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Molecular characterization, microbial recognition and immunomodulatory functions of a novel ladderlectin-like lectin (HoLL-like) from Hexagrammos otakii.

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Τίτλος: Molecular characterization, microbial recognition and immunomodulatory functions of a novel ladderlectin-like lectin (HoLL-like) from Hexagrammos otakii.
Συγγραφείς: Wen Y; College of Fisheries and Life Science, Dalian Ocean University, Dalian, 116023, China., Wei X; Key Laboratory of Applied Biology and Aquaculture of Northern Fishes in Liaoning Province, Dalian Ocean University, Dalian, 116023, China; College of Fisheries and Life Science, Dalian Ocean University, Dalian, 116023, China., He T; Key Laboratory of Applied Biology and Aquaculture of Northern Fishes in Liaoning Province, Dalian Ocean University, Dalian, 116023, China; College of Fisheries and Life Science, Dalian Ocean University, Dalian, 116023, China., Wang S; Key Laboratory of Applied Biology and Aquaculture of Northern Fishes in Liaoning Province, Dalian Ocean University, Dalian, 116023, China; College of Fisheries and Life Science, Dalian Ocean University, Dalian, 116023, China., Zhang Y; Key Laboratory of Applied Biology and Aquaculture of Northern Fishes in Liaoning Province, Dalian Ocean University, Dalian, 116023, China; College of Fisheries and Life Science, Dalian Ocean University, Dalian, 116023, China., Zhang Z; College of Environmental Sciences and Engineering, Dalian Maritime University, Dalian, 116026, China., Li J; Key Laboratory of Applied Biology and Aquaculture of Northern Fishes in Liaoning Province, Dalian Ocean University, Dalian, 116023, China; College of Fisheries and Life Science, Dalian Ocean University, Dalian, 116023, China., Wang X; Key Laboratory of Applied Biology and Aquaculture of Northern Fishes in Liaoning Province, Dalian Ocean University, Dalian, 116023, China; College of Fisheries and Life Science, Dalian Ocean University, Dalian, 116023, China., Wang W; Key Laboratory of Applied Biology and Aquaculture of Northern Fishes in Liaoning Province, Dalian Ocean University, Dalian, 116023, China; College of Fisheries and Life Science, Dalian Ocean University, Dalian, 116023, China. Electronic address: wangwei@dlou.edu.cn., Li X; Key Laboratory of Applied Biology and Aquaculture of Northern Fishes in Liaoning Province, Dalian Ocean University, Dalian, 116023, China; College of Fisheries and Life Science, Dalian Ocean University, Dalian, 116023, China; Dalian Xinghai Bay Laboratory, Dalian, 116034, China. Electronic address: lixuejie@dlou.edu.cn.
Πηγή: Fish & shellfish immunology [Fish Shellfish Immunol] 2026 Oct; Vol. 177, pp. 111603. Date of Electronic Publication: 2026 Jul 22.
Τύπος έκδοσης: Journal Article
Γλώσσα: English
Στοιχεία περιοδικού: Publisher: Academic Press Country of Publication: England NLM ID: 9505220 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1095-9947 (Electronic) Linking ISSN: 10504648 NLM ISO Abbreviation: Fish Shellfish Immunol Subsets: MEDLINE
Imprint Name(s): Original Publication: London ; New York : Academic Press, c1991-
Ιατρικοί όροι (MeSH): Immunity, Innate*/genetics , Fish Diseases*/immunology , Perciformes*/immunology , Perciformes*/genetics , Lectins, C-Type*/genetics , Lectins, C-Type*/immunology , Lectins, C-Type*/chemistry , Gene Expression Regulation*/immunology, Sequence Alignment/veterinary ; Fish Proteins/genetics ; Fish Proteins/chemistry ; Fish Proteins/immunology ; Vibrio/physiology ; Gene Expression Profiling/veterinary ; Vibrio Infections/immunology ; Vibrio Infections/veterinary ; Lectins/genetics ; Lectins/immunology ; Lectins/chemistry ; Animals ; Amino Acid Sequence ; Phylogeny ; Base Sequence ; Innate Immunity Recognition
Περίληψη: Ladderlectin, a member of the C-type lectin (CTL) family, has historically been identified only in fish and shrimp, where it is primarily involved in innate immune defense. In teleosts, ladderlectin plays a crucial dual role in both innate immunity against pathogens and reproductive regulation. However, the molecular characterization and immunomodulatory functions of ladderlectin homolog (ladderlectin-like) in Hexagrammos otakii remain poorly understood. In this study, a novel ladderlectin-like gene (HoLL-like) was identified and cloned from Hexagrammos otakii based on genomic data. Sequence analysis and domain prediction revealed that HoLL-like contains a 534-bp open reading frame encoding a 177-aa polypeptide, with an N-terminal signal peptide and a single C-type lectin-like domain (CTLD). The CTLD retains the WSD, WND, and WIGG motifs and is rich in cysteine residues. Phylogenetic analysis showed that HoLL-like forms a distinct, relatively independent clade within the teleost ladderlectin-like family. Quantitative RT-PCR analysis demonstrated that Holl-like is expressed in multiple tissues, with the highest transcript levels in the liver. Besides, it exhibited a time-dependent transcriptional response in the liver, spleen, skin, intestine, and kidney following Vibrio harveyi infection. After heterologous expression, purification, and refolding, the recombinant protein rHoLL-like displayed characteristic ladder-like oligomeric bands in immunoblotting. Functional assays revealed that rHoLL-like binds and agglutinates multiple Gram-positive and Gram-negative bacteria in a Ca2+-independent manner and binds pathogen-associated molecular patterns (PAMPs), including lipopolysaccharide (LPS), peptidoglycan (PGN), and poly(I:C) in a dose-dependent manner, showing higher affinity for LPS. Further analyses indicated that rHoLL-like did not directly agglutinate or lyse erythrocytes, but enhanced serum hemolytic and bactericidal activities under Ca2+-containing conditions. These effects were sensitive to EDTA and serum heat inactivation, suggesting that rHoLL-like may modulate heat-labile, Ca2+-dependent serum effector mechanisms, potentially associated with complement activity. Collectively, these findings suggest that HoLL-like plays a crucial role in the innate immune response of H. otakii against bacterial and other pathogen infections. This study expands our understanding of the functional repertoire of teleost ladderlectin-like proteins and provides new insights into the molecular strategies to prevent and control bacterial diseases in marine aquaculture, as well as for the development of immunoactive agents.
(Copyright © 2026 Elsevier Ltd. All rights reserved.)
Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.
Contributed Indexing: Keywords: Bacterial agglutination; C-type lectin; Hexagrammos otakii; Immunomodulation; Ladderlectin-like
Substance Nomenclature: 0 (Fish Proteins)
0 (Lectins, C-Type)
0 (Lectins)
Entry Date(s): Date Created: 20260722 Date Completed: 20260806 Latest Revision: 20260806
Update Code: 20260807
DOI: 10.1016/j.fsi.2026.111603
PMID: 42486209
Βάση Δεδομένων: MEDLINE
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  Data: Molecular characterization, microbial recognition and immunomodulatory functions of a novel ladderlectin-like lectin (HoLL-like) from Hexagrammos otakii.
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  Data: <searchLink fieldCode="MM" term="%22Immunity%2C+Innate%22">Immunity, Innate*</searchLink>/<searchLink fieldCode="MM" term="%22Immunity%2C+Innate+genetics%22">genetics</searchLink> <br /><searchLink fieldCode="MM" term="%22Fish+Diseases%22">Fish Diseases*</searchLink>/<searchLink fieldCode="MM" term="%22Fish+Diseases+immunology%22">immunology</searchLink> <br /><searchLink fieldCode="MM" term="%22Perciformes%22">Perciformes*</searchLink>/<searchLink fieldCode="MM" term="%22Perciformes+immunology%22">immunology</searchLink> <br /><searchLink fieldCode="MM" term="%22Perciformes%22">Perciformes*</searchLink>/<searchLink fieldCode="MM" term="%22Perciformes+genetics%22">genetics</searchLink> <br /><searchLink fieldCode="MM" term="%22Lectins%2C+C-Type%22">Lectins, C-Type*</searchLink>/<searchLink fieldCode="MM" term="%22Lectins%2C+C-Type+genetics%22">genetics</searchLink> <br /><searchLink fieldCode="MM" term="%22Lectins%2C+C-Type%22">Lectins, C-Type*</searchLink>/<searchLink fieldCode="MM" term="%22Lectins%2C+C-Type+immunology%22">immunology</searchLink> <br /><searchLink fieldCode="MM" term="%22Lectins%2C+C-Type%22">Lectins, C-Type*</searchLink>/<searchLink fieldCode="MM" term="%22Lectins%2C+C-Type+chemistry%22">chemistry</searchLink> <br /><searchLink fieldCode="MM" term="%22Gene+Expression+Regulation%22">Gene Expression Regulation*</searchLink>/<searchLink fieldCode="MM" term="%22Gene+Expression+Regulation+immunology%22">immunology</searchLink><br /><searchLink fieldCode="MH" term="%22Sequence+Alignment%22">Sequence Alignment</searchLink>/<searchLink fieldCode="MH" term="%22Sequence+Alignment+veterinary%22">veterinary</searchLink> ; <searchLink fieldCode="MH" term="%22Fish+Proteins%22">Fish Proteins</searchLink>/<searchLink fieldCode="MH" term="%22Fish+Proteins+genetics%22">genetics</searchLink> ; <searchLink fieldCode="MH" term="%22Fish+Proteins%22">Fish Proteins</searchLink>/<searchLink fieldCode="MH" term="%22Fish+Proteins+chemistry%22">chemistry</searchLink> ; <searchLink fieldCode="MH" term="%22Fish+Proteins%22">Fish Proteins</searchLink>/<searchLink fieldCode="MH" term="%22Fish+Proteins+immunology%22">immunology</searchLink> ; <searchLink fieldCode="MH" term="%22Vibrio%22">Vibrio</searchLink>/<searchLink fieldCode="MH" term="%22Vibrio+physiology%22">physiology</searchLink> ; <searchLink fieldCode="MH" term="%22Gene+Expression+Profiling%22">Gene Expression Profiling</searchLink>/<searchLink fieldCode="MH" term="%22Gene+Expression+Profiling+veterinary%22">veterinary</searchLink> ; <searchLink fieldCode="MH" term="%22Vibrio+Infections%22">Vibrio Infections</searchLink>/<searchLink fieldCode="MH" term="%22Vibrio+Infections+immunology%22">immunology</searchLink> ; <searchLink fieldCode="MH" term="%22Vibrio+Infections%22">Vibrio Infections</searchLink>/<searchLink fieldCode="MH" term="%22Vibrio+Infections+veterinary%22">veterinary</searchLink> ; <searchLink fieldCode="MH" term="%22Lectins%22">Lectins</searchLink>/<searchLink fieldCode="MH" term="%22Lectins+genetics%22">genetics</searchLink> ; <searchLink fieldCode="MH" term="%22Lectins%22">Lectins</searchLink>/<searchLink fieldCode="MH" term="%22Lectins+immunology%22">immunology</searchLink> ; <searchLink fieldCode="MH" term="%22Lectins%22">Lectins</searchLink>/<searchLink fieldCode="MH" term="%22Lectins+chemistry%22">chemistry</searchLink> ; <searchLink fieldCode="MH" term="%22Animals%22">Animals</searchLink> ; <searchLink fieldCode="MH" term="%22Amino+Acid+Sequence%22">Amino Acid Sequence</searchLink> ; <searchLink fieldCode="MH" term="%22Phylogeny%22">Phylogeny</searchLink> ; <searchLink fieldCode="MH" term="%22Base+Sequence%22">Base Sequence</searchLink> ; <searchLink fieldCode="MH" term="%22Innate+Immunity+Recognition%22">Innate Immunity Recognition</searchLink>
– Name: Abstract
  Label: Abstract
  Group: Ab
  Data: Ladderlectin, a member of the C-type lectin (CTL) family, has historically been identified only in fish and shrimp, where it is primarily involved in innate immune defense. In teleosts, ladderlectin plays a crucial dual role in both innate immunity against pathogens and reproductive regulation. However, the molecular characterization and immunomodulatory functions of ladderlectin homolog (ladderlectin-like) in Hexagrammos otakii remain poorly understood. In this study, a novel ladderlectin-like gene (HoLL-like) was identified and cloned from Hexagrammos otakii based on genomic data. Sequence analysis and domain prediction revealed that HoLL-like contains a 534-bp open reading frame encoding a 177-aa polypeptide, with an N-terminal signal peptide and a single C-type lectin-like domain (CTLD). The CTLD retains the WSD, WND, and WIGG motifs and is rich in cysteine residues. Phylogenetic analysis showed that HoLL-like forms a distinct, relatively independent clade within the teleost ladderlectin-like family. Quantitative RT-PCR analysis demonstrated that Holl-like is expressed in multiple tissues, with the highest transcript levels in the liver. Besides, it exhibited a time-dependent transcriptional response in the liver, spleen, skin, intestine, and kidney following Vibrio harveyi infection. After heterologous expression, purification, and refolding, the recombinant protein rHoLL-like displayed characteristic ladder-like oligomeric bands in immunoblotting. Functional assays revealed that rHoLL-like binds and agglutinates multiple Gram-positive and Gram-negative bacteria in a Ca<superscript>2+</superscript>-independent manner and binds pathogen-associated molecular patterns (PAMPs), including lipopolysaccharide (LPS), peptidoglycan (PGN), and poly(I:C) in a dose-dependent manner, showing higher affinity for LPS. Further analyses indicated that rHoLL-like did not directly agglutinate or lyse erythrocytes, but enhanced serum hemolytic and bactericidal activities under Ca<superscript>2+</superscript>-containing conditions. These effects were sensitive to EDTA and serum heat inactivation, suggesting that rHoLL-like may modulate heat-labile, Ca<superscript>2+</superscript>-dependent serum effector mechanisms, potentially associated with complement activity. Collectively, these findings suggest that HoLL-like plays a crucial role in the innate immune response of H. otakii against bacterial and other pathogen infections. This study expands our understanding of the functional repertoire of teleost ladderlectin-like proteins and provides new insights into the molecular strategies to prevent and control bacterial diseases in marine aquaculture, as well as for the development of immunoactive agents.<br /> (Copyright © 2026 Elsevier Ltd. All rights reserved.)
– Name: Abstract
  Label: Competing Interests
  Group: Ab
  Data: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.
– Name: SubjectMinor
  Label: Contributed Indexing
  Group:
  Data: <i>Keywords: </i>Bacterial agglutination; C-type lectin; Hexagrammos otakii; Immunomodulation; Ladderlectin-like
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        Text: English
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      – SubjectFull: Fish Proteins chemistry
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      – TitleFull: Molecular characterization, microbial recognition and immunomodulatory functions of a novel ladderlectin-like lectin (HoLL-like) from Hexagrammos otakii.
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