Two eisosome proteins play opposite roles in autophagic control and sustain cell integrity, function and pathogenicity in Beauveria bassiana.
Identifieur interne : 000853 ( Main/Corpus ); précédent : 000852; suivant : 000854Two eisosome proteins play opposite roles in autophagic control and sustain cell integrity, function and pathogenicity in Beauveria bassiana.
Auteurs : Long-Bin Zhang ; Li Tang ; Sheng-Hua Ying ; Ming-Guang FengSource :
- Environmental microbiology [ 1462-2920 ] ; 2017.
English descriptors
- KwdEn :
- Animals (MeSH), Autophagy (physiology), Beauveria (genetics), Beauveria (pathogenicity), Cell Membrane (metabolism), Cell Wall (metabolism), Endocytosis (physiology), Fungal Proteins (genetics), Hyphae (metabolism), Insecta (microbiology), Protein Domains (physiology), Sirolimus (pharmacology), Spores, Fungal (metabolism), Virulence (genetics).
- MESH :
- chemical , genetics : Fungal Proteins.
- genetics : Beauveria, Virulence.
- metabolism : Cell Membrane, Cell Wall, Hyphae, Spores, Fungal.
- microbiology : Insecta.
- pathogenicity : Beauveria.
- chemical , pharmacology : Sirolimus.
- physiology : Autophagy, Endocytosis, Protein Domains.
- Animals.
Abstract
Pil1A and Pil1B are two core eisosome proteins that are homologous to yeast Pil1/Lsp1 or filamentous fungal Pil1A/Pil1B but have been unexplored in entomopathogenic fungi. Here we examined subcellular localization and functions of Pil1A and Pil1B in Beauveria bassiana, a fungal insect pathogen. Either localization or co-localization experiments of the two proteins demonstrated that Pil1A and Pil1B were simultaneously localized at the periphery of hyphal cells for formation of stable, punctuate spots in B. bassiana. This is different from a reliance of proper Lsp1/Pil1B localization upon Pil1/Pil1A in other fungi. Deletions of pil1A and pil1B caused opposite changes in expression of many autophagy-related genes and formation of intravacuolar autophagosomes. Such opposite changes were restored to nearly normal status by exogenous rapamycin, implicating a link of Pil1A/B to the target of rapamycin signalling pathway. All single/double deletion mutants of pil1A and pil1B lost almost all pathogenicity due to reduced ability to secrete Pr1 proteases for cuticle degradation. They also showed differential changes in cell wall integrity and multiple stress responses. These findings unveil opposite roles for Pil1A and Pil1B in autophagic regulation and an essentiality of both for cell integrity, function and pathogenicity of the fungal entomopathogen.
DOI: 10.1111/1462-2920.13727
PubMed: 28276124
Links to Exploration step
pubmed:28276124Le document en format XML
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<author><name sortKey="Zhang, Long Bin" sort="Zhang, Long Bin" uniqKey="Zhang L" first="Long-Bin" last="Zhang">Long-Bin Zhang</name>
<affiliation><nlm:affiliation>Institute of Microbiology, College of Life Sciences, Zhejiang University, Hangzhou, Zhejiang, 310058, People's Republic of China.</nlm:affiliation>
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<author><name sortKey="Tang, Li" sort="Tang, Li" uniqKey="Tang L" first="Li" last="Tang">Li Tang</name>
<affiliation><nlm:affiliation>Institute of Microbiology, College of Life Sciences, Zhejiang University, Hangzhou, Zhejiang, 310058, People's Republic of China.</nlm:affiliation>
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<author><name sortKey="Ying, Sheng Hua" sort="Ying, Sheng Hua" uniqKey="Ying S" first="Sheng-Hua" last="Ying">Sheng-Hua Ying</name>
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<author><name sortKey="Feng, Ming Guang" sort="Feng, Ming Guang" uniqKey="Feng M" first="Ming-Guang" last="Feng">Ming-Guang Feng</name>
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<sourceDesc><biblStruct><analytic><title xml:lang="en">Two eisosome proteins play opposite roles in autophagic control and sustain cell integrity, function and pathogenicity in Beauveria bassiana.</title>
<author><name sortKey="Zhang, Long Bin" sort="Zhang, Long Bin" uniqKey="Zhang L" first="Long-Bin" last="Zhang">Long-Bin Zhang</name>
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<term>Autophagy (physiology)</term>
<term>Beauveria (genetics)</term>
<term>Beauveria (pathogenicity)</term>
<term>Cell Membrane (metabolism)</term>
<term>Cell Wall (metabolism)</term>
<term>Endocytosis (physiology)</term>
<term>Fungal Proteins (genetics)</term>
<term>Hyphae (metabolism)</term>
<term>Insecta (microbiology)</term>
<term>Protein Domains (physiology)</term>
<term>Sirolimus (pharmacology)</term>
<term>Spores, Fungal (metabolism)</term>
<term>Virulence (genetics)</term>
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<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Fungal Proteins</term>
</keywords>
<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Beauveria</term>
<term>Virulence</term>
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<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Cell Membrane</term>
<term>Cell Wall</term>
<term>Hyphae</term>
<term>Spores, Fungal</term>
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<keywords scheme="MESH" qualifier="microbiology" xml:lang="en"><term>Insecta</term>
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<keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Sirolimus</term>
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<front><div type="abstract" xml:lang="en">Pil1A and Pil1B are two core eisosome proteins that are homologous to yeast Pil1/Lsp1 or filamentous fungal Pil1A/Pil1B but have been unexplored in entomopathogenic fungi. Here we examined subcellular localization and functions of Pil1A and Pil1B in Beauveria bassiana, a fungal insect pathogen. Either localization or co-localization experiments of the two proteins demonstrated that Pil1A and Pil1B were simultaneously localized at the periphery of hyphal cells for formation of stable, punctuate spots in B. bassiana. This is different from a reliance of proper Lsp1/Pil1B localization upon Pil1/Pil1A in other fungi. Deletions of pil1A and pil1B caused opposite changes in expression of many autophagy-related genes and formation of intravacuolar autophagosomes. Such opposite changes were restored to nearly normal status by exogenous rapamycin, implicating a link of Pil1A/B to the target of rapamycin signalling pathway. All single/double deletion mutants of pil1A and pil1B lost almost all pathogenicity due to reduced ability to secrete Pr1 proteases for cuticle degradation. They also showed differential changes in cell wall integrity and multiple stress responses. These findings unveil opposite roles for Pil1A and Pil1B in autophagic regulation and an essentiality of both for cell integrity, function and pathogenicity of the fungal entomopathogen.</div>
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<Abstract><AbstractText>Pil1A and Pil1B are two core eisosome proteins that are homologous to yeast Pil1/Lsp1 or filamentous fungal Pil1A/Pil1B but have been unexplored in entomopathogenic fungi. Here we examined subcellular localization and functions of Pil1A and Pil1B in Beauveria bassiana, a fungal insect pathogen. Either localization or co-localization experiments of the two proteins demonstrated that Pil1A and Pil1B were simultaneously localized at the periphery of hyphal cells for formation of stable, punctuate spots in B. bassiana. This is different from a reliance of proper Lsp1/Pil1B localization upon Pil1/Pil1A in other fungi. Deletions of pil1A and pil1B caused opposite changes in expression of many autophagy-related genes and formation of intravacuolar autophagosomes. Such opposite changes were restored to nearly normal status by exogenous rapamycin, implicating a link of Pil1A/B to the target of rapamycin signalling pathway. All single/double deletion mutants of pil1A and pil1B lost almost all pathogenicity due to reduced ability to secrete Pr1 proteases for cuticle degradation. They also showed differential changes in cell wall integrity and multiple stress responses. These findings unveil opposite roles for Pil1A and Pil1B in autophagic regulation and an essentiality of both for cell integrity, function and pathogenicity of the fungal entomopathogen.</AbstractText>
<CopyrightInformation>© 2017 Society for Applied Microbiology and John Wiley & Sons Ltd.</CopyrightInformation>
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