LysM Receptor-Like Kinase LYK9 of <i>Pisum Sativum</i> L. May Regulate Plant Responses to Chitooligosaccharides Differing in Structure
This study focused on the interactions of pea (<i>Pisum sativum</i> L.) plants with phytopathogenic and beneficial fungi. Here, we examined whether the lysin-motif (LysM) receptor-like kinase <i>Ps</i>LYK9 is directly involved in the perception of long- and short-chain chitoo...
| Main Authors: | , , , , , , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
MDPI AG
2021-01-01
|
| Series: | International Journal of Molecular Sciences |
| Subjects: | |
| Online Access: | https://www.mdpi.com/1422-0067/22/2/711 |
| _version_ | 1797412437240053760 |
|---|---|
| author | Irina V. Leppyanen Olga A. Pavlova Maria A. Vashurina Andrey D. Bovin Alexandra V. Dolgikh Oksana Y. Shtark Igor V. Sendersky Vyacheslav V. Dolgikh Igor A. Tikhonovich Elena A. Dolgikh |
| author_facet | Irina V. Leppyanen Olga A. Pavlova Maria A. Vashurina Andrey D. Bovin Alexandra V. Dolgikh Oksana Y. Shtark Igor V. Sendersky Vyacheslav V. Dolgikh Igor A. Tikhonovich Elena A. Dolgikh |
| author_sort | Irina V. Leppyanen |
| collection | DOAJ |
| description | This study focused on the interactions of pea (<i>Pisum sativum</i> L.) plants with phytopathogenic and beneficial fungi. Here, we examined whether the lysin-motif (LysM) receptor-like kinase <i>Ps</i>LYK9 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 <i>lyk9</i> gene confirmed the involvement of <i>Ps</i>LYK9 in symbiosis development with AM fungi. Additionally, <i>Ps</i>LYK9 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 <i>Ps</i>LYK9 in the regulation of interactions with pathogenic and AM fungi. Co-immunoprecipitation assay revealed that <i>Ps</i>LYK9 and two proposed co-receptors, <i>Ps</i>LYR4 and <i>Ps</i>LYR3, can form complexes. Analysis of binding capacity showed that <i>Ps</i>LYK9 and <i>Ps</i>LYR4, 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 <i>Ps</i>LYK9 and <i>Ps</i>LYR4 can trigger a signal pathway that stimulates the immune response in peas. However, <i>Ps</i>LYR3 seems not to be involved in the perception of CO4-5, as a possible co-receptor of <i>Ps</i>LYK9. |
| first_indexed | 2024-03-09T05:02:01Z |
| format | Article |
| id | doaj.art-633e6616524f49608b8b49246c3178f6 |
| institution | Directory Open Access Journal |
| issn | 1661-6596 1422-0067 |
| language | English |
| last_indexed | 2024-03-09T05:02:01Z |
| publishDate | 2021-01-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | International Journal of Molecular Sciences |
| spelling | doaj.art-633e6616524f49608b8b49246c3178f62023-12-03T12:58:50ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672021-01-0122271110.3390/ijms22020711LysM Receptor-Like Kinase LYK9 of <i>Pisum Sativum</i> L. May Regulate Plant Responses to Chitooligosaccharides Differing in StructureIrina V. Leppyanen0Olga A. Pavlova1Maria A. Vashurina2Andrey D. Bovin3Alexandra V. Dolgikh4Oksana Y. Shtark5Igor V. Sendersky6Vyacheslav V. Dolgikh7Igor A. Tikhonovich8Elena A. Dolgikh9All-Russia Research Institute for Agricultural Microbiology, Podbelsky chausse 3, 196608 Saint Petersburg, RussiaAll-Russia Research Institute for Agricultural Microbiology, Podbelsky chausse 3, 196608 Saint Petersburg, RussiaAll-Russia Research Institute for Agricultural Microbiology, Podbelsky chausse 3, 196608 Saint Petersburg, RussiaAll-Russia Research Institute for Agricultural Microbiology, Podbelsky chausse 3, 196608 Saint Petersburg, RussiaAll-Russia Research Institute for Agricultural Microbiology, Podbelsky chausse 3, 196608 Saint Petersburg, RussiaAll-Russia Research Institute for Agricultural Microbiology, Podbelsky chausse 3, 196608 Saint Petersburg, RussiaAll-Russia Research Institute for Plant Protection, Podbelsky chausse 3, 196608 Saint Petersburg, RussiaAll-Russia Research Institute for Plant Protection, Podbelsky chausse 3, 196608 Saint Petersburg, RussiaAll-Russia Research Institute for Agricultural Microbiology, Podbelsky chausse 3, 196608 Saint Petersburg, RussiaAll-Russia Research Institute for Agricultural Microbiology, Podbelsky chausse 3, 196608 Saint Petersburg, RussiaThis study focused on the interactions of pea (<i>Pisum sativum</i> L.) plants with phytopathogenic and beneficial fungi. Here, we examined whether the lysin-motif (LysM) receptor-like kinase <i>Ps</i>LYK9 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 <i>lyk9</i> gene confirmed the involvement of <i>Ps</i>LYK9 in symbiosis development with AM fungi. Additionally, <i>Ps</i>LYK9 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 <i>Ps</i>LYK9 in the regulation of interactions with pathogenic and AM fungi. Co-immunoprecipitation assay revealed that <i>Ps</i>LYK9 and two proposed co-receptors, <i>Ps</i>LYR4 and <i>Ps</i>LYR3, can form complexes. Analysis of binding capacity showed that <i>Ps</i>LYK9 and <i>Ps</i>LYR4, 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 <i>Ps</i>LYK9 and <i>Ps</i>LYR4 can trigger a signal pathway that stimulates the immune response in peas. However, <i>Ps</i>LYR3 seems not to be involved in the perception of CO4-5, as a possible co-receptor of <i>Ps</i>LYK9.https://www.mdpi.com/1422-0067/22/2/711<i>Pisum sativum</i> L.lysin-motif receptor-like kinase <i>Ps</i>LYK9<i>lyk9</i> mutantsAM symbiosisphytopathogenic fungiheterologous synthesis |
| spellingShingle | Irina V. Leppyanen Olga A. Pavlova Maria A. Vashurina Andrey D. Bovin Alexandra V. Dolgikh Oksana Y. Shtark Igor V. Sendersky Vyacheslav V. Dolgikh Igor A. Tikhonovich Elena A. Dolgikh LysM Receptor-Like Kinase LYK9 of <i>Pisum Sativum</i> L. May Regulate Plant Responses to Chitooligosaccharides Differing in Structure International Journal of Molecular Sciences <i>Pisum sativum</i> L. lysin-motif receptor-like kinase <i>Ps</i>LYK9 <i>lyk9</i> mutants AM symbiosis phytopathogenic fungi heterologous synthesis |
| title | LysM Receptor-Like Kinase LYK9 of <i>Pisum Sativum</i> L. May Regulate Plant Responses to Chitooligosaccharides Differing in Structure |
| title_full | LysM Receptor-Like Kinase LYK9 of <i>Pisum Sativum</i> L. May Regulate Plant Responses to Chitooligosaccharides Differing in Structure |
| title_fullStr | LysM Receptor-Like Kinase LYK9 of <i>Pisum Sativum</i> L. May Regulate Plant Responses to Chitooligosaccharides Differing in Structure |
| title_full_unstemmed | LysM Receptor-Like Kinase LYK9 of <i>Pisum Sativum</i> L. May Regulate Plant Responses to Chitooligosaccharides Differing in Structure |
| title_short | LysM Receptor-Like Kinase LYK9 of <i>Pisum Sativum</i> L. May Regulate Plant Responses to Chitooligosaccharides Differing in Structure |
| title_sort | lysm receptor like kinase lyk9 of i pisum sativum i l may regulate plant responses to chitooligosaccharides differing in structure |
| topic | <i>Pisum sativum</i> L. lysin-motif receptor-like kinase <i>Ps</i>LYK9 <i>lyk9</i> mutants AM symbiosis phytopathogenic fungi heterologous synthesis |
| url | https://www.mdpi.com/1422-0067/22/2/711 |
| work_keys_str_mv | AT irinavleppyanen lysmreceptorlikekinaselyk9ofipisumsativumilmayregulateplantresponsestochitooligosaccharidesdifferinginstructure AT olgaapavlova lysmreceptorlikekinaselyk9ofipisumsativumilmayregulateplantresponsestochitooligosaccharidesdifferinginstructure AT mariaavashurina lysmreceptorlikekinaselyk9ofipisumsativumilmayregulateplantresponsestochitooligosaccharidesdifferinginstructure AT andreydbovin lysmreceptorlikekinaselyk9ofipisumsativumilmayregulateplantresponsestochitooligosaccharidesdifferinginstructure AT alexandravdolgikh lysmreceptorlikekinaselyk9ofipisumsativumilmayregulateplantresponsestochitooligosaccharidesdifferinginstructure AT oksanayshtark lysmreceptorlikekinaselyk9ofipisumsativumilmayregulateplantresponsestochitooligosaccharidesdifferinginstructure AT igorvsendersky lysmreceptorlikekinaselyk9ofipisumsativumilmayregulateplantresponsestochitooligosaccharidesdifferinginstructure AT vyacheslavvdolgikh lysmreceptorlikekinaselyk9ofipisumsativumilmayregulateplantresponsestochitooligosaccharidesdifferinginstructure AT igoratikhonovich lysmreceptorlikekinaselyk9ofipisumsativumilmayregulateplantresponsestochitooligosaccharidesdifferinginstructure AT elenaadolgikh lysmreceptorlikekinaselyk9ofipisumsativumilmayregulateplantresponsestochitooligosaccharidesdifferinginstructure |