Lipid-binding aegerolysin from biocontrol fungus Beauveria bassiana

Kraševec, Nada (avtor), Panevska, Anastasija (avtor), Lemež, Špela (avtor), Razinger, Jaka (avtor), Sepčić, Kristina (avtor), Anderluh, Gregor (avtor), Podobnik, Marjetka (avtor)

Fungi are the most common pathogens of insects and thus important regulators of their populations. Lipid-binding aegerolysin proteins, which are commonly found in the fungal kingdom, may be involved in several biologically relevant processes including attack and defense against other organisms. Aegerolysins act alone or together with membrane-attack-complex/perforin (MACPF)-like proteins to form transmembrane pores that lead to cell lysis. We performed an in-depth bioinformatics analysis of aegerolysins in entomopathogenic fungi and selected a candidate aegerolysin, beauveriolysin A (BlyA) from Beauveria bassiana. BlyA was expressed as a recombinant protein in Escherichia coli, and purified to further determine its functional and structural properties, including lipid-binding ability. Aegerolysins were found to be encoded in genomes of entomopathogenic fungi, such as Beauveria, Cordyceps, Metarhizium and Ophiocordyceps. Detailed bioinformatics analysis revealed that they are linked to MACPF-like genes in most genomes. We also show that BlyA interacts with an insect-specific membrane lipid. These results were placed in the context of other fungal and bacterial aegerolysins and their partner proteins. We believe that aegerolysins play a role in promoting the entomopathogenic and antagonistic activity of B. bassiana, which is an active ingredient of bioinsecticides.

• Jezik: Angleški jezik
• Ključne besede: beauveriolysin, membrane-attack-complex/perforin (MACPF) protein, pore-forming proteins, entomopathogenic and antagonistic fungi, bioinformatics, ceramide phosphoethanolamine (CPE), lipid binding
• Vrsta gradiva: Članek v reviji
• Tipologija: 1.01 - Izvirni znanstveni članek
• Organizacija: BF - Biotehniška fakulteta
• Status publikacije: Objavljeno
• Različica publikacije: Objavljena publikacija
• Leto izida: 2021
• Št. strani: 23 str.
• Številčenje: Vol. 13, iss. 11, art. 820
• PID: 20.500.12556/RUL-136364
• UDK: 615.9
• ISSN pri članku: 2072-6651
• DOI: 10.3390/toxins13110820
• COBISS.SI-ID: 87179523
• Datum objave v RUL: 26.04.2022

Gradivo je del revije

• Naslov: Toxins : Elektronski vir
• Skrajšan naslov: Toxins
• Založnik: MDPI
• ISSN: 2072-6651
• COBISS.SI-ID: 517594649

Licence

• Licenca: CC BY 4.0, Creative Commons Priznanje avtorstva 4.0 Mednarodna
• Povezava: http://creativecommons.org/licenses/by/4.0/deed.sl
• Opis: To je standardna licenca Creative Commons, ki daje uporabnikom največ možnosti za nadaljnjo uporabo dela, pri čemer morajo navesti avtorja.
• Začetek licenciranja: 20.11.2021

Sekundarni jezik

• Jezik: Slovenski jezik
• Ključne besede: boveriolizin, MACPF-protein, porotvorni proteini, entomopatogene in antagonistične glive, bioinformatika, ceramid fosfoetanolamin (CPE), vezava na lipide