Your browser does not allow JavaScript!
JavaScript is necessary for the proper functioning of this website. Please enable JavaScript or use a modern browser.
Open Science Slovenia
Open Science
DiKUL
slv
|
eng
Search
Browse
New in RUL
About RUL
In numbers
Help
Sign in
Unconventional secretion of nigerolysins A from Aspergillus species
ID
Kraševec, Nada
(
Author
),
ID
Novak, Maruša
(
Author
),
ID
Barat, Simona
(
Author
),
ID
Skočaj, Matej
(
Author
),
ID
Sepčić, Kristina
(
Author
),
ID
Anderluh, Gregor
(
Author
)
PDF - Presentation file,
Download
(5,19 MB)
MD5: C45B9FC36BB436CE1FBD0E8C9310F359
URL - Source URL, Visit
https://www.mdpi.com/2076-2607/8/12/1973
Image galllery
Abstract
Aegerolysins are small lipid-binding proteins particularly abundant in fungi. Aegerolysins from oyster mushrooms interact with an insect-specific membrane lipid and, together with MACPF proteins produced by the same organism, form pesticidal pore-forming complexes. The specific interaction with the same membrane lipid was recently demonstrated for nigerolysin A2 (NigA2), an aegerolysin from Aspergillus niger. In Aspergillus species, the aegerolysins were frequently found as secreted proteins, indicating their function in fungal defense. Using immunocytochemistry and live-cell imaging we investigated the subcellular localization of the nigerolysins A in A. niger, while their secretion was addressed by secretion prediction and Western blotting. We show that both nigerolysins A are leaderless proteins that reach the cell exterior by an unconventional protein secretion. NigA proteins are evenly distributed in the cytoplasm of fungal hyphae. A detailed bioinformatics analysis of Aspergillus aegerolysins suggests that the same function occurs only in a limited number of aegerolysins. From alignment, analysis of chromosomal loci, orthology, synteny, and phylogeny it follows that the same or a similar function described for pairs of pesticidal proteins of Pleurotus sp. can be expected in species of the subgenus Circumdati, section Nigri, series Nigri, and some other species with adjacent pairs of putative pesticidal proteins.
Language:
English
Keywords:
aegerolysin
,
nigerolysin
,
membrane-attack-complex/perforin (MACPF) protein
,
Aspergillus
,
Fungi
,
bioinformatics
,
localization
,
unconventional secretion
,
ceramide phosphoethanolamine (CPE)
,
invertebrate lipid binding
Work type:
Article
Typology:
1.01 - Original Scientific Article
Organization:
BF - Biotechnical Faculty
Publication status:
Published
Publication version:
Version of Record
Year:
2020
Number of pages:
23 str.
Numbering:
Vol. 8, iss. 12, art. 1973
PID:
20.500.12556/RUL-134669
UDC:
577
ISSN on article:
2076-2607
DOI:
10.3390/microorganisms8121973
COBISS.SI-ID:
42464771
Publication date in RUL:
25.01.2022
Views:
810
Downloads:
133
Metadata:
Cite this work
Plain text
BibTeX
EndNote XML
EndNote/Refer
RIS
ABNT
ACM Ref
AMA
APA
Chicago 17th Author-Date
Harvard
IEEE
ISO 690
MLA
Vancouver
:
Copy citation
Share:
Record is a part of a journal
Title:
Microorganisms
Shortened title:
Microorganisms
Publisher:
MDPI AG
ISSN:
2076-2607
COBISS.SI-ID:
523277081
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:
11.12.2020
Secondary language
Language:
Slovenian
Keywords:
egerolizin
,
nigerolizin
,
MACPF-protein
,
Aspergillus
,
glive
,
bioinformatika
,
lokalizacija
,
nekonvencionalna sekrecija
,
ceramid fosfoetanolamin
,
vezava na nevretenčarske lipide
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:
P1-0391
Name:
Molekulske interakcije
Funder:
ARRS - Slovenian Research Agency
Project number:
P1-0207
Name:
Toksini in biomembrane
Similar documents
Similar works from RUL:
Similar works from other Slovenian collections:
Back