A novel antimicrobial peptide CpAMP identified from Chinese horseshoe crab, Tachypleus tridentatus

Weifeng Wang; Sisi Wei; Xiaoyong Xie; Baoying Guo; Hong Liu; Huanling Wang

doi:10.1016/j.fsi.2024.110026

A novel antimicrobial peptide CpAMP identified from Chinese horseshoe crab, Tachypleus tridentatus

Fish Shellfish Immunol. 2024 Nov 14:110026. doi: 10.1016/j.fsi.2024.110026. Online ahead of print.

Authors

Weifeng Wang¹, Sisi Wei², Xiaoyong Xie³, Baoying Guo², Hong Liu⁴, Huanling Wang⁵

Affiliations

¹ College of Marine Science and Technology, Zhejiang Ocean University, Zhoushan 316022, China; Key Lab of Freshwater Animal Breeding, Key Laboratory of Agricultural Animal Genetics, Breeding and Reproduction, Ministry of Education, College of Fisheries, Huazhong Agricultural University, Wuhan 430070, China.
² College of Marine Science and Technology, Zhejiang Ocean University, Zhoushan 316022, China.
³ Key Laboratory of South China Sea Fishery Resources Exploitation & Utilization, Ministry of Agriculture, South China Sea Fisheries Research Institute, Chinese Academy of Fishery Sciences, Guangzhou 510300, China.
⁴ Key Lab of Freshwater Animal Breeding, Key Laboratory of Agricultural Animal Genetics, Breeding and Reproduction, Ministry of Education, College of Fisheries, Huazhong Agricultural University, Wuhan 430070, China.
⁵ Key Lab of Freshwater Animal Breeding, Key Laboratory of Agricultural Animal Genetics, Breeding and Reproduction, Ministry of Education, College of Fisheries, Huazhong Agricultural University, Wuhan 430070, China. Electronic address: [email protected].

PMID: 39550017
DOI: 10.1016/j.fsi.2024.110026

Abstract

Antibacterial peptide (AMP) is a crucial component of the innate immune system in most organism, play an important role in host defense processes. Many of these peptides have broad antimicrobial activity against Gram-negative, -positive bacteria and fungi. In the present study, a novel AMP named CpAMP was identified using transcriptome analysis in Chinese horseshoe crab. The preprotein of CpAMP consists of a signal peptide (21 aa) and a mature peptide (47 aa) enriched by cysteine. And the putative mature peptide CpAMP was 4.95 kDa with a theoretical isoelectric point (pI) of 8.73. The mature CpAMP showed α-helix and irregularly curled structure in the cys-stabilized region. CpAMP exhibited a broad spectrum of antimicrobial activity against Gram-negative, -positive bacteria and antibiotic-resistant strains. In addition, CpAMP can significantly increase the survival rate of zebrafish infected with bacteria. Due to its broad-spectrum antibacterial activity and the sensitivity of drug-resistant strains, CpAMP could be used as a new type of drug for inhibition of pathogenic microorganisms or as an immune enhancer in animals.

Keywords: Antimicrobial peptides; Tachypleus tridentatus; broad-spectrum activity.