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Tytuł:
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A C-type lectin with a single CRD from Onychostoma macrolepis mediates immune recognition against bacterial challenge.
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Autorzy:
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Shang-Guan XY; College of Animal Science and Technology, Northwest A&F University, Yangling, Shan'xi, 712100, China.
Cai YJ; College of Animal Science and Technology, Northwest A&F University, Yangling, Shan'xi, 712100, China.
Xu HZ; College of Animal Science and Technology, Northwest A&F University, Yangling, Shan'xi, 712100, China.
Cheng X; College of Animal Science and Technology, Northwest A&F University, Yangling, Shan'xi, 712100, China.
Zhang RF; College of Animal Science and Technology, Northwest A&F University, Yangling, Shan'xi, 712100, China.
Liu HX; College of Animal Science and Technology, Northwest A&F University, Yangling, Shan'xi, 712100, China. Electronic address: .
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Źródło:
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Fish & shellfish immunology [Fish Shellfish Immunol] 2021 Aug; Vol. 115, pp. 160-170. Date of Electronic Publication: 2021 Jun 17.
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Typ publikacji:
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Journal Article
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Język:
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English
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Imprint Name(s):
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Original Publication: London ; New York : Academic Press, c1991-
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MeSH Terms:
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Cyprinidae/*genetics
Cyprinidae/*immunology
Fish Diseases/*immunology
Gene Expression Regulation/*immunology
Immunity, Innate/*genetics
Lectins, C-Type/*genetics
Lectins, C-Type/*immunology
Aeromonas hydrophila/physiology ; Amino Acid Sequence ; Animals ; Base Sequence ; Fish Proteins/chemistry ; Fish Proteins/genetics ; Fish Proteins/immunology ; Gene Expression Profiling/veterinary ; Gram-Negative Bacterial Infections/immunology ; Gram-Negative Bacterial Infections/veterinary ; Lectins, C-Type/chemistry ; Phylogeny ; Sequence Alignment/veterinary
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Contributed Indexing:
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Keywords: Agglutinating activity; C-type lectin; Innate immunity; Onychostoma macrolepis; Sugar-binding ability
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Substance Nomenclature:
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0 (Fish Proteins)
0 (Lectins, C-Type)
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Entry Date(s):
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Date Created: 20210620 Date Completed: 20210723 Latest Revision: 20210723
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Update Code:
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20240104
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DOI:
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10.1016/j.fsi.2021.06.007
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PMID:
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34147614
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C-type lectins (CTL) are a large group of pattern-recognition proteins and to play important roles in glycoprotein metabolism, multicellular integration, and immunity. Based on their overall domain structure, they can be classified as different groups that possess different physiological functions. A typical C-type lectin (named as OmLec1) was identified from the fish, Onychostoma macrolepis, an important cultured fish in China. Open reading frame of OmLec1 contains a 570 bp, encoding a protein of 189 amino acids that includes a signal peptide and a single carbohydrate-recognition domain. The phylogenetic analysis showed that OmLec1 could be grouped with C-type lectin from other fish. OmLec1 was expressed in all the tissues in our study, and the expression level was highest in liver. And its relative expression levels were significantly upregulated following infection with Aeromonas hydrophila. The recombinant OmLec1 protein (rOmLec1) could agglutinate some Gram-negative bacteria and Gram-positive bacteria in vitro in the presence of Ca 2+ , showing a typical Ca 2+ -dependent carbohydrate-binding protein. Furthermore, rOmLec1 purified from E. coli BL21 (DE3), strongly bound to LPS and PGN, as well as all tested bacteria in a Ca 2+ -dependent manner. These results indicate that OmLec1 plays a central role in the innate immune response and as a pattern recognition receptor that recognizes diverse pathogens among O. macrolepis.
(Copyright © 2021 Elsevier Ltd. All rights reserved.)
