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Characterization and functional analysis of a novel goose-type lysozyme from teleost Sebastes schlegelii with implications for antibacterial defense and immune cell modulation.

Authors :
Jing H
Yan X
Wang Y
Yang K
Chen ZY
Wang GH
Zhang M
Source :
Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology [Comp Biochem Physiol B Biochem Mol Biol] 2025 Feb-Mar; Vol. 276, pp. 111060. Date of Electronic Publication: 2024 Dec 16.
Publication Year :
2025

Abstract

Lysozymes are crucial enzymes involved in the innate immune response against bacterial pathogens. In this study, we identified and characterized a goose-type lysozyme gene (SsLyG) from the black rockfish Sebastes schlegelii, an economically important aquaculture species. The deduced amino acid sequence of SsLyG contains 495 residues, which inculded a signal peptide, an immunoglobulin domain, and a goose egg-white lysozyme (GEWL) domain. Tissue expression analysis revealed the highest SsLyG levels in blood, and its transcription was significantly upregulated in the spleen and kidney upon bacterial and polyI:C challenges. Recombinant SsLyGE (rSsLyGE) exhibited lytic activity against Micrococcus lysodeikticus and concentration-dependent binding ability to Staphylococcus aureus and Micrococcus luteus. Furthermore, rSsLyGE promoted peripheral blood lymphocyte proliferation, enhanced macrophage respiratory burst activity, and increased reactive oxygen species production. RNA interference-mediated knockdown of SsLyG resulted in higher bacterial loads in the liver and spleen after Listonella anguillarum challenge, suggesting its role in early antibacterial defense. Collectively, these findings provide insights into the immune function of SsLyG and its potential application in developing antimicrobial strategies for aquaculture.<br />Competing Interests: Declaration of competing interest The authors declare that they have no competing interest.<br /> (Copyright © 2024 Elsevier Inc. All rights reserved.)

Details

Language :
English
ISSN :
1879-1107
Volume :
276
Database :
MEDLINE
Journal :
Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology
Publication Type :
Academic Journal
Accession number :
39694086
Full Text :
https://doi.org/10.1016/j.cbpb.2024.111060