A novel LRR and Ig domain-containing protein could function as an immune effector in Crassostrea gigas

A variety of combinations of leucine-rich repeat (LRR) and immunoglobulin-like (Ig) domains have been found and discovered in invertebrates and vertebrates, but the functions remain largely unexplored. In the present study, a novel LRR and Ig domain-containing protein (LRRIG), CgLRRIG-3, was identif...

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Published in:Fish & Shellfish Immunology
Main Authors: Wang, Xiudan, Zhao, Xiaoli, Yan, Chunyu, Jia, Zhihao, Lv, Zhao, Ma, Cuiping, Wang, Mengqiang
Format: Report
Language:English
Published: ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD 2019
Subjects:
Psi
Online Access:http://ir.qdio.ac.cn/handle/337002/161103
https://doi.org/10.1016/j.fsi.2019.03.003
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spelling ftchinacasciocas:oai:ir.qdio.ac.cn:337002/161103 2023-05-15T15:57:51+02:00 A novel LRR and Ig domain-containing protein could function as an immune effector in Crassostrea gigas Wang, Xiudan Zhao, Xiaoli Yan, Chunyu Jia, Zhihao Lv, Zhao Ma, Cuiping Wang, Mengqiang 2019-05-01 http://ir.qdio.ac.cn/handle/337002/161103 https://doi.org/10.1016/j.fsi.2019.03.003 英语 eng ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD FISH & SHELLFISH IMMUNOLOGY http://ir.qdio.ac.cn/handle/337002/161103 doi:10.1016/j.fsi.2019.03.003 Crassostrea gigas Leucine-rich repeat domain Immunoglobulin domain LRRIG Pattern recognition receptor Immune effector Fisheries Immunology Marine & Freshwater Biology Veterinary Sciences LEUCINE-RICH REPEAT SOLUBLE ADENYLYL-CYCLASE ONLY PROTEINS RECOGNITION SUPERFAMILY EXPRESSION PATTERN PHAGOCYTOSIS MECHANISMS COMPLEXITY 期刊论文 2019 ftchinacasciocas https://doi.org/10.1016/j.fsi.2019.03.003 2022-06-27T05:40:38Z A variety of combinations of leucine-rich repeat (LRR) and immunoglobulin-like (Ig) domains have been found and discovered in invertebrates and vertebrates, but the functions remain largely unexplored. In the present study, a novel LRR and Ig domain-containing protein (LRRIG), CgLRRIG-3, was identified and characterized from oyster Crassostrea gigas. It contained two typical LRR motifs, a LRRNT motif and an Ig domain and PSI-BALST and phylogeny analysis revealed that the sequence of CgLRRIG-3 was most related with leucine-rich repeat neuronal 1 proteins from vertebrate. Its mRNA transcripts were constitutively expressed in muscle, gill, hepatopancreas, mantle, gonad and hemocytes with the highest level in hepatopancreas. The mRNA expression level of CgLRRIG-3 in hemocytes could respond to the stimulations of variety PAMPs including lipopolysaccharide (LPS), peptidoglycan (PGN), glucan (GLU) and polyinosinic-polycytidylic acid (poly I:C). The recombinant proteins exhibited a wide PAMP binding repertoire to four typical PAMPs and could significantly induce the expression of CgTNF-1 and CgIL17-5 as well as increase phagocytosis in primary cultured oyster hemocytes. In hepatopancreas, CgLRRIG-3 was mainly distributed in the basolateral membrane of digestive tubule and the hemocoel sinusoid between the digestive tubules. And in hemocytes, the positive signal was mainly distributed in a special group of granulocytes. These results collectively indicated that CgLRRIG-3 could not only function as an immune effector. Report Crassostrea gigas Institute of Oceanology, Chinese Academy of Sciences: IOCAS-IR Psi ENVELOPE(-63.000,-63.000,-64.300,-64.300) Fish & Shellfish Immunology 88 318 327
institution Open Polar
collection Institute of Oceanology, Chinese Academy of Sciences: IOCAS-IR
op_collection_id ftchinacasciocas
language English
topic Crassostrea gigas
Leucine-rich repeat domain
Immunoglobulin domain
LRRIG
Pattern recognition receptor
Immune effector
Fisheries
Immunology
Marine & Freshwater Biology
Veterinary Sciences
LEUCINE-RICH REPEAT
SOLUBLE ADENYLYL-CYCLASE
ONLY PROTEINS
RECOGNITION
SUPERFAMILY
EXPRESSION
PATTERN
PHAGOCYTOSIS
MECHANISMS
COMPLEXITY
spellingShingle Crassostrea gigas
Leucine-rich repeat domain
Immunoglobulin domain
LRRIG
Pattern recognition receptor
Immune effector
Fisheries
Immunology
Marine & Freshwater Biology
Veterinary Sciences
LEUCINE-RICH REPEAT
SOLUBLE ADENYLYL-CYCLASE
ONLY PROTEINS
RECOGNITION
SUPERFAMILY
EXPRESSION
PATTERN
PHAGOCYTOSIS
MECHANISMS
COMPLEXITY
Wang, Xiudan
Zhao, Xiaoli
Yan, Chunyu
Jia, Zhihao
Lv, Zhao
Ma, Cuiping
Wang, Mengqiang
A novel LRR and Ig domain-containing protein could function as an immune effector in Crassostrea gigas
topic_facet Crassostrea gigas
Leucine-rich repeat domain
Immunoglobulin domain
LRRIG
Pattern recognition receptor
Immune effector
Fisheries
Immunology
Marine & Freshwater Biology
Veterinary Sciences
LEUCINE-RICH REPEAT
SOLUBLE ADENYLYL-CYCLASE
ONLY PROTEINS
RECOGNITION
SUPERFAMILY
EXPRESSION
PATTERN
PHAGOCYTOSIS
MECHANISMS
COMPLEXITY
description A variety of combinations of leucine-rich repeat (LRR) and immunoglobulin-like (Ig) domains have been found and discovered in invertebrates and vertebrates, but the functions remain largely unexplored. In the present study, a novel LRR and Ig domain-containing protein (LRRIG), CgLRRIG-3, was identified and characterized from oyster Crassostrea gigas. It contained two typical LRR motifs, a LRRNT motif and an Ig domain and PSI-BALST and phylogeny analysis revealed that the sequence of CgLRRIG-3 was most related with leucine-rich repeat neuronal 1 proteins from vertebrate. Its mRNA transcripts were constitutively expressed in muscle, gill, hepatopancreas, mantle, gonad and hemocytes with the highest level in hepatopancreas. The mRNA expression level of CgLRRIG-3 in hemocytes could respond to the stimulations of variety PAMPs including lipopolysaccharide (LPS), peptidoglycan (PGN), glucan (GLU) and polyinosinic-polycytidylic acid (poly I:C). The recombinant proteins exhibited a wide PAMP binding repertoire to four typical PAMPs and could significantly induce the expression of CgTNF-1 and CgIL17-5 as well as increase phagocytosis in primary cultured oyster hemocytes. In hepatopancreas, CgLRRIG-3 was mainly distributed in the basolateral membrane of digestive tubule and the hemocoel sinusoid between the digestive tubules. And in hemocytes, the positive signal was mainly distributed in a special group of granulocytes. These results collectively indicated that CgLRRIG-3 could not only function as an immune effector.
format Report
author Wang, Xiudan
Zhao, Xiaoli
Yan, Chunyu
Jia, Zhihao
Lv, Zhao
Ma, Cuiping
Wang, Mengqiang
author_facet Wang, Xiudan
Zhao, Xiaoli
Yan, Chunyu
Jia, Zhihao
Lv, Zhao
Ma, Cuiping
Wang, Mengqiang
author_sort Wang, Xiudan
title A novel LRR and Ig domain-containing protein could function as an immune effector in Crassostrea gigas
title_short A novel LRR and Ig domain-containing protein could function as an immune effector in Crassostrea gigas
title_full A novel LRR and Ig domain-containing protein could function as an immune effector in Crassostrea gigas
title_fullStr A novel LRR and Ig domain-containing protein could function as an immune effector in Crassostrea gigas
title_full_unstemmed A novel LRR and Ig domain-containing protein could function as an immune effector in Crassostrea gigas
title_sort novel lrr and ig domain-containing protein could function as an immune effector in crassostrea gigas
publisher ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
publishDate 2019
url http://ir.qdio.ac.cn/handle/337002/161103
https://doi.org/10.1016/j.fsi.2019.03.003
long_lat ENVELOPE(-63.000,-63.000,-64.300,-64.300)
geographic Psi
geographic_facet Psi
genre Crassostrea gigas
genre_facet Crassostrea gigas
op_relation FISH & SHELLFISH IMMUNOLOGY
http://ir.qdio.ac.cn/handle/337002/161103
doi:10.1016/j.fsi.2019.03.003
op_doi https://doi.org/10.1016/j.fsi.2019.03.003
container_title Fish & Shellfish Immunology
container_volume 88
container_start_page 318
op_container_end_page 327
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