protein from scallop Chlamys farreri serving as pattern recognition receptor with heat-aggregated IgG binding activity.
BACKGROUND
The C1q domain containing (C1qDC) proteins refer to a family of all proteins that contain the globular C1q (gC1q) domain, and participate in a series of immune responses depending on their gC1q domains to bind a variety of self and non-self binding ligands.


METHODS
In the present study, the mRNA expression patterns, localization, and activities of a C1qDC protein from scallop Chlamys farreri (CfC1qDC) were investigated to understand its possible functions in innate immunity. The relative expression levels of CfC1qDC mRNA in hemocytes were all significantly up-regulated after four typical PAMPs (LPS, PGN, β-glucan and polyI:C) stimulation. During the embryonic development of scallop, the mRNA transcripts of CfC1qDC were detected in all the stages, and the expression level was up-regulated from D-hinged larva and reached the highest at eye-spot larva. The endogenous CfC1qDC was dominantly located in the hepatopancreas, gill, kidney and gonad of adult scallop through immunofluorescence. The recombinant protein of CfC1qDC (rCfC1qDC) could not only bind various PAMPs, such as LPS, PGN, β-glucan as well as polyI:C, but also enhance the phagocytic activity of scallop hemocytes towards Escherichia coli. Meanwhile, rCfC1qDC could interact with human heat-aggregated IgG, and this interaction could be inhibited by LPS.


CONCLUSIONS
All these results indicated that CfC1qDC in C. farreri not only served as a PRR involved in the PAMPs recognition, but also an opsonin participating in the clearance of invaders in innate immunity. Moreover, the ability of CfC1qDC to interact with immunoglobulins provided a clue to understand the evolution of classical pathway in complement system.
Key Laboratory of Experimental Marine Biology, Institute of Oceanology, Chinese Academy of Sciences, Qingdao, China.
Leilei
L
Wang
Lingling
L
Wang
Huan
H
Zhang
Zhi
Z
Zhou
Vinu S
VS
Siva
Linsheng
L
Song
D000818:Animals; D015922:Complement C1q / Q000737:chemistry*; D018076:DNA, Complementary / Q000378:metabolism; D006434:Hemocytes / Q000378:metabolism; D006801:Humans; D007107:Immune System; D007074:Immunoglobulin G / Q000378:metabolism; D008024:Ligands; D008070:Lipopolysaccharides / Q000737:chemistry; D008856:Microscopy, Fluorescence / Q000379:methods; D008958:Models, Molecular; D049897:Pectinidae; D010587:Phagocytosis; D011485:Protein Binding; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D012333:RNA, Messenger / Q000378:metabolism; D051381:Rats; D051192:Receptors, Pattern Recognition / Q000235:genetics; D011994:Recombinant Proteins / Q000378:metabolism; D013997:Time Factors
D018076:DNA, Complementary; D007074:Immunoglobulin G; D008024:Ligands; D008070:Lipopolysaccharides; D012333:RNA, Messenger; D051192:Receptors, Pattern Recognition; D011994:Recombinant Proteins; D015922:Complement C1q