Identification of the first cathelicidin gene from skin of Chinese giant salamanders Andrias davidianus with its potent antimicrobial activity

Yang, Hui; Lu, Baoyue; Zhou, Dandan; Zhao, Lin; Song, Weijia; Wang, Lixin

doi:10.1016/j.dci.2017.08.002

Cited by 26 publications

(11 citation statements)

References 40 publications

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“…Zhou et al identified five novel AMPs from Hylarana guentheri by isolation and purification [11], and Ma et al identified 34 AMPs from Rana nigrovittata by peptidomics and genomics [12]. Yang et al also identified a novel cathelicidin from the Chinese giant salamander Andrias davidianus using transcriptome sequencing and PCR amplification [13]. In the current study, we identified a novel cecropin from the armyworm by transcriptome sequencing and sequence alignment analysis.…”

Section: Discussionmentioning

confidence: 64%

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

et al. 2020

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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, Ala 23-Pro 24 , 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 effective antimicrobial activity against Salmonella, Escherichia coli, Klebsiella pneumonia, and Pseudomonas aeruginosa. Its antimicrobial activity against Salmonella remained after incubation for 1 h at 100°C or in 250 mM NaCl, KCl, or MgCl 2 solution, implying good thermal-and salt-resistant stabilities. The bactericidal effect of AC-1 on E. coli gradually increased with increasing AC-1 concentration, resulting in deformation, severe edema, cytolysis, cell membrane damage, and reducing intracellular electron density. Additionally, recombinant AC-1 protein expressed in E. coli was digested by enterokinase protease to obtain AC-1, which showed similar antimicrobial activity against E. coli to chemically synthesized AC-1. Conclusions: This study identified a novel antimicrobial peptide that may represent a potential alternative to antibiotics.

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Section: Discussionmentioning

confidence: 64%

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

et al. 2020

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show abstract

“…Zhou et al identi ed ve novel AMPs from Hylarana guentheri by isolation and puri cation [11], and Ma et al identi ed 34 AMPs from Rana nigrovittataby peptidomics and genomics [12]. Yang et al also identi ed a novel cathelicidin from the Chinese giant salamander Andrias davidianus using transcriptome sequencing and PCR ampli cation [13]. In the current study, we identi ed a novel cecropin from the armyworm by transcriptome sequencing and sequence alignment analysis.…”

Section: Discussionmentioning

confidence: 65%

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

Lian¹,

Zhang

Liang

et al. 2020

Preprint

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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 effective antimicrobial activity against Salmonella, Escherichia coli, Klebsiella pneumonia, and Pseudomonas aeruginosa. Its antimicrobial activity against Salmonella remained after incubation for 1 h at 100 °C or in 250 mM NaCl, KCl, or MgCl2 solution, implying good thermal- and salt-resistant stabilities. The bactericidal effect of AC-1 on E. coli gradually increased with increasing AC-1 concentration, resulting in deformation, severe edema, cytolysis, cell membrane damage, and reducing intracellular electron density. Additionally, recombinant AC-1 protein expressed in E. coli was digested by enterokinase protease to obtain AC-1, which showed similar antimicrobial activity against E. coli to chemically synthesized AC-1.Conclusions: This study identified a novel antimicrobial peptide that may represent a potential alternative to antibiotics.

show abstract

“…Zhou et al identi ed ve novel AMPs from Hylarana guentheri by isolation and puri cation [11], and Ma et al identi ed 34 AMPs from Rana nigrovittataby peptidomics and genomics [12]. Yang et al also identi ed a novel cathelicidin from the Chinese giant salamander Andrias davidianus using transcriptome sequencing and PCR ampli cation [13]. In the current study, we identi ed a novel cecropin from the armyworm by the transcriptome sequencing and sequence alignment analysis.…”

Section: Discussionmentioning

confidence: 65%

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

Lian

Zhang

Liang

et al. 2020

Preprint

View full text Add to dashboard Cite

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, Ala 23 -Pro 24 , 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 effective antimicrobial activity against Salmonella , Escherichia coli ( E. c oli ), Klebsiella pneumonia ( K. pneumonia ), and Pseudomonas aeruginosa ( P . aeruginosa ). Its antimicrobial activity against Salmonella remained after incubation for 1 h at 100 °C or in 250 mM NaCl, KCl, and MgCl 2 solution, implying good thermal- and salt-resistant stabilities. The bactericidal effect of AC-1 on E. c oli gradually increased with the increase of AC-1 concentration, and AC-1 could cause significant deformation , severe edema, cytoplasmic lysis, cell membrane damage of E. c oli , and reduce intracellular electron density. Additionally, the fusion protein AC-1 expressed in E. coli was digested by enterokinase protease to obtain the AC-1, which showed similar antimicrobial activity against E. c oli with chemically-synthesized AC-1. Conclusions: This study identified a novel antimicrobial peptide that may represent a potential alternative to antibiotics.

show abstract

Identification of the first cathelicidin gene from skin of Chinese giant salamanders Andrias davidianus with its potent antimicrobial activity

Cited by 26 publications

References 40 publications

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

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

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

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

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