PUBLICATION
The hepatic lectin of zebrafish binds a wide range of bacteria and participates in immune defense
- Authors
- Yang, Q., Wang, P., Wang, S., Wang, Y., Feng, S., Zhang, S., Li, H.
- ID
- ZDB-PUB-180820-17
- Date
- 2018
- Source
- Fish & shellfish immunology 82: 267-278 (Journal)
- Registered Authors
- Li, Hongyan
- Keywords
- C-type lectin, Danio rerio, Hepatic lectin, Innate immunity, Zebrafish
- MeSH Terms
-
- Amino Acid Sequence
- Animals
- Asialoglycoprotein Receptor/chemistry
- Asialoglycoprotein Receptor/genetics
- Asialoglycoprotein Receptor/immunology*
- Base Sequence
- Fish Diseases/immunology*
- Fish Proteins/chemistry
- Fish Proteins/genetics
- Fish Proteins/immunology
- Gene Expression Profiling/veterinary
- Gene Expression Regulation/immunology*
- Gram-Negative Bacteria/physiology
- Gram-Positive Bacteria/physiology
- Immunity, Innate/genetics*
- Lectins, C-Type/chemistry
- Lectins, C-Type/genetics
- Lectins, C-Type/immunology*
- Lipopolysaccharides/pharmacology
- Phylogeny
- Sequence Alignment/veterinary
- Teichoic Acids/pharmacology
- Zebrafish/genetics*
- Zebrafish/immunology*
- Zebrafish Proteins/chemistry
- Zebrafish Proteins/genetics
- Zebrafish Proteins/immunology*
- PubMed
- 30120977 Full text @ Fish Shellfish Immunol.
Citation
Yang, Q., Wang, P., Wang, S., Wang, Y., Feng, S., Zhang, S., Li, H. (2018) The hepatic lectin of zebrafish binds a wide range of bacteria and participates in immune defense. Fish & shellfish immunology. 82:267-278.
Abstract
C-type lectins (CTLs) have a diverse range of functions including cell-cell adhesion, immune response to pathogens and apoptosis. Asialoglycoprotein receptor (ASGPR), also known as hepatic lectin, a member of CTLs, was the first animal lectin identified, yet information regarding it remains rather limited in teleost. In this study, we identified a putative protein in zebrafish, named as the zebrafish hepatic lectin (Zhl). The zhl encoded a typical Ca2+-dependent carbohydrate-binding protein, and was mainly expressed in the liver in a tissue specific fashion. Challenge with LPS and LTA resulted in significant up-regulation of zhl expression, suggesting involvement in immune response. Actually, recombinant C-type lectin domain (rCTLD) of Zhl was found to be capable of agglutinating and binding to both Gram-negative and Gram-positive bacteria and enhancing the phagocytosis of the bacteria by macrophages. Moreover, rCTLD specifically bound to insoluble lipopolysaccharide (LPS), lipoteichoic acid (LTA) and peptidoglycan (PGN), which were inhibited by galactose. Interestingly, Zhl was located in the membrane, and its overexpression could inhibit the production of pre-inflammatory cytokines. Taken together, these results indicate that Zhl has immune activity capable of defending invading pathogens, enriching our understanding of the function of ASGPR/hepatic lectin.
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping