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...
Published in: | Fish & Shellfish Immunology |
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ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
2019
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Online Access: | http://ir.qdio.ac.cn/handle/337002/161104 http://ir.qdio.ac.cn/handle/337002/161105 https://doi.org/10.1016/j.fsi.2019.03.003 |
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ftchinacasciocas:oai:ir.qdio.ac.cn:337002/161105 2023-05-15T15:57:47+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/337002/161104 http://ir.qdio.ac.cn/handle/337002/161105 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/337002/161104 http://ir.qdio.ac.cn/handle/337002/161105 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 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 |
spellingShingle |
Crassostrea gigas Leucine-rich repeat domain Immunoglobulin domain LRRIG Pattern recognition receptor Immune effector Fisheries Immunology Marine & Freshwater Biology Veterinary Sciences 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 |
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/337002/161104 http://ir.qdio.ac.cn/handle/337002/161105 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/337002/161104 http://ir.qdio.ac.cn/handle/337002/161105 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 |
_version_ |
1766393474409562112 |