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Characterization and functional study of a Cecropin‐like peptide from the Chinese oak silkworm, Antheraea pernyi
Author(s) -
Fang ShaoLiang,
Wang Lei,
Fang Qi,
Chen Chen,
Zhao XiaoSan,
Qian Cen,
Wei GuoQing,
Zhu BaoJian,
Liu ChaoLiang
Publication year - 2017
Publication title -
archives of insect biochemistry and physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.576
H-Index - 66
eISSN - 1520-6327
pISSN - 0739-4462
DOI - 10.1002/arch.21368
Subject(s) - antheraea pernyi , peptide , cecropin , escherichia coli , biochemistry , amino acid , signal peptide , circular dichroism , antibacterial activity , biology , peptide sequence , complementary dna , bacteria , microbiology and biotechnology , antimicrobial peptides , gene , genetics
In present study, a Cecropin‐like peptide from Antheraea pernyi ( Ap Cec) was cloned and characterized. The full‐length Ap Cec cDNA encoded a protein with 64 amino acids including a putative 22‐amino‐acid signal peptide, a 4‐amino‐acid propeptide, and a 38‐amino‐acid mature peptide. Ap Cec gene was highly expressed in Malpighian tubules of A. pernyi after induction for 24 h by Escherichia coli in PBS. Pro‐ Ap Cec (including propeptide and mature peptide) and M‐ Ap Cec (just mature peptide) were synthesized chemically and analyzed by HPLC and mass spectroscopy. The antibacterial activity of M‐ Ap Cec is more potent than pro‐ Ap Cec against E. coli K12 or B. subtilus in both minimum inhibitory concentration and inhibition zone assays. Hemolytic assay results showed M‐ Ap Cec possessed a low cytotoxicity to mammalian cells. The secondary structure of M‐ Ap Cec forms α‐helical structure, shown by circular dichroism spectroscopy. Transmission electron microscopy analysis suggested that M‐ Ap Cec killed bacteria by disrupting bacterial cell membrane integrity. Our results indicate Ap Cec may play an important role in defending from pathogenic bacteria in A. pernyi , and it may be as a potential candidate for applications in antibacterial drug development and agriculture.