biostudies-literatureGong RNational Natural Science Foundation of Fujian Province, ChinaMarine Biotechnology Economic Integration Service Platform from Fujian Association for Science and Technologythe Xiamen Science and Technology Planning ProjectXiamen Science and Technology Planning Projectthe National Natural Science Foundation of Fujian Province, China651https://www.ebi.ac.uk/biostudies/studies/S-EPMC9605627biostudies-literatureUnknown20(10)Hepcidin is widely present in many kinds of fish and is an important innate immune factor. A variety of HAMP2-type hepcidins have strong antimicrobial activity and immunomodulatory functions and are expected to be developed as substitutes for antibiotics. In this study, the antimicrobial activity of Hepc2 from Japanese seabass (<i>Lateolabrax japonicus</i>) (designated as LJ-hep2) was investigated using its recombinant precursor protein (rLJ-hep2) expressed in <i>Pichia pastoris</i> and a chemically synthesized mature peptide (LJ-hep2_(66-86)). The results showed that both rLJ-hep2 and synthetic LJ-hep2_(66-86) displayed broad antimicrobial spectrum with potent activity against gram-negative and gram-positive bacteria, and fungi. Especially, LJ-hep2_(66-86) haMarine drugsThe Antimicrobial Peptide LJ-hep2 from <i>Lateolabrax japonicus</i> Exerting Activities against Multiple Pathogenic Bacteria and Immune Protection In Vivo.PMC9605627# 3502Z20203012#2021J050082021J050083502Z20203012Zhang WGong RAn ZChen FWang KJfalseThe Antimicrobial Peptide LJ-hep2 from <i>Lateolabrax japonicus</i> Exerting Activities against Multiple Pathogenic Bacteria and Immune Protection In Vivo.Hepcidin is widely present in many kinds of fish and is an important innate immune factor. A variety of HAMP2-type hepcidins have strong antimicrobial activity and immunomodulatory functions and are expected to be developed as substitutes for antibiotics. In this study, the antimicrobial activity of Hepc2 from Japanese seabass (<i>Lateolabrax japonicus</i>) (designated as LJ-hep2) was investigated using its recombinant precursor protein (rLJ-hep2) expressed in <i>Pichia pastoris</i> and a chemically synthesized mature peptide (LJ-hep2_(66-86)). The results showed that both rLJ-hep2 and synthetic LJ-hep2_(66-86) displayed broad antimicrobial spectrum with potent activity against gram-negative and gram-positive bacteria, and fungi. Especially, LJ-hep2_(66-86) ha2022-01-01T00:00:00Z2022 Oct2026-04-08T11:50:08.655Z2024-11-13T23:29:31.849ZS-EPMC96056273628647410.3390/md20100651