Expression and purification of an active cecropin-like recombinant protein against multidrug resistance Escherichia coli

Téllez, Germán Alberto; Castaño-Osorio, Jhon Carlos

doi:10.1016/j.pep.2014.05.004

Cited by 15 publications

(17 citation statements)

References 16 publications

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“…Although the yield is quite high, the long cultivation time and complicated purification process still hinder its application. With the use of E. coli as the host, the highest production is reported by Téllez and Castaño‐Osorio . They claimed to produce 100 mg/L cecropin‐like peptide under 12 H cultivation.…”

Section: Discussionmentioning

confidence: 99%

“…suggested that cecropin XJ, originally isolated from the larvae of Bombyx mori , could be produced via its genetic expression in the Saccharomyces cerevisia e INVSc1 strain . Téllez and Castaño‐Osorio reported that the expression of a cecropin‐like peptide with a cysteine protease domain tag may help the purification process . From the aforementioned reports, it appears the most commonly used approach is to construct a cecropin fusion protein and to express it using E. coli or yeast as the host.…”

Section: Introductionmentioning

confidence: 99%

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Enhanced cecropin B2 production via chitin‐binding domain and intein self‐cleavage system

Fang

Lai

Liu

et al. 2018

Biotech and App Biochem

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In this study, various constructs and hosts were used to produce high levels of cecropin B2 (cecB2). To mitigate cecB2's toxic inhibition of host cells, various cecB2 constructs were built. Results showed that the combination of a chitin-binding domain and an intein self-cleavage motif in front of cecropin B2, without a His-tag, was best for cecB2 expression. E. coli ER2566 was the best host, and 2YT was the best medium for cultivation. Under these conditions, a cecB2 yield of 98.2 mg/L could be obtained after purification. The purified cecB2 expressed a wide antimicrobial effect on most Gram-negative strains, including multidrug-resistant Acinetobactor baumannii and Staphylococcus aureus. This study provides a systematic approach to the efficient production of the antimicrobial peptide (AMP) cecB2 via the recombinant E. coli process, which is expected to be an efficient way for the production of other AMPs.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Enhanced cecropin B2 production via chitin‐binding domain and intein self‐cleavage system

Fang

Lai

Liu

et al. 2018

Biotech and App Biochem

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“…In this context, a 3·5 kDa cecropin‐like AMP, lucilin, consisting of 36 amino acid residues, was discovered in L. sericata through a genetic sequence in mRNA . However, the antimicrobial activity and toxicity of lucilin alone are unknown as the authors reported the expression of lucilin in the form of its active recombinant fusion protein with a cysteine protease domain.…”

Section: Introductionmentioning

confidence: 99%

TIME management by medicinal larvae

Pritchard

Čeřovský

Nigam

et al. 2015

International Wound Journal

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Wound bed preparation (WBP) is an integral part of the care programme for chronic wounds. The acronym TIME is used in the context of WBP and describes four barriers to healing in chronic wounds; namely, dead Tissue, Infection and inflammation, Moisture imbalance and a non-migrating Edge. Larval debridement therapy (LDT) stems from observations that larvae of the blowfly Lucilia sericata clean wounds of debris. Subsequent clinical studies have proven debriding efficacy, which is likely to occur as a result of enzymatically active alimentary products released by the insect. The antimicrobial, anti-inflammatory and wound healing activities of LDT have also been investigated, predominantly in a pre-clinical context. This review summarises the findings of investigations into the molecular mechanisms of LDT and places these in context with the clinical concept of WBP and TIME. It is clear from these findings that biotherapy with L. sericata conforms with TIME, through the enzymatic removal of dead tissue and its associated biofilm, coupled with the secretion of defined antimicrobial peptides. This biotherapeutic impact on the wound serves to reduce inflammation, with an associated capacity for an indirect effect on moisture imbalance. Furthermore, larval serine proteinases have the capacity to alter fibroblast behaviour in a manner conducive to the formation of granulation tissue.

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“…As far back as the Napoleonic wars, field hospitals began reporting soldiers with noninfected, maggot‐infested battle wounds showing accelerated healing and no signs of infection . While there is still much debate as to the precise mechanisms involved in wound healing, the antibacterial properties for L. sericata have been thoroughly investigated and many antibacterial factors described …”

mentioning

confidence: 99%

“…7 While there is still much debate as to the precise mechanisms involved in wound healing, the antibacterial properties for L. sericata have been thoroughly investigated and many antibacterial factors described. [8][9][10][11][12][13] It had been suggested that some antimicrobial activity may be attributed to the process of debridement, during which ingested bacteria are eradicated as they pass through the alimentary tract of the maggot. 14 More recent investigations into this activity have focused on discerning the identities of the antibacterial components present in the excretions/secretions (ES) of L. sericata.…”

mentioning

confidence: 99%

Detection and partial characterization of antifungal bioactivity from the secretions of the medicinal maggot, Lucilia sericata

Evans

Dudley

Nigam

2015

Wound Repair Regeneration

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The antibacterial properties of the excretions/secretions (ES) of the medicinal maggot, Lucilia sericata have long been known and the effectiveness of maggot debridement therapy in relation to the clearance of bacteria from the surface of wounds has been the source of much research over recent years. Less well known, however, are the antifungal properties of L. sericata ES. Here, we show by means of the colony forming unit assay and optical density assays, that L. sericata native ES possess significant antifungal properties and appears to possess a highly heat stable, freeze/thaw, and lyophilization resistant antifungal component. We also show that the antifungal activity present in the native ES consists of a number of antifungal components present in three fraction masses consisting of >10, 10-0.5, and <0.5 kDa, with the greatest level of activity being seen in the <0.5 kDa fraction.

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Expression and purification of an active cecropin-like recombinant protein against multidrug resistance Escherichia coli

Cited by 15 publications

References 16 publications

Enhanced cecropin B2 production via chitin‐binding domain and intein self‐cleavage system

Enhanced cecropin B2 production via chitin‐binding domain and intein self‐cleavage system

TIME management by medicinal larvae

Detection and partial characterization of antifungal bioactivity from the secretions of the medicinal maggot, Lucilia sericata

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