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...

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Bibliographic Details
Published in:Frontiers in Immunology
Main Authors: Shuai Jiang, Lingling Wang, Mengmeng Huang, Zhihao Jia, Tobias Weinert, Eberhard Warkentin, Conghui Liu, Xiaorui Song, Haixia Zhang, Jennifer Witt, Limei Qiu, Guohong Peng, Linsheng Song
Format: Article in Journal/Newspaper
Language:English
Published: Frontiers Media S.A. 2017
Subjects:
innate immunity
pattern recognition receptor
DM9 domain
crystal structure
mannose binding
phagocytosis
Immunologic diseases. Allergy
RC581-607
Crassostrea gigas
Online Access:https://doi.org/10.3389/fimmu.2017.01607
https://doaj.org/article/fe66db9b86884abab550606c035fdf11
Description
Summary: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 β-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.

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