Heterologous Expression and Antimicrobial Mechanism of a Cysteine-Rich Peptide from Barnacle <i>Pollicipes pollicipes</i>.

ABSTRACT: The escalating crisis of antimicrobial resistance in aquaculture, driven by the indiscriminate use of antibiotics, underscores the urgent need to develop novel anti-infective agents. This study addresses this requirement by investigating cysteine-rich antimicrobial peptides (AMPs) in understudied crustacean species. A cysteine-rich AMP, designated PpRcys1, was identified and characterized from the genome of Pollicipes pollicipes. PpRcys1 comprises 104 amino acids, with 85 residues forming the mature peptide region, and exhibits random coils, a CSαβ-fold, and one β-sheet. Our findings demonstrated that recombinant PpRcys1 (rPpRcys1) possesses broad-spectrum antimicrobial activity against three Gram-positive bacteria (Staphylococcus aureus, Bacill

SUBMITTER: He Z 

PROVIDER: S-EPMC12195476 | biostudies-literature | 2025 Jun

REPOSITORIES: biostudies-literature