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Bioinsekticidni potencial egerolizinskih proteinov gliv iz rodu Pleurotus
ID Fortuna, Klavdija (Author), ID Sepčić, Kristina (Mentor) More about this mentor... This link opens in a new window, ID Panevska, Anastasija (Comentor)

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Abstract
Vezava egerolizinov iz gliv rodu Pleurotus na za nevretenčarje specifičen sfingolipid ceramid fosfoetanolamin (CPE) in tvorba transmembranskih por v povezavi s pleurotolizinom B (PlyB) kažeta na možnost uporabe egerolizinskih/PlyB kompleksov kot novih biopesticidov ter za razvoj gensko spremenjenih poljščin za zatiranje in nadzor nad nekaterimi rastlinskimi škodljivci. Erilizin A (EryA) je edini poznani glivni egerolizin, ki specifično reagira z membranami, ki so obogatene s CPE. Z mutirano različico EryA E69A smo, podobno kot pri egerolizinu ostreolizinu A6 (OlyA6), želeli izničiti holesterolno specifičnost vezave in povečati afiniteto vezave na CPE. Mutirane različice nam ni uspelo pridobiti, zato njegova nadaljnja karakterizacija ni bila mogoča. Kompleks OlyA6/PlyB ima po podatkih prejšnjih raziskav najmočnejše litično delovanje med vsemi raziskanimi egerolizin/PlyB kompleksi, še močnejšo insekticidno aktivnost pa bi lahko izkazovala mutirana različica OlyA6 E69A. Obe različici proteina (OlyA6 in OlyA6 E69A) v odsotnosti proteinskega partnerja PlyB ne delujeta litično, medtem ko sta v kombinaciji s PlyB zelo litični že pri nizkih koncentracijah, ko je v membranah prisoten holesterol (Hol). Afiniteta vezave mutirane različice na vezikle, ki ne vsebujejo Hol, se v primerjavi z divjo obliko proteina poveča, medtem ko kompleks OlyA6 E69A/PlyB v primerjavi s kompleksom OlyA6/PlyB ni izkazoval večje porotvornosti na bioloških membranah. Potrdili smo, da OlyA6 E69A prepozna različne konformacije CPE v bioloških membranah, zato bi bila ta mutirana različica proteina lahko biotehnološko zelo pomembna, saj je veliko žuželk avksotrofnih za Hol.

Language:Slovenian
Keywords:bioinsekticid, egerolizin, marmorirana smrdljivka, membranski lipidi, ostrigar, porotvorni protein, protein z domeno MACPF
Work type:Master's thesis/paper
Typology:2.09 - Master's Thesis
Organization:BF - Biotechnical Faculty
Year:2022
PID:20.500.12556/RUL-139835 This link opens in a new window
COBISS.SI-ID:125241603 This link opens in a new window
Publication date in RUL:08.09.2022
Views:660
Downloads:10
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Secondary language

Language:English
Title:BIOINSECTICIDAL POTENTIAL OF AEGEROLYSIN PROTEINS FROM MUSHROOMS OF THE GENUS Pleurotus
Abstract:
Binding of Pleurotus aegerolysins to invertebrate-specific sphingolipid ceramide phosphoethanolamine (CPE) and the formation of transmembrane pores in association with pleurotolysin B (PlyB) suggest the possibility of using aegerolysin/PlyB complexes as novel biopesticides as well as producing genetically modified crops resistant to from an economical point of view important pests. Erylysin A (EryA) is the only known fungal aegerolysin that specifically interacts with CPE-enriched membranes. By isolating the single point mutant, EryA E69A, we sought to eliminate cholesterol-specific binding and increase the affinity for CPE. The mutant could not be obtained so its further characterization was not possible. According to previous research, the OlyA6/PlyB complex has the strongest lytic activity of all aegerolysin/PlyB complexes studied and an even stronger insecticidal activity could be shown by using the OlyA6 E69A mutant. Both versions of the protein do not exhibit lytic activity in the absence of the PlyB protein partner, while in combination with PlyB they are both lytic even at low concentrations when cholesterol (Chol) is present in the membranes. The binding affinity of the mutant to Chol-free vesicles is increased compared to the wild type protein, while the OlyA6 E69A/PlyB complex showed no greater permeabilization of biological membranes compared to the OlyA6/PlyB complex. We confirmed that OlyA6 E69A recognizes different CPE conformations in biological membranes, confirming that this mutant could be biotechnologically very important as many insects are auxotrophic for Chol.

Keywords:bioinsecticide, aegerolysin, brown marmorated stink bug, membrane lipids, oyster mushroom, pore-forming protein, MACPF-protein

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