Jaburetox: update on a urease-derived peptide
Abstract Urease from Canavalia ensiformis seeds was the first enzyme ever to be crystallized, in 1926. These proteins, found in plants, bacteria and fungi, present different biological properties including catalytic hydrolysis of urea, and also enzyme-independent activities, such as induction of exo...
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ftdoajarticles:oai:doaj.org/article:0778924069264c6eb40742ef1b370402 2023-05-15T15:13:29+02:00 Jaburetox: update on a urease-derived peptide Arlete Beatriz Becker-Ritt Camila Saretta Portugal Célia Regina Carlini 2017-06-01T00:00:00Z https://doi.org/10.1186/s40409-017-0122-y https://doaj.org/article/0778924069264c6eb40742ef1b370402 EN eng SciELO http://link.springer.com/article/10.1186/s40409-017-0122-y https://doaj.org/toc/1678-9199 doi:10.1186/s40409-017-0122-y 1678-9199 https://doaj.org/article/0778924069264c6eb40742ef1b370402 Journal of Venomous Animals and Toxins including Tropical Diseases, Vol 23, Iss 1, Pp 1-8 (2017) Peptide Bacteria Membranes Nanoparticles Arctic medicine. Tropical medicine RC955-962 Toxicology. Poisons RA1190-1270 Zoology QL1-991 article 2017 ftdoajarticles https://doi.org/10.1186/s40409-017-0122-y 2022-12-31T04:12:06Z Abstract Urease from Canavalia ensiformis seeds was the first enzyme ever to be crystallized, in 1926. These proteins, found in plants, bacteria and fungi, present different biological properties including catalytic hydrolysis of urea, and also enzyme-independent activities, such as induction of exocytosis, pro-inflammatory effects, neurotoxicity, antifungal and insecticidal properties. Urease is toxic to insects and fungi per se but part of this toxicity relies on an internal peptide (~11 kDa), which is released upon digestion of the protein by insect enzymes. A recombinant form of this peptide, called jaburetox (JBTX), was constructed using jbureII gene as a template. The peptide exhibits liposome disruption properties, and insecticidal and fungicidal activities. Here we review the known biological properties activities of JBTX, and comment on new ones not yet fully characterized. JBTX was able to cause mortality of Aedes aegypti larvae in a feeding assay whereas in a dose as low as of 0.1 μg it provoked death of Triatoma infestans bugs. JBTX (10−5–10−6 M) inhibits the growth of E. coli, P. aeruginosa and B. cereus after 24 h incubation. Multilamellar liposomes interacting with JBTX undergo reorganization of the membrane’s lipids as detected by small angle X-ray scattering (SAXS) studies. Encapsulating JBTX into lipid nanoparticles led to an increase of the peptide’s antifungal activity. Transgenic tobacco and sugarcane plants expressing the insecticidal peptide JBTX, showed increased resistance to attack of the insect pests Spodoptera frugiperda, Diatraea saccharalis and Telchin licus licus. Many questions remain unanswered; however, so far, JBTX has shown to be a versatile peptide that can be used against various insect and fungus species, and in new bacterial control strategies. Article in Journal/Newspaper Arctic Directory of Open Access Journals: DOAJ Articles Arctic Journal of Venomous Animals and Toxins including Tropical Diseases 23 1 |
institution |
Open Polar |
collection |
Directory of Open Access Journals: DOAJ Articles |
op_collection_id |
ftdoajarticles |
language |
English |
topic |
Peptide Bacteria Membranes Nanoparticles Arctic medicine. Tropical medicine RC955-962 Toxicology. Poisons RA1190-1270 Zoology QL1-991 |
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Peptide Bacteria Membranes Nanoparticles Arctic medicine. Tropical medicine RC955-962 Toxicology. Poisons RA1190-1270 Zoology QL1-991 Arlete Beatriz Becker-Ritt Camila Saretta Portugal Célia Regina Carlini Jaburetox: update on a urease-derived peptide |
topic_facet |
Peptide Bacteria Membranes Nanoparticles Arctic medicine. Tropical medicine RC955-962 Toxicology. Poisons RA1190-1270 Zoology QL1-991 |
description |
Abstract Urease from Canavalia ensiformis seeds was the first enzyme ever to be crystallized, in 1926. These proteins, found in plants, bacteria and fungi, present different biological properties including catalytic hydrolysis of urea, and also enzyme-independent activities, such as induction of exocytosis, pro-inflammatory effects, neurotoxicity, antifungal and insecticidal properties. Urease is toxic to insects and fungi per se but part of this toxicity relies on an internal peptide (~11 kDa), which is released upon digestion of the protein by insect enzymes. A recombinant form of this peptide, called jaburetox (JBTX), was constructed using jbureII gene as a template. The peptide exhibits liposome disruption properties, and insecticidal and fungicidal activities. Here we review the known biological properties activities of JBTX, and comment on new ones not yet fully characterized. JBTX was able to cause mortality of Aedes aegypti larvae in a feeding assay whereas in a dose as low as of 0.1 μg it provoked death of Triatoma infestans bugs. JBTX (10−5–10−6 M) inhibits the growth of E. coli, P. aeruginosa and B. cereus after 24 h incubation. Multilamellar liposomes interacting with JBTX undergo reorganization of the membrane’s lipids as detected by small angle X-ray scattering (SAXS) studies. Encapsulating JBTX into lipid nanoparticles led to an increase of the peptide’s antifungal activity. Transgenic tobacco and sugarcane plants expressing the insecticidal peptide JBTX, showed increased resistance to attack of the insect pests Spodoptera frugiperda, Diatraea saccharalis and Telchin licus licus. Many questions remain unanswered; however, so far, JBTX has shown to be a versatile peptide that can be used against various insect and fungus species, and in new bacterial control strategies. |
format |
Article in Journal/Newspaper |
author |
Arlete Beatriz Becker-Ritt Camila Saretta Portugal Célia Regina Carlini |
author_facet |
Arlete Beatriz Becker-Ritt Camila Saretta Portugal Célia Regina Carlini |
author_sort |
Arlete Beatriz Becker-Ritt |
title |
Jaburetox: update on a urease-derived peptide |
title_short |
Jaburetox: update on a urease-derived peptide |
title_full |
Jaburetox: update on a urease-derived peptide |
title_fullStr |
Jaburetox: update on a urease-derived peptide |
title_full_unstemmed |
Jaburetox: update on a urease-derived peptide |
title_sort |
jaburetox: update on a urease-derived peptide |
publisher |
SciELO |
publishDate |
2017 |
url |
https://doi.org/10.1186/s40409-017-0122-y https://doaj.org/article/0778924069264c6eb40742ef1b370402 |
geographic |
Arctic |
geographic_facet |
Arctic |
genre |
Arctic |
genre_facet |
Arctic |
op_source |
Journal of Venomous Animals and Toxins including Tropical Diseases, Vol 23, Iss 1, Pp 1-8 (2017) |
op_relation |
http://link.springer.com/article/10.1186/s40409-017-0122-y https://doaj.org/toc/1678-9199 doi:10.1186/s40409-017-0122-y 1678-9199 https://doaj.org/article/0778924069264c6eb40742ef1b370402 |
op_doi |
https://doi.org/10.1186/s40409-017-0122-y |
container_title |
Journal of Venomous Animals and Toxins including Tropical Diseases |
container_volume |
23 |
container_issue |
1 |
_version_ |
1766344035163701248 |