Journal
DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY
Volume 116, Issue -, Pages -Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.dci.2020.103937
Keywords
Crassostrea gigas; DM9 domain; Pathogen recognition; Encapsulation
Categories
Funding
- National Key RD Project [2018YFD0900502]
- National Science Foundation of China [41961124009, U1706204]
- earmarked fund from Modern Agro-industry Technology Research System [CARS-49]
- Fund for Outstanding Talents and Innovative Team of Agricultural Scientific Research in the Ministry of Agriculture, Key R&D Program of Liaoning Province [2017203001]
- Research Foundation for Distinguished Professor in Liaoning [XLYC1902012]
- AoShan Talents Cultivation Program
- Qingdao National Laboratory for Marine Science and Technology [2017ASTCP-OS13]
- Research Foundation for Talented Scholars in Dalian Ocean University
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DM9 domain containing protein (DM9CP) is a pattern recognition molecule found in most organisms except plants. A novel DM9-containing protein (CgDM9CP-3) was identified in Pacific oyster Crassostrea gigas, with high expression in gills and cytomembrane of haemocytes. CgDM9CP-3 can be significantly up-regulated after pathogen stimulations and has the ability to interact with various microorganisms.
DM9 domain containing protein (DM9CP) is a recently identified pattern recognition molecules exiting in most organisms except plants. In the present study, a novel DM9-containing protein (CgDM9CP-3) was identified from Pacific oyster Crassostrea gigas with an open reading frame of 438 bp, encoding a polypeptide of 145 amino acids containing two tandem DM9 repeats. The deduced amino acid sequence of CgDM9CP-3 shared 52.4% and 58.6% identity with CgDM9CP-1 and CgDM9CP-2, respectively. The mRNA transcripts of CgDM9CP-3 were highest expressed in oyster gills and its protein was mainly distributed in cytomembrane of haemocytes. After the stimulations with Vibrio splendidus and mannose, the mRNA expression of CgDM9CP-3 in oyster gills was significantly up-regulated and reached the peak level at 12 h and 24 h (p < 0.05), which was 7.80-fold (p < 0.05) and 42.82-fold (p < 0.05) of that in the control group, respectively. The recombinant CgDM9CP-3 protein (rCgDM9CP-3) was able to bind LPS, PGN and D-Mannose, fungi Pichia pastoris and Yarrowia lipolytica, as well as gram-negative bacteria Escherichia coli, Vibrio anguillarum and V. splendidus in a Ca2+-dependent manner. Moreover, it could enhance the encapsulation of haemocytes and exhibited agglutination activity towards fungi P. pastoris and Y. lipolytica in vitro with Ca2+. These results suggested that CgDM9CP-3 not only acted as a PRR involved in the pathogen recognition, but also enhanced cellular encapsulation in oyster C. gigas.
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