DM9 Domain Containing Protein Functions As a Pattern Recognition Receptor with Broad Microbial Recognition Spectrum
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 C...
Published in: | Frontiers in Immunology |
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Online Access: | http://ir.qdio.ac.cn/handle/337002/157305 http://ir.qdio.ac.cn/handle/337002/157306 https://doi.org/10.3389/fimmu.2017.01607 |
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ftchinacasciocas:oai:ir.qdio.ac.cn:337002/157306 2023-05-15T15:58:51+02:00 DM9 Domain Containing Protein Functions As a Pattern Recognition Receptor with Broad Microbial Recognition Spectrum Jiang, Shuai Wang, Lingling Huang, Mengmeng Jia, Zhihao Weinert, Tobias Warkentin, Eberhard Liu, Conghui Song, Xiaorui Zhang, Haixia Witt, Jennifer Qiu, Limei Peng, Guohong Song, Linsheng 2017-11-29 http://ir.qdio.ac.cn/handle/337002/157305 http://ir.qdio.ac.cn/handle/337002/157306 https://doi.org/10.3389/fimmu.2017.01607 英语 eng FRONTIERS MEDIA SA FRONTIERS IN IMMUNOLOGY http://ir.qdio.ac.cn/handle/337002/157305 http://ir.qdio.ac.cn/handle/337002/157306 doi:10.3389/fimmu.2017.01607 innate immunity pattern recognition receptor DM9 domain crystal structure mannose binding phagocytosis Immunology 期刊论文 2017 ftchinacasciocas https://doi.org/10.3389/fimmu.2017.01607 2022-06-27T05:39:24Z 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. Report Crassostrea gigas Institute of Oceanology, Chinese Academy of Sciences: IOCAS-IR Frontiers in Immunology 8 |
institution |
Open Polar |
collection |
Institute of Oceanology, Chinese Academy of Sciences: IOCAS-IR |
op_collection_id |
ftchinacasciocas |
language |
English |
topic |
innate immunity pattern recognition receptor DM9 domain crystal structure mannose binding phagocytosis Immunology |
spellingShingle |
innate immunity pattern recognition receptor DM9 domain crystal structure mannose binding phagocytosis Immunology Jiang, Shuai Wang, Lingling Huang, Mengmeng Jia, Zhihao Weinert, Tobias Warkentin, Eberhard Liu, Conghui Song, Xiaorui Zhang, Haixia Witt, Jennifer Qiu, Limei Peng, Guohong Song, Linsheng DM9 Domain Containing Protein Functions As a Pattern Recognition Receptor with Broad Microbial Recognition Spectrum |
topic_facet |
innate immunity pattern recognition receptor DM9 domain crystal structure mannose binding phagocytosis Immunology |
description |
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. |
format |
Report |
author |
Jiang, Shuai Wang, Lingling Huang, Mengmeng Jia, Zhihao Weinert, Tobias Warkentin, Eberhard Liu, Conghui Song, Xiaorui Zhang, Haixia Witt, Jennifer Qiu, Limei Peng, Guohong Song, Linsheng |
author_facet |
Jiang, Shuai Wang, Lingling Huang, Mengmeng Jia, Zhihao Weinert, Tobias Warkentin, Eberhard Liu, Conghui Song, Xiaorui Zhang, Haixia Witt, Jennifer Qiu, Limei Peng, Guohong Song, Linsheng |
author_sort |
Jiang, Shuai |
title |
DM9 Domain Containing Protein Functions As a Pattern Recognition Receptor with Broad Microbial Recognition Spectrum |
title_short |
DM9 Domain Containing Protein Functions As a Pattern Recognition Receptor with Broad Microbial Recognition Spectrum |
title_full |
DM9 Domain Containing Protein Functions As a Pattern Recognition Receptor with Broad Microbial Recognition Spectrum |
title_fullStr |
DM9 Domain Containing Protein Functions As a Pattern Recognition Receptor with Broad Microbial Recognition Spectrum |
title_full_unstemmed |
DM9 Domain Containing Protein Functions As a Pattern Recognition Receptor with Broad Microbial Recognition Spectrum |
title_sort |
dm9 domain containing protein functions as a pattern recognition receptor with broad microbial recognition spectrum |
publisher |
FRONTIERS MEDIA SA |
publishDate |
2017 |
url |
http://ir.qdio.ac.cn/handle/337002/157305 http://ir.qdio.ac.cn/handle/337002/157306 https://doi.org/10.3389/fimmu.2017.01607 |
genre |
Crassostrea gigas |
genre_facet |
Crassostrea gigas |
op_relation |
FRONTIERS IN IMMUNOLOGY http://ir.qdio.ac.cn/handle/337002/157305 http://ir.qdio.ac.cn/handle/337002/157306 doi:10.3389/fimmu.2017.01607 |
op_doi |
https://doi.org/10.3389/fimmu.2017.01607 |
container_title |
Frontiers in Immunology |
container_volume |
8 |
_version_ |
1766394623974965248 |