Recombinant expression and biological characterization of the antimicrobial peptide fowlicidin-2 in Pichia pastoris

Xing, Liwei; Tian, Shi‐Xun; Yang, Na; Qu, Pei; Liu, Di; Jiao, Jian; Wang, Jue; Feng, Xingjun

doi:10.3892/etm.2016.3578

Cited by 17 publications

(8 citation statements)

References 34 publications

(35 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Given their antimicrobial potential, recombinant expression in bacterial species is a challenge. Some methods like bacterial production of fusion proteins or inteins do exist, for example in E. coli [ 140 ], Bacillus subtilis [ 141 ], or the yeast Pichia pastoris [ 142 ]. The purified peptides often retain their antibiotic activity but are (in these examples) not tested for endotoxins or immunomodulatory activity.…”

Section: Discussionmentioning

confidence: 99%

Cathelicidins: Immunomodulatory Antimicrobials

et al. 2018

View full text Add to dashboard Cite

Cathelicidins are host defense peptides with antimicrobial and immunomodulatory functions. These effector molecules of the innate immune system of many vertebrates are diverse in their amino acid sequence but share physicochemical characteristics like positive charge and amphipathicity. Besides being antimicrobial, cathelicidins have a wide variety in immunomodulatory functions, both boosting and inhibiting inflammation, directing chemotaxis, and effecting cell differentiation, primarily towards type 1 immune responses. In this review, we will examine the biology and various functions of cathelicidins, focusing on putting in vitro results in the context of in vivo situations. The pro-inflammatory and anti-inflammatory functions are highlighted, as well both direct and indirect effects on chemotaxis and cell differentiation. Additionally, we will discuss the potential and limitations of using cathelicidins as immunomodulatory or antimicrobial drugs.

show abstract

Section: Discussionmentioning

confidence: 99%

Cathelicidins: Immunomodulatory Antimicrobials

et al. 2018

View full text Add to dashboard Cite

show abstract

“…There are 3 pathways for AMP production: extraction from natural resources, chemical synthesis, and recombinant expression. 26 Considering the low yield of AMPs obtained from natural producers and the high cost of chemical peptide synthesis, 27,28 the biological production of AMPs by heterologous microbial hosts may provide an opportunity for their production in large amounts. 29 Due to its ability to grow rapidly to high cell densities in inexpensive medium, the methylotrophic yeast P. pastoris has become widely used as a heterologous gene expression system for AMPs.…”

Section: Confocal Laser Scanning Microscopymentioning

confidence: 99%

Design, expression, and characterization of the hybrid antimicrobial peptide T‐catesbeianin‐1 based on FyuA

Tie

Zhang

et al. 2018

Journal of Peptide Science

View full text Add to dashboard Cite

The overuse of antibiotics has resulted in the emergence of antibiotic-resistant bacteria, which presents an urgent need for new antimicrobial agents. At present, antimicrobial peptides have attracted a great deal of attention from researchers. However, antimicrobial peptides often affect a broad range of microorganisms, including the normal flora in a host organism. In the present study, we designed a novel hybrid antimicrobial peptide, expressed the hybrid peptide, and studied its specific target. The hybrid peptide, named T-catesbeianin-1, which includes the FyuA-binding domain of pesticin and the peptide catesbeianin-1, was designed and expressed in Pichia pastoris X-33. Then, we determined the antimicrobial activity, cytotoxicity, and specific target of the peptide. T-catesbeianin-1 has strong antimicrobial activity and binds to FyuA to inhibit or kill Escherichia coli present in clinical specimens and mixed-species culture. In summary, these findings suggested that T-catesbeianin-1 might be promising and specific antibiotic agent for therapeutic application against fyuA + E. coli.

show abstract

“…Li et al expressed the peptide CGA-N46 in Bacillus subtilis DB1342 [17]. Luiz et al produced the abaecin peptide [18] and Li et al expressed the antimicrobial peptide fowlicidin-2, both in Pichia pastoris [19]. In the current study, we expressed recombinant AC-1 using an E. coli prokaryotic expression system, and the AC-1 obtained by enterokinase digestion exhibited similar antimicrobial activity to chemically synthesized AC-1.…”

Section: Discussionmentioning

confidence: 67%

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

et al. 2020

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, 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.

show abstract

Recombinant expression and biological characterization of the antimicrobial peptide fowlicidin-2 in Pichia pastoris

Cited by 17 publications

References 34 publications

Cathelicidins: Immunomodulatory Antimicrobials

Cathelicidins: Immunomodulatory Antimicrobials

Design, expression, and characterization of the hybrid antimicrobial peptide T‐catesbeianin‐1 based on FyuA

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

Contact Info

Product

Resources

About