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A tandem-repeat galectin-1 from Apostichopus japonicus with broad PAMP recognition pattern and antibacterial activity.
Fish Shellfish Immunol. 2020 Apr; 99:167-175.FS

Abstract

Galectins belong to the family of carbohydrate-binding proteins and play major roles in the immune and inflammatory responses of both vertebrates and invertebrates. In the present study, one novel galectin-1 protein named AjGal-1 was identified from Apostichopus japonicas with an open reading frame of 1179 bp encoding a polypeptide of 392 amino acids. The deduced amino acids sequence of AjGal-1 contained three carbohydrate recognition domains (CRDs) which shared 34-37% identity with that of other galectin proteins from echinodermata, fishes, and birds. In the phylogenetic tree, AjGal-1 was closely clustered with galectins from Mesocentrotus nudus and Paracentrotus lividus. The mRNA transcripts of AjGal-1 were ubiquitously expressed in all the detected tissues, including gut, longitudinal muscle, gonad, coelomocytes, respiratory tree, tentacle and body wall, with the highest expression level in coelomocytes. After Vibrio splendidus stimulation, the mRNA expression levels of AjGal-1 in coelomocytes were significantly increased at 6 and 12 h (P < 0.01) compared with that in control group, and went back to normal level at 72 h. The recombinant protein of AjGal-1 (rAjGal-1) could bind various PAMPs including d-galactose, lipopolysaccharide (LPS), peptidoglycan (PGN) and mannose (Man), and exhibited the highest affinity to d-galactose. Meanwhile, rAjGal-1 could also bind and agglutinate different kinds of microorganisms, including gram-negative bacteria (V. splendidus and Escherichia coli), gram-positive bacteria (Micrococus leteus), and fungi (Pichia pastoris). rAjGal-1 also exhibited anti-microbial activity against V. splendidus and E. coli. All these results suggested that AjGal-1 could function as an important PRR with broad spectrum of microbial recognition and anti-microbial activity against the invading pathogen in A. japonicas.

Authors+Show Affiliations

School of Marine Sciences, Ningbo University, Ningbo, 315211, China.Liaoning Key Laboratory of Marine Animal Immunology, Dalian Ocean University, Dalian, 116023, China; Liaoning Key Laboratory of Marine Animal Immunology & Disease Control, Dalian Ocean University, Dalian, 116023, China; Dalian Key Laboratory of Aquatic Animal Disease Prevention and Control, Dalian Ocean University, Dalian, 116023, China.Liaoning Key Laboratory of Marine Animal Immunology, Dalian Ocean University, Dalian, 116023, China; Laboratory of Marine Fisheries Science and Food Production Processes, Qingdao National Laboratory for Marine Science and Technology, Qingdao, 266235, China; Liaoning Key Laboratory of Marine Animal Immunology & Disease Control, Dalian Ocean University, Dalian, 116023, China; Dalian Key Laboratory of Aquatic Animal Disease Prevention and Control, Dalian Ocean University, Dalian, 116023, China.Liaoning Key Laboratory of Marine Animal Immunology, Dalian Ocean University, Dalian, 116023, China; Liaoning Key Laboratory of Marine Animal Immunology & Disease Control, Dalian Ocean University, Dalian, 116023, China; Dalian Key Laboratory of Aquatic Animal Disease Prevention and Control, Dalian Ocean University, Dalian, 116023, China.School of Marine Sciences, Ningbo University, Ningbo, 315211, China; Liaoning Key Laboratory of Marine Animal Immunology, Dalian Ocean University, Dalian, 116023, China; Liaoning Key Laboratory of Marine Animal Immunology & Disease Control, Dalian Ocean University, Dalian, 116023, China.Liaoning Key Laboratory of Marine Animal Immunology, Dalian Ocean University, Dalian, 116023, China; Liaoning Key Laboratory of Marine Animal Immunology & Disease Control, Dalian Ocean University, Dalian, 116023, China; Dalian Key Laboratory of Aquatic Animal Disease Prevention and Control, Dalian Ocean University, Dalian, 116023, China.Laboratory of Marine Fisheries Science and Food Production Processes, Qingdao National Laboratory for Marine Science and Technology, Qingdao, 266235, China; Liaoning Key Laboratory of Marine Animal Immunology, Dalian Ocean University, Dalian, 116023, China; Liaoning Key Laboratory of Marine Animal Immunology & Disease Control, Dalian Ocean University, Dalian, 116023, China; Dalian Key Laboratory of Aquatic Animal Disease Prevention and Control, Dalian Ocean University, Dalian, 116023, China.School of Marine Sciences, Ningbo University, Ningbo, 315211, China.Laboratory of Marine Fisheries Science and Food Production Processes, Qingdao National Laboratory for Marine Science and Technology, Qingdao, 266235, China; Liaoning Key Laboratory of Marine Animal Immunology, Dalian Ocean University, Dalian, 116023, China; Liaoning Key Laboratory of Marine Animal Immunology & Disease Control, Dalian Ocean University, Dalian, 116023, China; Dalian Key Laboratory of Aquatic Animal Disease Prevention and Control, Dalian Ocean University, Dalian, 116023, China. Electronic address: lshsong@dlou.edu.cn.

Pub Type(s)

Journal Article

Language

eng

PubMed ID

32044463

Citation

Zhang, Chi, et al. "A Tandem-repeat Galectin-1 From Apostichopus Japonicus With Broad PAMP Recognition Pattern and Antibacterial Activity." Fish & Shellfish Immunology, vol. 99, 2020, pp. 167-175.
Zhang C, Xue Z, Yu Z, et al. A tandem-repeat galectin-1 from Apostichopus japonicus with broad PAMP recognition pattern and antibacterial activity. Fish Shellfish Immunol. 2020;99:167-175.
Zhang, C., Xue, Z., Yu, Z., Wang, H., Liu, Y., Li, H., Wang, L., Li, C., & Song, L. (2020). A tandem-repeat galectin-1 from Apostichopus japonicus with broad PAMP recognition pattern and antibacterial activity. Fish & Shellfish Immunology, 99, 167-175. https://doi.org/10.1016/j.fsi.2020.02.011
Zhang C, et al. A Tandem-repeat Galectin-1 From Apostichopus Japonicus With Broad PAMP Recognition Pattern and Antibacterial Activity. Fish Shellfish Immunol. 2020;99:167-175. PubMed PMID: 32044463.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - A tandem-repeat galectin-1 from Apostichopus japonicus with broad PAMP recognition pattern and antibacterial activity. AU - Zhang,Chi, AU - Xue,Zhuang, AU - Yu,Zichao, AU - Wang,Hui, AU - Liu,Yu, AU - Li,Huan, AU - Wang,Lingling, AU - Li,Chenghua, AU - Song,Linsheng, Y1 - 2020/02/07/ PY - 2019/12/19/received PY - 2020/01/31/revised PY - 2020/02/05/accepted PY - 2020/2/12/pubmed PY - 2020/2/12/medline PY - 2020/2/12/entrez KW - Anti-microbial activity KW - Apostichopus japonicus KW - Galectin KW - Innate immunity KW - Microbial recognition SP - 167 EP - 175 JF - Fish & shellfish immunology JO - Fish Shellfish Immunol. VL - 99 N2 - Galectins belong to the family of carbohydrate-binding proteins and play major roles in the immune and inflammatory responses of both vertebrates and invertebrates. In the present study, one novel galectin-1 protein named AjGal-1 was identified from Apostichopus japonicas with an open reading frame of 1179 bp encoding a polypeptide of 392 amino acids. The deduced amino acids sequence of AjGal-1 contained three carbohydrate recognition domains (CRDs) which shared 34-37% identity with that of other galectin proteins from echinodermata, fishes, and birds. In the phylogenetic tree, AjGal-1 was closely clustered with galectins from Mesocentrotus nudus and Paracentrotus lividus. The mRNA transcripts of AjGal-1 were ubiquitously expressed in all the detected tissues, including gut, longitudinal muscle, gonad, coelomocytes, respiratory tree, tentacle and body wall, with the highest expression level in coelomocytes. After Vibrio splendidus stimulation, the mRNA expression levels of AjGal-1 in coelomocytes were significantly increased at 6 and 12 h (P < 0.01) compared with that in control group, and went back to normal level at 72 h. The recombinant protein of AjGal-1 (rAjGal-1) could bind various PAMPs including d-galactose, lipopolysaccharide (LPS), peptidoglycan (PGN) and mannose (Man), and exhibited the highest affinity to d-galactose. Meanwhile, rAjGal-1 could also bind and agglutinate different kinds of microorganisms, including gram-negative bacteria (V. splendidus and Escherichia coli), gram-positive bacteria (Micrococus leteus), and fungi (Pichia pastoris). rAjGal-1 also exhibited anti-microbial activity against V. splendidus and E. coli. All these results suggested that AjGal-1 could function as an important PRR with broad spectrum of microbial recognition and anti-microbial activity against the invading pathogen in A. japonicas. SN - 1095-9947 UR - https://www.unboundmedicine.com/medline/citation/32044463/A_tandem-repeat_galectin-1_from_Apostichopus_japonicus_with_broad_PAMP_recognition_pattern_and_antibacterial_activity L2 - https://linkinghub.elsevier.com/retrieve/pii/S1050-4648(20)30082-6 DB - PRIME DP - Unbound Medicine ER -
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