Identification and characteristics of a novel cecropin from the armyworm, Mythimna separata.

ABSTRACT:

Background

The recent emergence of antibiotic-resistant strains of bacteria has increased the need to develop effective alternatives to antibiotics. Antimicrobial peptides have been considered as a promising product with several advantages.

Results

In this present study, we identified a novel cecropin from the armyworm, Mythimna separata (armyworm cecropin 1, AC-1) by transcriptome sequencing and multi-sequence alignment analysis. The AC-1 precursor comprised 63 amino acid residues, containing a conserved cleavage site of the signal peptide, Ala₂₃-Pro₂₄, while the mature AC-1 included 39 amino acid residues. Chemically synthesized AC-1 exhibited low hemolytic activity against chicken red blood cells, low cytotoxicity against swine testis cells, and effe

SUBMITTER: Lian K 

PROVIDER: S-EPMC7395354 | biostudies-literature | 2020 Aug

REPOSITORIES: biostudies-literature