The molecular characterization, expression analysis and antimicrobial activity of theromacin from Asian polychaeta (Perinereis linea)

Antimicrobial peptides (AMPs) are molecular factors in innate immunity and are believed to play a key role in invertebrate host defence. We identified theromacin (TM) from an Asian polychaeta, Perinereis linea, using de novo RNA-seq analysis. TM, a typical AMP of invertebrates, is a cysteine-rich AMP with five disulfide bonds consisting of ten cysteine residues. In gene expression analysis, TM genes were constantly upregulated after lipopolysaccharide (LPS) stimulation. In contrast, after peptidoglycan (PGN) stimulation, it was upregulated initially and downregulated after 12 h. We synthesized a peptide based on the macin AMP in the TM amino acid sequence. The synthetic peptide showed antibacterial activity against some Gram-positive and Gram-negative bacteria. Therefore, the AMPs of P. linea might have broad roles in host defence and exhibit different degrees of activity.

Abstract sourced from PubMed (NCBI) for the cited record. See the original publication for the authoritative version.

Theromacin, a cysteine-rich antimicrobial peptide with five disulfide bonds, was identified by RNA-seq in the polychaete Perinereis linea; a synthetic macin-based peptide inhibited some Gram-positive and Gram-negative bacteria, and TM expression rose after LPS stimulation.

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