DM9 Domain Containing Protein Functions As a Pattern Recognition Receptor with Broad Microbial Recognition Spectrum

doi:10.3389/fimmu.2017.01607

CORC > 海洋研究所 > 中国科学院海洋研究所 > 实验海洋生物学重点实验室

	DM9 Domain Containing Protein Functions As a Pattern Recognition Receptor with Broad Microbial Recognition Spectrum
	Jiang, Shuai 1; Wang, Lingling 2; Huang, Mengmeng1 ; Jia, Zhihao 1; Weinert, Tobias 3; Warkentin, Eberhard 4; Liu, Conghui1 ; Song, Xiaorui1 ; Zhang, Haixia 1; Witt, Jennifer 4
刊名	FRONTIERS IN IMMUNOLOGY
	2017-11-29
卷号	8 页码:17
关键词	innate immunity pattern recognition receptor DM9 domain crystal structure mannose binding phagocytosis
ISSN号	1664-3224
DOI	10.3389/fimmu.2017.01607
通讯作者	Peng, Guohong(guohong.peng@biophys.mpg.de) ; Song, Linsheng(lshsong@dlou.edu.cn)
英文摘要	DM9 domain was first identified in Drosophila melanogaster, and it was subsequently found to integrate with or without other protein domains across a wide range of invertebrates and vertebrates. In the present study, a member of DM9 domain containing protein (DM9CP) family from marine invertebrate Crassostrea gigas (designated CgDM9CP-1), which was only composed of two DM9 domains, was taken as a protein model to study the biological functions of DM9 domain and its molecular determinants. CgDM9CP-1 was found to exhibit high binding specificity and avidity toward D-mannose residue. It served as a pattern recognition receptor (PRR) with a broad range of recognition spectrum to various pathogen-associated molecular patterns, including lipopolysaccharide, peptidylglycan, mannan, and beta-1, 3-glucan in a D-mannose-dependent manner, as well as bacteria and fungi. In order to reveal the molecular mechanism underlying its pattern recognition activity, the crystal structures of wild-type and loss-of-function mutants were solved, and Asp22 and Lys43 were found to be the critical residues for ligand recognition. Moreover, CgDM9CP-1 protein was found to mainly distribute on the surface of C. gigas hemocytes, and it could be translocated into cytoplasm and colocalized with the engulfed microbes during hemocyte phagocytosis. The present result clearly indicated that CgDM9CP-1 was a PRR, and it provided an important clue for the better understanding of DM9CP function.
资助项目	Natural Science Foundation of China[31530069] ; Natural Science Foundation of China[41406170] ; High Technology Project (863 Program) from the Chinese Ministry of Science and Technology[2014AA093501] ; Dalian High Level Talent Innovation Support Program[2015R020] ; Research Foundation for Distinguished Professor in Liaoning ; Talented Scholars in Dalian Ocean University ; Earmarked Fund for Modern Agro-industry Technology Research System[CARS-49] ; Max-Planck-Gesellschaft
WOS研究方向	Immunology
语种	英语
出版者	FRONTIERS MEDIA SA
WOS记录号	WOS:000416404600001
内容类型	期刊论文
源URL	[http://ir.qdio.ac.cn/handle/337002/157305]
专题	海洋研究所_实验海洋生物学重点实验室
通讯作者	Peng, Guohong; Song, Linsheng
作者单位	1.Chinese Acad Sci, Inst Oceanol, Key Lab Expt Marine Biol, Qingdao, Peoples R China 2.Dalian Ocean Univ, Liaoning Key Lab Marine Anim Immunol Dis Control, Dalian, Peoples R China 3.Paul Scherrer Inst, Lab Biomol Res, Villigen, Switzerland 4.Max Planck Inst Biophys, Dept Mol Membrane Biol, Frankfurt, Germany
推荐引用方式 GB/T 7714	Jiang, Shuai,Wang, Lingling,Huang, Mengmeng,et al. DM9 Domain Containing Protein Functions As a Pattern Recognition Receptor with Broad Microbial Recognition Spectrum[J]. FRONTIERS IN IMMUNOLOGY,2017,8:17.
APA	Jiang, Shuai.,Wang, Lingling.,Huang, Mengmeng.,Jia, Zhihao.,Weinert, Tobias.,...&Song, Linsheng.(2017).DM9 Domain Containing Protein Functions As a Pattern Recognition Receptor with Broad Microbial Recognition Spectrum.FRONTIERS IN IMMUNOLOGY,8,17.
MLA	Jiang, Shuai,et al."DM9 Domain Containing Protein Functions As a Pattern Recognition Receptor with Broad Microbial Recognition Spectrum".FRONTIERS IN IMMUNOLOGY 8(2017):17.