Pecbloodin 18-37 : a promising antimicrobial peptide from Boleophthalmus pectinirostris with therapeutic potential against Edwardsiella tarda infection

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Authors: Yuqi Bai, Wenbin Zheng, Weibin Zhang, Jingyuan Zhan, Fangyi Chen, Ke-Jian Wang
Cited by: 1
References: 50

Abstract

ABSTRACT Edwardsiella tarda is a significant pathogen in aquaculture, causing severe systemic infections and considerable economic losses worldwide. The limited efficacy of current treatments and the emergence of multidrug-resistant strains underscore the urgent need for novel antimicrobial strategies. Antimicrobial peptides have garnered increasing interest due to their broad-spectrum activity and low risk of resistance development. In this study, we identified a novel immune-related gene from the mudskipper Boleophthalmus pectinirostris , named Pecbloodin , which encodes a mature peptide of 67 amino acids. A truncated peptide derived from this sequence, Pecbloodin 18-37 , exhibited broad-spectrum antibacterial activity, high thermal stability, and tolerance to sodium ions. Functional assays demonstrated that Pecbloodin 18-37 exerts rapid bactericidal effects by compromising bacterial membrane integrity, inducing cellular content leakage, and triggering endogenous reactive oxygen species accumulation. Furthermore, it effectively inhibited bacterial biofilm formation and did not promote resistance under prolonged exposure. Importantly, in vivo experiments using an E. tarda -infected mudskipper model revealed that Pecbloodin 18-37 significantly improved host survival and modulated the immune response. Overall, Pecbloodin 18-37 shows great potential as a promising alternative to conventional antibiotics for the control of E. tarda infections in aquaculture, addressing the pressing issue of antibiotic resistance. IMPORTANCE Edwardsiella tarda is an urgent threat to global aquaculture. We mined the mudskipper Boleophthalmus pectinirostris genome for antimicrobial peptide and identified Pecbloodin 18-37 , a 20-aa thermostable peptide that rapidly permeabilizes bacterial membranes, elicits intracellular reactive oxygen species, blocks biofilm formation, and does not select for resistance. In E. tarda -challenged fish, a single dose reduced mortality by 25% and restored immune homeostasis. The peptide is readily synthesized and feed-compatible, providing an immediate, resistance-proof substitute for conventional antibiotics in fish farming.

Fields of Study & Subjects

Antimicrobial Peptides and Activities Invertebrate Immune Response Mechanisms Aquaculture disease management and microbiota

Publication details

Journal / source
Applied and Environmental Microbiology
Publisher
American Society for Microbiology
Volume
92
Issue
3
Pages
e0204325–e0204325
Publication date
23 February 2026
Language
EN