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LysM Receptor-Like Kinase LYK9 of Pisum Sativum L. May Regulate Plant Responses to Chitooligosaccharides Differing in Structure
This study focused on the interactions of pea (Pisum sativum L.) plants with phytopathogenic and beneficial fungi. Here, we examined whether the lysin-motif (LysM) receptor-like kinase PsLYK9 is directly involved in the perception of long- and short-chain chitooligosaccharides (COs) released after h...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7828211/ https://www.ncbi.nlm.nih.gov/pubmed/33445801 http://dx.doi.org/10.3390/ijms22020711 |
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author | Leppyanen, Irina V. Pavlova, Olga A. Vashurina, Maria A. Bovin, Andrey D. Dolgikh, Alexandra V. Shtark, Oksana Y. Sendersky, Igor V. Dolgikh, Vyacheslav V. Tikhonovich, Igor A. Dolgikh, Elena A. |
author_facet | Leppyanen, Irina V. Pavlova, Olga A. Vashurina, Maria A. Bovin, Andrey D. Dolgikh, Alexandra V. Shtark, Oksana Y. Sendersky, Igor V. Dolgikh, Vyacheslav V. Tikhonovich, Igor A. Dolgikh, Elena A. |
author_sort | Leppyanen, Irina V. |
collection | PubMed |
description | This study focused on the interactions of pea (Pisum sativum L.) plants with phytopathogenic and beneficial fungi. Here, we examined whether the lysin-motif (LysM) receptor-like kinase PsLYK9 is directly involved in the perception of long- and short-chain chitooligosaccharides (COs) released after hydrolysis of the cell walls of phytopathogenic fungi and identified in arbuscular mycorrhizal (AM) fungal exudates. The identification and analysis of pea mutants impaired in the lyk9 gene confirmed the involvement of PsLYK9 in symbiosis development with AM fungi. Additionally, PsLYK9 regulated the immune response and resistance to phytopathogenic fungi, suggesting its bifunctional role. The existence of co-receptors may provide explanations for the potential dual role of PsLYK9 in the regulation of interactions with pathogenic and AM fungi. Co-immunoprecipitation assay revealed that PsLYK9 and two proposed co-receptors, PsLYR4 and PsLYR3, can form complexes. Analysis of binding capacity showed that PsLYK9 and PsLYR4, synthesized as extracellular domains in insect cells, were able to bind the deacetylated (DA) oligomers CO5-DA–CO8-DA. Our results suggest that the receptor complex consisting of PsLYK9 and PsLYR4 can trigger a signal pathway that stimulates the immune response in peas. However, PsLYR3 seems not to be involved in the perception of CO4-5, as a possible co-receptor of PsLYK9. |
format | Online Article Text |
id | pubmed-7828211 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-78282112021-01-25 LysM Receptor-Like Kinase LYK9 of Pisum Sativum L. May Regulate Plant Responses to Chitooligosaccharides Differing in Structure Leppyanen, Irina V. Pavlova, Olga A. Vashurina, Maria A. Bovin, Andrey D. Dolgikh, Alexandra V. Shtark, Oksana Y. Sendersky, Igor V. Dolgikh, Vyacheslav V. Tikhonovich, Igor A. Dolgikh, Elena A. Int J Mol Sci Article This study focused on the interactions of pea (Pisum sativum L.) plants with phytopathogenic and beneficial fungi. Here, we examined whether the lysin-motif (LysM) receptor-like kinase PsLYK9 is directly involved in the perception of long- and short-chain chitooligosaccharides (COs) released after hydrolysis of the cell walls of phytopathogenic fungi and identified in arbuscular mycorrhizal (AM) fungal exudates. The identification and analysis of pea mutants impaired in the lyk9 gene confirmed the involvement of PsLYK9 in symbiosis development with AM fungi. Additionally, PsLYK9 regulated the immune response and resistance to phytopathogenic fungi, suggesting its bifunctional role. The existence of co-receptors may provide explanations for the potential dual role of PsLYK9 in the regulation of interactions with pathogenic and AM fungi. Co-immunoprecipitation assay revealed that PsLYK9 and two proposed co-receptors, PsLYR4 and PsLYR3, can form complexes. Analysis of binding capacity showed that PsLYK9 and PsLYR4, synthesized as extracellular domains in insect cells, were able to bind the deacetylated (DA) oligomers CO5-DA–CO8-DA. Our results suggest that the receptor complex consisting of PsLYK9 and PsLYR4 can trigger a signal pathway that stimulates the immune response in peas. However, PsLYR3 seems not to be involved in the perception of CO4-5, as a possible co-receptor of PsLYK9. MDPI 2021-01-12 /pmc/articles/PMC7828211/ /pubmed/33445801 http://dx.doi.org/10.3390/ijms22020711 Text en © 2021 by the authors. 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 (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Leppyanen, Irina V. Pavlova, Olga A. Vashurina, Maria A. Bovin, Andrey D. Dolgikh, Alexandra V. Shtark, Oksana Y. Sendersky, Igor V. Dolgikh, Vyacheslav V. Tikhonovich, Igor A. Dolgikh, Elena A. LysM Receptor-Like Kinase LYK9 of Pisum Sativum L. May Regulate Plant Responses to Chitooligosaccharides Differing in Structure |
title | LysM Receptor-Like Kinase LYK9 of Pisum Sativum L. May Regulate Plant Responses to Chitooligosaccharides Differing in Structure |
title_full | LysM Receptor-Like Kinase LYK9 of Pisum Sativum L. May Regulate Plant Responses to Chitooligosaccharides Differing in Structure |
title_fullStr | LysM Receptor-Like Kinase LYK9 of Pisum Sativum L. May Regulate Plant Responses to Chitooligosaccharides Differing in Structure |
title_full_unstemmed | LysM Receptor-Like Kinase LYK9 of Pisum Sativum L. May Regulate Plant Responses to Chitooligosaccharides Differing in Structure |
title_short | LysM Receptor-Like Kinase LYK9 of Pisum Sativum L. May Regulate Plant Responses to Chitooligosaccharides Differing in Structure |
title_sort | lysm receptor-like kinase lyk9 of pisum sativum l. may regulate plant responses to chitooligosaccharides differing in structure |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7828211/ https://www.ncbi.nlm.nih.gov/pubmed/33445801 http://dx.doi.org/10.3390/ijms22020711 |
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