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DM9 Domain Containing Protein Functions As a Pattern Recognition Receptor with Broad Microbial Recognition Spectrum
Jiang, Shuai1; Wang, Lingling2; Huang, Mengmeng1; Jia, Zhihao1; Weinert, Tobias3; Warkentin, Eberhard4; Liu, Conghui1; Song, Xiaorui1; Zhang, Haixia1; Witt, Jennifer4; Qiu, Limei1; Peng, Guohong1,4; Song, Linsheng2
2017-11-29
Source PublicationFRONTIERS IN IMMUNOLOGY
ISSN1664-3224
Volume8Pages:17
Corresponding AuthorPeng, Guohong(guohong.peng@biophys.mpg.de) ; Song, Linsheng(lshsong@dlou.edu.cn)
AbstractDM9 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.
Keywordinnate immunity pattern recognition receptor DM9 domain crystal structure mannose binding phagocytosis
DOI10.3389/fimmu.2017.01607
Indexed BySCI
Language英语
Funding ProjectNatural 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 Research AreaImmunology
WOS SubjectImmunology
WOS IDWOS:000416404600001
PublisherFRONTIERS MEDIA SA
Citation statistics
Document Type期刊论文
Identifierhttp://ir.qdio.ac.cn/handle/337002/157306
Collection实验海洋生物学重点实验室
Corresponding AuthorPeng, Guohong; Song, Linsheng
Affiliation1.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
First Author AffilicationInstitute of Oceanology, Chinese Academy of Sciences
Corresponding Author AffilicationInstitute of Oceanology, Chinese Academy of Sciences
Recommended Citation
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.
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