A Cytochrome B5-Like Heme/Steroid Binding Domain Protein, PlCB5L1, Regulates Mycelial Growth, Pathogenicity and Oxidative Stress Tolerance in Peronophythora litchii

As an electron transport component, cytochrome b5 is an essential component of the Class II cytochrome P450 monooxygenation system and widely present in animals, plants, and fungi. However, the roles of Cyt-b5 domain proteins in pathogenic oomycetes remain unknown. Peronophythora litchii is an oomyc...

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Autores principales: Wen Li, Peng Li, Xiaofan Zhou, Junjian Situ, Yiming Lin, Jiahui Qiu, Yuling Yuan, Pinggen Xi, Zide Jiang, Guanghui Kong
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Publicado: Frontiers Media S.A. 2021
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spelling oai:doaj.org-article:3626293b5d2b436bbe3ff25a07d96ff12021-12-01T01:13:30ZA Cytochrome B5-Like Heme/Steroid Binding Domain Protein, PlCB5L1, Regulates Mycelial Growth, Pathogenicity and Oxidative Stress Tolerance in Peronophythora litchii1664-462X10.3389/fpls.2021.783438https://doaj.org/article/3626293b5d2b436bbe3ff25a07d96ff12021-11-01T00:00:00Zhttps://www.frontiersin.org/articles/10.3389/fpls.2021.783438/fullhttps://doaj.org/toc/1664-462XAs an electron transport component, cytochrome b5 is an essential component of the Class II cytochrome P450 monooxygenation system and widely present in animals, plants, and fungi. However, the roles of Cyt-b5 domain proteins in pathogenic oomycetes remain unknown. Peronophythora litchii is an oomycete pathogen that causes litchi downy blight, the most destructive disease of litchi. In this study, we identified a gene, designated PlCB5L1, that encodes a Cyt-b5 domain protein in P. litchii, and characterized its function. PlCB5L1 is highly expressed in the zoospores, cysts, germinated cysts, and during early stages of infection. PlCB5L1 knockout mutants showed reduced growth rate and β-sitosterol utilization. Importantly, we also found that PlCB5L1 is required for the full pathogenicity of P. litchii. Compared with the wild-type strain, the PlCB5L1 mutants exhibited significantly higher tolerance to SDS and sorbitol, but impaired tolerance to cell wall stress, osmotic stress, and oxidative stress. Further, the expression of genes involved in oxidative stress tolerance, including peroxidase, cytochrome P450, and laccase genes, were down-regulated in PlCB5L1 mutants under oxidative stress. This is the first report that a Cyt-b5 domain protein contributes to the development, stress response, and pathogenicity in plant pathogenic oomycetes.Wen LiPeng LiXiaofan ZhouXiaofan ZhouJunjian SituYiming LinJiahui QiuYuling YuanPinggen XiZide JiangGuanghui KongFrontiers Media S.A.articlePeronophythora litchiicytochrome b5-like heme/steroid binding domaingrowthpathogenicityoxidative stressPlant cultureSB1-1110ENFrontiers in Plant Science, Vol 12 (2021)
institution DOAJ
collection DOAJ
language EN
topic Peronophythora litchii
cytochrome b5-like heme/steroid binding domain
growth
pathogenicity
oxidative stress
Plant culture
SB1-1110
spellingShingle Peronophythora litchii
cytochrome b5-like heme/steroid binding domain
growth
pathogenicity
oxidative stress
Plant culture
SB1-1110
Wen Li
Peng Li
Xiaofan Zhou
Xiaofan Zhou
Junjian Situ
Yiming Lin
Jiahui Qiu
Yuling Yuan
Pinggen Xi
Zide Jiang
Guanghui Kong
A Cytochrome B5-Like Heme/Steroid Binding Domain Protein, PlCB5L1, Regulates Mycelial Growth, Pathogenicity and Oxidative Stress Tolerance in Peronophythora litchii
description As an electron transport component, cytochrome b5 is an essential component of the Class II cytochrome P450 monooxygenation system and widely present in animals, plants, and fungi. However, the roles of Cyt-b5 domain proteins in pathogenic oomycetes remain unknown. Peronophythora litchii is an oomycete pathogen that causes litchi downy blight, the most destructive disease of litchi. In this study, we identified a gene, designated PlCB5L1, that encodes a Cyt-b5 domain protein in P. litchii, and characterized its function. PlCB5L1 is highly expressed in the zoospores, cysts, germinated cysts, and during early stages of infection. PlCB5L1 knockout mutants showed reduced growth rate and β-sitosterol utilization. Importantly, we also found that PlCB5L1 is required for the full pathogenicity of P. litchii. Compared with the wild-type strain, the PlCB5L1 mutants exhibited significantly higher tolerance to SDS and sorbitol, but impaired tolerance to cell wall stress, osmotic stress, and oxidative stress. Further, the expression of genes involved in oxidative stress tolerance, including peroxidase, cytochrome P450, and laccase genes, were down-regulated in PlCB5L1 mutants under oxidative stress. This is the first report that a Cyt-b5 domain protein contributes to the development, stress response, and pathogenicity in plant pathogenic oomycetes.
format article
author Wen Li
Peng Li
Xiaofan Zhou
Xiaofan Zhou
Junjian Situ
Yiming Lin
Jiahui Qiu
Yuling Yuan
Pinggen Xi
Zide Jiang
Guanghui Kong
author_facet Wen Li
Peng Li
Xiaofan Zhou
Xiaofan Zhou
Junjian Situ
Yiming Lin
Jiahui Qiu
Yuling Yuan
Pinggen Xi
Zide Jiang
Guanghui Kong
author_sort Wen Li
title A Cytochrome B5-Like Heme/Steroid Binding Domain Protein, PlCB5L1, Regulates Mycelial Growth, Pathogenicity and Oxidative Stress Tolerance in Peronophythora litchii
title_short A Cytochrome B5-Like Heme/Steroid Binding Domain Protein, PlCB5L1, Regulates Mycelial Growth, Pathogenicity and Oxidative Stress Tolerance in Peronophythora litchii
title_full A Cytochrome B5-Like Heme/Steroid Binding Domain Protein, PlCB5L1, Regulates Mycelial Growth, Pathogenicity and Oxidative Stress Tolerance in Peronophythora litchii
title_fullStr A Cytochrome B5-Like Heme/Steroid Binding Domain Protein, PlCB5L1, Regulates Mycelial Growth, Pathogenicity and Oxidative Stress Tolerance in Peronophythora litchii
title_full_unstemmed A Cytochrome B5-Like Heme/Steroid Binding Domain Protein, PlCB5L1, Regulates Mycelial Growth, Pathogenicity and Oxidative Stress Tolerance in Peronophythora litchii
title_sort cytochrome b5-like heme/steroid binding domain protein, plcb5l1, regulates mycelial growth, pathogenicity and oxidative stress tolerance in peronophythora litchii
publisher Frontiers Media S.A.
publishDate 2021
url https://doaj.org/article/3626293b5d2b436bbe3ff25a07d96ff1
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