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Dissecting out the molecular mechanism of insecticidal activity of ostreolysin A6/pleurotolysin B complexes on western corn rootworm
ID Milijaš Jotić, Matej (Author), ID Panevska, Anastasija (Author), ID Iacovache, Ioan (Author), ID Kostanjšek, Rok (Author), ID Mravinec, Martina (Author), ID Skočaj, Matej (Author), ID Zuber, Benoît (Author), ID Pavšič, Ana (Author), ID Razinger, Jaka (Author), ID Modic, Špela (Author), ID Trenti, Francesco (Author), ID Guella, Graziano (Author), ID Sepčić, Kristina (Author)

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Abstract
Ostreolysin A6 (OlyA6) is a protein produced by the oyster mushroom (Pleurotus ostreatus). It binds to membrane sphingomyelin/cholesterol domains, and together with its protein partner, pleurotolysin B (PlyB), it forms 13-meric transmembrane pore complexes. Further, OlyA6 binds 1000 times more strongly to the insect-specific membrane sphingolipid, ceramide phosphoethanolamine (CPE). In concert with PlyB, OlyA6 has potent and selective insecticidal activity against the western corn rootworm. We analysed the histological alterations of the midgut wall columnar epithelium of western corn rootworm larvae fed with OlyA6/PlyB, which showed vacuolisation of the cell cytoplasm, swelling of the apical cell surface into the gut lumen, and delamination of the basal lamina underlying the epithelium. Additionally, cryo-electron microscopy was used to explore the membrane interactions of the OlyA6/PlyB complex using lipid vesicles composed of artificial lipids containing CPE, and western corn rootworm brush border membrane vesicles. Multimeric transmembrane pores were formed in both vesicle preparations, similar to those described for sphingomyelin/cholesterol membranes. These results strongly suggest that the molecular mechanism of insecticidal action of OlyA6/PlyB arises from specific interactions of OlyA6 with CPE, and the consequent formation of transmembrane pores in the insect midgut.

Language:English
Keywords:aegerolysin, bioinsecticide, MACPF-protein, oyster mushroom, pore-forming protein, western corn rootworm
Work type:Article
Typology:1.01 - Original Scientific Article
Organization:BF - Biotechnical Faculty
Publication status:Published
Publication version:Version of Record
Year:2021
Number of pages:16 str.
Numbering:Vol. 13, iss. 7, art. 455
PID:20.500.12556/RUL-135717 This link opens in a new window
UDC:577
ISSN on article:2072-6651
DOI:10.3390/toxins13070455 This link opens in a new window
COBISS.SI-ID:68691203 This link opens in a new window
Publication date in RUL:29.03.2022
Views:582
Downloads:117
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Record is a part of a journal

Title:Toxins : Elektronski vir
Shortened title:Toxins
Publisher:MDPI
ISSN:2072-6651
COBISS.SI-ID:517594649 This link opens in a new window

Licences

License:CC BY 4.0, Creative Commons Attribution 4.0 International
Link:http://creativecommons.org/licenses/by/4.0/
Description:This is the standard Creative Commons license that gives others maximum freedom to do what they want with the work as long as they credit the author.
Licensing start date:01.07.2021

Secondary language

Language:Slovenian
Keywords:egerolizin, bioinsekticid, protein z domeno MACPF, bukov ostrigar, porotvorni protein, koruzni hrošč

Projects

Funder:ARRS - Slovenian Research Agency
Project number:J4-1772
Name:Proteinski kompleksi iz glivnega rodu Pleurotus kot novi biopesticidi za zatiranje koloradskega in koruznega hrošča

Funder:ARRS - Slovenian Research Agency
Project number:P1-0207
Name:Toksini in biomembrane

Funder:ARRS - Slovenian Research Agency
Project number:P4-0072
Name:Agrobiodiverziteta

Funder:SNSF - Swiss National Science Foundation
Project number:179520

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