Facilitative production of an antimicrobial peptide royalisin and its antibody via an artificial oil‐body system

Tseng, Jun-Ming; Huang, Jun-Ru; Huang, Hsiou-Chen; Tzen, Jason T.C.; Chou, Wing‐Ming; Peng, Ching‐I

doi:10.1002/btpr.528

Cited by 41 publications

(38 citation statements)

References 37 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The antibacterial defensins were also produced in E. coli using a divergent method. The royalisin defensin from the royal jelly of Apis mellifera has an important estimated production potential (0.192 mg/L of cell culture) when produced in an artificial oil-body system (AOB) over-expressed in E. coli [98]. Oil bodies are plant seed organelles for intracellular lipid storage, composed of a triacylglycerol (TGA) matrix surrounded by a phospholipid (PL) monolayer and specific proteins, such as the structural oleosin [99].…”

Section: Discussionmentioning

confidence: 99%

Cysteine-stabilized αβ defensins: From a common fold to antibacterial activity

Dias

Franco

2015

Peptides

View full text Add to dashboard Cite

Antimicrobial peptides (AMPs) seem to be promising alternatives to common antibiotics, which are facing increasing bacterial resistance. Among them are the cysteine-stabilized αβ defensins. These peptides are small, with a length ranging from 34 to 54 amino acid residues, cysteine-rich and extremely stable, normally composed of an α-helix and three β-strands stabilized by three or four disulfide bonds and commonly found in several organisms. Moreover, animal and plant CSαβ defensins present different specificities, the first being mainly active against bacteria and the second against fungi. The role of the CSαβ-motif remains unknown, but a common antibacterial mechanism of action, based on the inhibition of the cell-wall formation, has already been observed in some fungal and invertebrate defensins. In this context, the present work aims to group the data about CSαβ defensins, highlighting their evolution, conservation, structural characteristics, antibacterial activity and biotechnological perspectives.

show abstract

Section: Discussionmentioning

confidence: 99%

Cysteine-stabilized αβ defensins: From a common fold to antibacterial activity

Dias

Franco

2015

Peptides

View full text Add to dashboard Cite

show abstract

“…Def-1 has been shown to be effective against Gram-positive bacteria (Fujiwara et al, 1990;Bachanová et al, 2002;Shen et al, 2012); however, some studies using recombinant Def-1 have also reported its activity against Gram-negative bacteria including Pseudomonas aeruginosa and Salmonella enterica (Tseng et al, 2011;Bílikova et al, 2015). In accordance with these previous studies, Pseudomonas aeruginosa seemed to be resistant to Def-1.…”

Section: Discussionmentioning

confidence: 99%

Antibiofilm efficacy of honey and bee-derived defensin-1 on multispecies wound biofilm

Sojka

Valachová

Bucekova

et al. 2016

Journal of Medical Microbiology

View full text Add to dashboard Cite

Many clinically relevant biofilms are polymicrobial. Examining the effect of antimicrobials in a multispecies biofilm consortium is of great clinical importance. The goal of this study was to investigate the effect of different honey types against bacterial wound pathogens grown in multispecies biofilm and to test the antibiofilm activity of honey defensin-1 (Def-1) in its recombinant form. A modified Lubbock chronic wound biofilm formed by four bacterial species (Staphylococcus aureus, Streptococcus agalactiae, Pseudomonas aeruginosa and Enterococcus faecalis) was used for evaluation of honey and recombinant bee-derived Def-1 antibiofilm efficacy. Recombinant Def-1 was prepared by heterologous expression in Escherichia coli. We showed that different types of honey (manuka and honeydew) were able to significantly reduce the cell viability of wound pathogens (Staphylococcus aureus, Streptococcus agalactiae and Pseudomonas aeruginosa) in mature polymicrobial biofilm. None of the tested honeys showed the ability to eradicate Enterococcus faecalis in biofilm. In addition, recombinant Def-1 successfully reduced the viability of Staphylococcus aureus and Pseudomonas aeruginosa cells within established polymicrobial biofilm after 24 and 48 h of treatment. Interestingly, recombinant Def-1 did not affect the viability of Streptococcus agalactiae cells within the biofilm, whereas both natural honeys significantly reduced the viable bacteria. Although Enterococcus faecalis was highly resistant to Def-1, Def-1 significantly affected the biofilm formation of Enterococcus faecalis and Streptococcus agalactiae after 24 h of treatment, most likely by inhibiting its extracellular polymeric substances production. In conclusion, our study revealed that honey and Def-1 are effective against established multispecies biofilm; however, Enterococcus faecalis grown in multispecies biofilm was resistant to both antimicrobials.

show abstract

“…A bacterial expression/purification system to produce recombinant proteins was developed by using artificial oil bodies [141,[164][165][166][167][168][169]. In this system, a target protein was first overexpressed as an insoluble oleosin-fused polypeptide, collected from the pellet of cell lysate simply by centrifugation, assembled into artificial oil bodies, separated from oleosin, and then harvested by concentrating the ultimate supernatant.…”

Section: Protein Expression/purificationmentioning

confidence: 99%

Integral Proteins in Plant Oil Bodies

Tzen

2012

ISRN Botany

Self Cite

View full text Add to dashboard Cite

Hydrophobic storage neutral lipids are stably preserved in specialized organelles termed oil bodies in the aqueous cytosolic compartment of plant cells via encapsulation with surfactant molecules including phospholipids and integral proteins. To date, three classes of integral proteins, termed oleosin, caleosin, and steroleosin, have been identified in oil bodies of angiosperm seeds. Proposed structures, targeting traffic routes, and biological functions of these three integral oil-body proteins were summarized and discussed. In the viewpoint of evolution, isoforms of oleosin and caleosin are found in oil bodies of pollens as well as those of more primitive species; moreover, caleosin-and steroleosin-like proteins are also present in other subcellular locations besides oil bodies. Technically, artificial oil bodies of structural stability similar to native ones were successfully constituted and seemed to serve as a useful tool for both basic research studies and biotechnological applications.

show abstract

Facilitative production of an antimicrobial peptide royalisin and its antibody via an artificial oil‐body system

Cited by 41 publications

References 37 publications

Cysteine-stabilized αβ defensins: From a common fold to antibacterial activity

Cysteine-stabilized αβ defensins: From a common fold to antibacterial activity

Antibiofilm efficacy of honey and bee-derived defensin-1 on multispecies wound biofilm

Integral Proteins in Plant Oil Bodies

Contact Info

Product

Resources

About