First evidence of cholinesterase-like activity in Basidiomycota.
Cholinesterases (ChE), the enzymes whose primary function is the hydrolysis of choline esters, are widely expressed throughout the nature. Although they have already been found in plants and microorganisms, including ascomycete fungi, this study is the first report of ChE-like activity in fungi of t...
| Main Authors: | , , , , |
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| Format: | Article |
| Language: | English |
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Public Library of Science (PLoS)
2019-01-01
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| Series: | PLoS ONE |
| Online Access: | https://doi.org/10.1371/journal.pone.0216077 |
| _version_ | 1818726921178972160 |
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| author | Kristina Sepčić Jerica Sabotič Robin A Ohm Damjana Drobne Anita Jemec Kokalj |
| author_facet | Kristina Sepčić Jerica Sabotič Robin A Ohm Damjana Drobne Anita Jemec Kokalj |
| author_sort | Kristina Sepčić |
| collection | DOAJ |
| description | Cholinesterases (ChE), the enzymes whose primary function is the hydrolysis of choline esters, are widely expressed throughout the nature. Although they have already been found in plants and microorganisms, including ascomycete fungi, this study is the first report of ChE-like activity in fungi of the phylum Basidiomycota. This activity was detected in almost a quarter of the 45 tested aqueous fungal extracts. The ability of these extracts to hydrolyse acetylthiocholine was about ten times stronger than the hydrolytic activity towards butyrylthiocholine and propionylthiocholine. In-gel detection of ChE-like activity with acetylthiocholine indicated a great variability in the characteristics of these enzymes which are not characterized as vertebrate-like based on (i) differences in inhibition by excess substrate, (ii) susceptibility to different vertebrate acetylcholinesterase and butyrylcholinesterase inhibitors, and (iii) a lack of orthologs using phylogenetic analysis. Limited inhibition by single inhibitors and multiple activity bands using in-gel detection indicate the presence of several ChE-like enzymes in these aqueous extracts. We also observed inhibitory activity of the same aqueous mushroom extracts against insect acetylcholinesterase in 10 of the 45 samples tested; activity was independent of the presence of ChE-like activity in extracts. Both ChE-like activities with different substrates and the ability of extracts to inhibit insect acetylcholinesterase were not restricted to any fungal family but were rather present across all included Basidiomycota families. This study can serve as a platform for further research regarding ChE activity in mushrooms. |
| first_indexed | 2024-12-17T22:05:53Z |
| format | Article |
| id | doaj.art-a684fb1d692a4821a4ca1e0214a92cc7 |
| institution | Directory Open Access Journal |
| issn | 1932-6203 |
| language | English |
| last_indexed | 2024-12-17T22:05:53Z |
| publishDate | 2019-01-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj.art-a684fb1d692a4821a4ca1e0214a92cc72022-12-21T21:30:52ZengPublic Library of Science (PLoS)PLoS ONE1932-62032019-01-01144e021607710.1371/journal.pone.0216077First evidence of cholinesterase-like activity in Basidiomycota.Kristina SepčićJerica SabotičRobin A OhmDamjana DrobneAnita Jemec KokaljCholinesterases (ChE), the enzymes whose primary function is the hydrolysis of choline esters, are widely expressed throughout the nature. Although they have already been found in plants and microorganisms, including ascomycete fungi, this study is the first report of ChE-like activity in fungi of the phylum Basidiomycota. This activity was detected in almost a quarter of the 45 tested aqueous fungal extracts. The ability of these extracts to hydrolyse acetylthiocholine was about ten times stronger than the hydrolytic activity towards butyrylthiocholine and propionylthiocholine. In-gel detection of ChE-like activity with acetylthiocholine indicated a great variability in the characteristics of these enzymes which are not characterized as vertebrate-like based on (i) differences in inhibition by excess substrate, (ii) susceptibility to different vertebrate acetylcholinesterase and butyrylcholinesterase inhibitors, and (iii) a lack of orthologs using phylogenetic analysis. Limited inhibition by single inhibitors and multiple activity bands using in-gel detection indicate the presence of several ChE-like enzymes in these aqueous extracts. We also observed inhibitory activity of the same aqueous mushroom extracts against insect acetylcholinesterase in 10 of the 45 samples tested; activity was independent of the presence of ChE-like activity in extracts. Both ChE-like activities with different substrates and the ability of extracts to inhibit insect acetylcholinesterase were not restricted to any fungal family but were rather present across all included Basidiomycota families. This study can serve as a platform for further research regarding ChE activity in mushrooms.https://doi.org/10.1371/journal.pone.0216077 |
| spellingShingle | Kristina Sepčić Jerica Sabotič Robin A Ohm Damjana Drobne Anita Jemec Kokalj First evidence of cholinesterase-like activity in Basidiomycota. PLoS ONE |
| title | First evidence of cholinesterase-like activity in Basidiomycota. |
| title_full | First evidence of cholinesterase-like activity in Basidiomycota. |
| title_fullStr | First evidence of cholinesterase-like activity in Basidiomycota. |
| title_full_unstemmed | First evidence of cholinesterase-like activity in Basidiomycota. |
| title_short | First evidence of cholinesterase-like activity in Basidiomycota. |
| title_sort | first evidence of cholinesterase like activity in basidiomycota |
| url | https://doi.org/10.1371/journal.pone.0216077 |
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