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Bioinformatics Analysis and Functional Characterization of the CFEM Proteins of Metarhizium anisopliae
The entomopathogen Metarhizium anisopliae is a facultative rhizosphere or endophytic fungus available for managing pests and improving plant growth. The CFEM (common in fungal extracellular membrane) proteins form a unique group in fungi but are rarely reported in entomopathogens. In this study, we...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9318983/ https://www.ncbi.nlm.nih.gov/pubmed/35887418 http://dx.doi.org/10.3390/jof8070661 |
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author | Cai, Ni Liu, Rong Yan, Duozi Zhang, Neng Zhu, Kaihui Zhang, Daogang Nong, Xiangqun Tu, Xiongbing Zhang, Zehua Wang, Guangjun |
author_facet | Cai, Ni Liu, Rong Yan, Duozi Zhang, Neng Zhu, Kaihui Zhang, Daogang Nong, Xiangqun Tu, Xiongbing Zhang, Zehua Wang, Guangjun |
author_sort | Cai, Ni |
collection | PubMed |
description | The entomopathogen Metarhizium anisopliae is a facultative rhizosphere or endophytic fungus available for managing pests and improving plant growth. The CFEM (common in fungal extracellular membrane) proteins form a unique group in fungi but are rarely reported in entomopathogens. In this study, we cloned and identified 13 CFEM genes from M. anisopliae (MaCFEMs). Sequence alignment and WebLogo analysis showed that eight cysteines were the most conserved amino acids in their CFEM domain. Phylogenic analysis suggested that these 13 proteins could be divided into 4 clades based on the presence of the transmembrane region and the position of CFEM domain in the whole sequence. Six MaCFEM proteins with a signal peptide and without a transmembrane domain were considered candidate effector proteins. According to Phyre2 analysis, the MaCFEM88 and MaCFEM85 have the most homologous to Csa2 in Candida albicans. Subcellular localization analysis revealed that five effectors were located in the plasma membrane, while MaCFEM88 may locate in both plasma membrane and nucleus in the treated Nicotiana benthamiana. Expression pattern analysis showed that MaCFEM81, 85, 88, and 89 expression level was significantly higher in the sporulation stage compared to other growth stages. Furthermore, the yeast secretion assay showed that six candidate effectors were able to secrete out of the cell. All of the MaCFEMs couldn’t affect INF1-induced programmed cell death (PCD), but MaCFEM85 and 88 could trigger a slight hypersensitive response both when applied separately or in combination with INF1 in N. benthamiana leaves. These findings showed that six MaCFEM potential effectors with various structures and subcellular localizations in host cells might be used to illustrate the roles of MaCFEM proteins during M. anisopliae-plant interactions. |
format | Online Article Text |
id | pubmed-9318983 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-93189832022-07-27 Bioinformatics Analysis and Functional Characterization of the CFEM Proteins of Metarhizium anisopliae Cai, Ni Liu, Rong Yan, Duozi Zhang, Neng Zhu, Kaihui Zhang, Daogang Nong, Xiangqun Tu, Xiongbing Zhang, Zehua Wang, Guangjun J Fungi (Basel) Article The entomopathogen Metarhizium anisopliae is a facultative rhizosphere or endophytic fungus available for managing pests and improving plant growth. The CFEM (common in fungal extracellular membrane) proteins form a unique group in fungi but are rarely reported in entomopathogens. In this study, we cloned and identified 13 CFEM genes from M. anisopliae (MaCFEMs). Sequence alignment and WebLogo analysis showed that eight cysteines were the most conserved amino acids in their CFEM domain. Phylogenic analysis suggested that these 13 proteins could be divided into 4 clades based on the presence of the transmembrane region and the position of CFEM domain in the whole sequence. Six MaCFEM proteins with a signal peptide and without a transmembrane domain were considered candidate effector proteins. According to Phyre2 analysis, the MaCFEM88 and MaCFEM85 have the most homologous to Csa2 in Candida albicans. Subcellular localization analysis revealed that five effectors were located in the plasma membrane, while MaCFEM88 may locate in both plasma membrane and nucleus in the treated Nicotiana benthamiana. Expression pattern analysis showed that MaCFEM81, 85, 88, and 89 expression level was significantly higher in the sporulation stage compared to other growth stages. Furthermore, the yeast secretion assay showed that six candidate effectors were able to secrete out of the cell. All of the MaCFEMs couldn’t affect INF1-induced programmed cell death (PCD), but MaCFEM85 and 88 could trigger a slight hypersensitive response both when applied separately or in combination with INF1 in N. benthamiana leaves. These findings showed that six MaCFEM potential effectors with various structures and subcellular localizations in host cells might be used to illustrate the roles of MaCFEM proteins during M. anisopliae-plant interactions. MDPI 2022-06-24 /pmc/articles/PMC9318983/ /pubmed/35887418 http://dx.doi.org/10.3390/jof8070661 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Cai, Ni Liu, Rong Yan, Duozi Zhang, Neng Zhu, Kaihui Zhang, Daogang Nong, Xiangqun Tu, Xiongbing Zhang, Zehua Wang, Guangjun Bioinformatics Analysis and Functional Characterization of the CFEM Proteins of Metarhizium anisopliae |
title | Bioinformatics Analysis and Functional Characterization of the CFEM Proteins of Metarhizium anisopliae |
title_full | Bioinformatics Analysis and Functional Characterization of the CFEM Proteins of Metarhizium anisopliae |
title_fullStr | Bioinformatics Analysis and Functional Characterization of the CFEM Proteins of Metarhizium anisopliae |
title_full_unstemmed | Bioinformatics Analysis and Functional Characterization of the CFEM Proteins of Metarhizium anisopliae |
title_short | Bioinformatics Analysis and Functional Characterization of the CFEM Proteins of Metarhizium anisopliae |
title_sort | bioinformatics analysis and functional characterization of the cfem proteins of metarhizium anisopliae |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9318983/ https://www.ncbi.nlm.nih.gov/pubmed/35887418 http://dx.doi.org/10.3390/jof8070661 |
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