Glucose-6-phosphate 1-Epimerase CrGlu6 Contributes to Development and Biocontrol Efficiency in <i>Clonostachys chloroleuca</i>

<i>Clonostachys chloroleuca</i> (formerly classified as <i>C. rosea</i>) is an important mycoparasite active against various plant fungal pathogens. Mitogen-activated protein kinase (MAPK) signaling pathways are vital in mycoparasitic interactions; they participate in respons...

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Main Authors: Binna Lv, Yan Guo, Xue Zhao, Shidong Li, Manhong Sun
Format: Article
Language:English
Published: MDPI AG 2023-07-01
Series:Journal of Fungi
Subjects:
Online Access:https://www.mdpi.com/2309-608X/9/7/764
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author Binna Lv
Yan Guo
Xue Zhao
Shidong Li
Manhong Sun
author_facet Binna Lv
Yan Guo
Xue Zhao
Shidong Li
Manhong Sun
author_sort Binna Lv
collection DOAJ
description <i>Clonostachys chloroleuca</i> (formerly classified as <i>C. rosea</i>) is an important mycoparasite active against various plant fungal pathogens. Mitogen-activated protein kinase (MAPK) signaling pathways are vital in mycoparasitic interactions; they participate in responses to diverse stresses and mediate fungal development. In previous studies, the MAPK-encoding gene <i>Crmapk</i> has been proven to be involved in mycoparasitism and the biocontrol processes of <i>C. chloroleuca</i>, but its regulatory mechanisms remain unclear. Aldose 1-epimerases are key enzymes in filamentous fungi that generate energy for fungal growth and development. By protein–protein interaction assays, the glucose-6-phosphate 1-epimerase CrGlu6 was found to interact with Crmapk, and expression of the <i>CrGlu6</i> gene was significantly upregulated when <i>C. chloroleuca</i> colonized <i>Sclerotinia sclerotiorum</i> sclerotia. Gene deletion and complementation analyses showed that <i>CrGlu6</i> deficiency caused abnormal morphology of hyphae and cells, and greatly reduced conidiation. Moreover, deletion mutants presented much lower antifungal activities and mycoparasitic ability, and control efficiency against sclerotinia stem rot was markedly decreased. When the <i>CrGlu6</i> gene was reinserted, all biological characteristics and biocontrol activities were recovered. These findings provide new insight into the mechanisms of glucose-6-phosphate 1-epimerase in mycoparasitism and help to further reveal the regulation of MAPK and its interacting proteins in the biocontrol of <i>C. chloroleuca</i>.
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spelling doaj.art-ce0ae55066c24076ba9edb1f23a86eb12023-11-18T20:02:06ZengMDPI AGJournal of Fungi2309-608X2023-07-019776410.3390/jof9070764Glucose-6-phosphate 1-Epimerase CrGlu6 Contributes to Development and Biocontrol Efficiency in <i>Clonostachys chloroleuca</i>Binna Lv0Yan Guo1Xue Zhao2Shidong Li3Manhong Sun4Institute of Plant Protection, Chinese Academy of Agricultural Sciences, Beijing 100193, ChinaInstitute of Plant Protection, Chinese Academy of Agricultural Sciences, Beijing 100193, ChinaInstitute of Plant Protection, Chinese Academy of Agricultural Sciences, Beijing 100193, ChinaInstitute of Plant Protection, Chinese Academy of Agricultural Sciences, Beijing 100193, ChinaInstitute of Plant Protection, Chinese Academy of Agricultural Sciences, Beijing 100193, China<i>Clonostachys chloroleuca</i> (formerly classified as <i>C. rosea</i>) is an important mycoparasite active against various plant fungal pathogens. Mitogen-activated protein kinase (MAPK) signaling pathways are vital in mycoparasitic interactions; they participate in responses to diverse stresses and mediate fungal development. In previous studies, the MAPK-encoding gene <i>Crmapk</i> has been proven to be involved in mycoparasitism and the biocontrol processes of <i>C. chloroleuca</i>, but its regulatory mechanisms remain unclear. Aldose 1-epimerases are key enzymes in filamentous fungi that generate energy for fungal growth and development. By protein–protein interaction assays, the glucose-6-phosphate 1-epimerase CrGlu6 was found to interact with Crmapk, and expression of the <i>CrGlu6</i> gene was significantly upregulated when <i>C. chloroleuca</i> colonized <i>Sclerotinia sclerotiorum</i> sclerotia. Gene deletion and complementation analyses showed that <i>CrGlu6</i> deficiency caused abnormal morphology of hyphae and cells, and greatly reduced conidiation. Moreover, deletion mutants presented much lower antifungal activities and mycoparasitic ability, and control efficiency against sclerotinia stem rot was markedly decreased. When the <i>CrGlu6</i> gene was reinserted, all biological characteristics and biocontrol activities were recovered. These findings provide new insight into the mechanisms of glucose-6-phosphate 1-epimerase in mycoparasitism and help to further reveal the regulation of MAPK and its interacting proteins in the biocontrol of <i>C. chloroleuca</i>.https://www.mdpi.com/2309-608X/9/7/764biocontrol<i>Clonostachys chloroleuca</i>glucose-6-phosphate 1-epimeraseMAPKmycoparasitism<i>Sclerotinia sclerotiorum</i>
spellingShingle Binna Lv
Yan Guo
Xue Zhao
Shidong Li
Manhong Sun
Glucose-6-phosphate 1-Epimerase CrGlu6 Contributes to Development and Biocontrol Efficiency in <i>Clonostachys chloroleuca</i>
Journal of Fungi
biocontrol
<i>Clonostachys chloroleuca</i>
glucose-6-phosphate 1-epimerase
MAPK
mycoparasitism
<i>Sclerotinia sclerotiorum</i>
title Glucose-6-phosphate 1-Epimerase CrGlu6 Contributes to Development and Biocontrol Efficiency in <i>Clonostachys chloroleuca</i>
title_full Glucose-6-phosphate 1-Epimerase CrGlu6 Contributes to Development and Biocontrol Efficiency in <i>Clonostachys chloroleuca</i>
title_fullStr Glucose-6-phosphate 1-Epimerase CrGlu6 Contributes to Development and Biocontrol Efficiency in <i>Clonostachys chloroleuca</i>
title_full_unstemmed Glucose-6-phosphate 1-Epimerase CrGlu6 Contributes to Development and Biocontrol Efficiency in <i>Clonostachys chloroleuca</i>
title_short Glucose-6-phosphate 1-Epimerase CrGlu6 Contributes to Development and Biocontrol Efficiency in <i>Clonostachys chloroleuca</i>
title_sort glucose 6 phosphate 1 epimerase crglu6 contributes to development and biocontrol efficiency in i clonostachys chloroleuca i
topic biocontrol
<i>Clonostachys chloroleuca</i>
glucose-6-phosphate 1-epimerase
MAPK
mycoparasitism
<i>Sclerotinia sclerotiorum</i>
url https://www.mdpi.com/2309-608X/9/7/764
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