A LysM Domain-Containing Protein LtLysM1 Is Important for Vegetative Growth and Pathogenesis in Woody Plant Pathogen Lasiodiplodia theobromae.
Identifieur interne : 000052 ( Main/Corpus ); précédent : 000051; suivant : 000053A LysM Domain-Containing Protein LtLysM1 Is Important for Vegetative Growth and Pathogenesis in Woody Plant Pathogen Lasiodiplodia theobromae.
Auteurs : Dulanjalee Lakmali Harishchandra ; Wei Zhang ; Xinghong Li ; Kandawatte Wedaralalage Thilini Chethana ; Kevin David Hyde ; Siraprapa Brooks ; Jiye Yan ; Junbo PengSource :
- The plant pathology journal [ 1598-2254 ] ; 2020.
Abstract
Lysin motif (LysM) proteins are reported to be necessary for the virulence and immune response suppression in many herbaceous plant pathogens, while far less is documented in woody plant pathogens. In this study, we preliminarily characterized the molecular function of a LysM protein LtLysM1 in woody plant pathogen Lasiodiplodia theobromae. Transcriptional profiles revealed that LtLysM1 is highly expressed at infectious stages, especially at 36 and 48 hours post inoculation. Amino acid sequence analyses revealed that LtLysM1 was a putative glycoprotein with 10 predicted N-glycosylation sites and one LysM domain. Pathogenicity tests showed that overexpressed transformants of LtLysM1 displayed increased virulence on grapevine shoots in comparison with that of wild type CSS-01s, and RNAi transformants of LtLysM1 exhibited significantly decreased lesion length when compared with that of wild type CSS-01s. Moreover, LtLysM1 was confirmed to be a secreted protein by a yeast signal peptide trap assay. Transient expression in Nicotiana benthamiana together with protein immunoblotting confirmed that LtLysM1 was an N-glycosylated protein. In contrast to previously reported LysM protein Slp1 and OsCEBiP, LtLysM1 molecule did not interact with itself based on yeast two hybrid and co-immunoprecipitation assays. These results indicate that LtLysM1 is a secreted protein and functions as a critical virulence factor during the disease symptom development in woody plants.
DOI: 10.5423/PPJ.OA.05.2020.0084
PubMed: 32788891
PubMed Central: PMC7403516
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<front><div type="abstract" xml:lang="en">Lysin motif (LysM) proteins are reported to be necessary for the virulence and immune response suppression in many herbaceous plant pathogens, while far less is documented in woody plant pathogens. In this study, we preliminarily characterized the molecular function of a LysM protein LtLysM1 in woody plant pathogen <i>Lasiodiplodia theobromae.</i>
Transcriptional profiles revealed that LtLysM1 is highly expressed at infectious stages, especially at 36 and 48 hours post inoculation. Amino acid sequence analyses revealed that LtLysM1 was a putative glycoprotein with 10 predicted <i>N</i>
-glycosylation sites and one LysM domain. Pathogenicity tests showed that overexpressed transformants of <i>LtLysM1</i>
displayed increased virulence on grapevine shoots in comparison with that of wild type CSS-01s, and RNAi transformants of <i>LtLysM1</i>
exhibited significantly decreased lesion length when compared with that of wild type CSS-01s. Moreover, LtLysM1 was confirmed to be a secreted protein by a yeast signal peptide trap assay. Transient expression in <i>Nicotiana benthamiana</i>
together with protein immunoblotting confirmed that LtLysM1 was an <i>N</i>
-glycosylated protein. In contrast to previously reported LysM protein Slp1 and OsCEBiP, LtLysM1 molecule did not interact with itself based on yeast two hybrid and co-immunoprecipitation assays. These results indicate that LtLysM1 is a secreted protein and functions as a critical virulence factor during the disease symptom development in woody plants.</div>
</front>
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<Title>The plant pathology journal</Title>
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<ArticleTitle>A LysM Domain-Containing Protein LtLysM1 Is Important for Vegetative Growth and Pathogenesis in Woody Plant Pathogen <i>Lasiodiplodia theobromae</i>
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<Abstract><AbstractText>Lysin motif (LysM) proteins are reported to be necessary for the virulence and immune response suppression in many herbaceous plant pathogens, while far less is documented in woody plant pathogens. In this study, we preliminarily characterized the molecular function of a LysM protein LtLysM1 in woody plant pathogen <i>Lasiodiplodia theobromae.</i>
Transcriptional profiles revealed that LtLysM1 is highly expressed at infectious stages, especially at 36 and 48 hours post inoculation. Amino acid sequence analyses revealed that LtLysM1 was a putative glycoprotein with 10 predicted <i>N</i>
-glycosylation sites and one LysM domain. Pathogenicity tests showed that overexpressed transformants of <i>LtLysM1</i>
displayed increased virulence on grapevine shoots in comparison with that of wild type CSS-01s, and RNAi transformants of <i>LtLysM1</i>
exhibited significantly decreased lesion length when compared with that of wild type CSS-01s. Moreover, LtLysM1 was confirmed to be a secreted protein by a yeast signal peptide trap assay. Transient expression in <i>Nicotiana benthamiana</i>
together with protein immunoblotting confirmed that LtLysM1 was an <i>N</i>
-glycosylated protein. In contrast to previously reported LysM protein Slp1 and OsCEBiP, LtLysM1 molecule did not interact with itself based on yeast two hybrid and co-immunoprecipitation assays. These results indicate that LtLysM1 is a secreted protein and functions as a critical virulence factor during the disease symptom development in woody plants.</AbstractText>
<CopyrightInformation>© The Korean Society of Plant Pathology.</CopyrightInformation>
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<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Harishchandra</LastName>
<ForeName>Dulanjalee Lakmali</ForeName>
<Initials>DL</Initials>
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<AffiliationInfo><Affiliation>Centre of Excellence in Fungal Research, School of Science, Mae Fah Luang University, Chiang Rai 57100, Thailand.</Affiliation>
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<Author ValidYN="Y"><LastName>Yan</LastName>
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</AffiliationInfo>
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<Author ValidYN="Y"><LastName>Peng</LastName>
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<AffiliationInfo><Affiliation>Beijing Key Laboratory of Environment Friendly Management on Fruit Diseases and Pests in North China, Institute of Plant and Environment Protection, Beijing Academy of Agriculture and Forestry Sciences, Beijing 100097, China.</Affiliation>
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