Proteomic analysis upon peach fruit infection with Monilinia fructicola and M. laxa identify responses contributing to brown rot resistance.
Identifieur interne : 000152 ( Main/Curation ); précédent : 000151; suivant : 000153Proteomic analysis upon peach fruit infection with Monilinia fructicola and M. laxa identify responses contributing to brown rot resistance.
Auteurs : Antonios Papavasileiou [Grèce] ; Georgia Tanou [Grèce] ; Anastasios Samaras [Grèce] ; Martina Samiotaki [Grèce] ; Athanassios Molassiotis [Grèce] ; George Karaoglanidis [Grèce]Source :
- Scientific reports [ 2045-2322 ] ; 2020.
Abstract
Brown rot, caused by Monilinia spp., is a major peach disease worldwide. In this study, the response of peach cultivars Royal Glory (RG) and Rich Lady (RL) to infection by Monilinia fructicola or Monilinia laxa, was characterized. Phenotypic data, after artificial inoculations, revealed that 'RL' was relatively susceptible whereas 'RG' was moderately resistant to Monilinia spp. Comparative proteomic analysis identified mesocarp proteins of the 2 cultivars whose accumulation were altered by the 2 Monilinia species. Functional analysis indicated that pathogen-affected proteins in 'RG' were mainly involved in energy and metabolism, while, differentially accumulated proteins by the pathogen presence in 'RL' were involved in disease/defense and metabolism. A higher number of proteins was differentiated in 'RG' fruit compared to 'RL'. Upon Monilinia spp. infection, various proteins were-down accumulated in 'RL' fruit. Protein identification by mass spectrometric analysis revealed that several defense-related proteins including thaumatin, formate dehydrogenase, S-formylglutathione hydrolase, CBS domain-containing protein, HSP70, and glutathione S-transferase were up-accumulated in 'RG' fruit following inoculation. The expression profile of selected defense-related genes, such as major latex allergen, 1-aminocyclopropane-1-carboxylate deaminase and UDP-glycoltransferase was assessed by RT-PCR. This is the first study deciphering differential regulations of peach fruit proteome upon Monilinia infection elucidating resistance responses.
DOI: 10.1038/s41598-020-64864-x
PubMed: 32385387
PubMed Central: PMC7210933
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type="eISSN">2045-2322</idno><imprint><date when="2020" type="published">2020</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Brown rot, caused by Monilinia spp., is a major peach disease worldwide. In this study, the response of peach cultivars Royal Glory (RG) and Rich Lady (RL) to infection by Monilinia fructicola or Monilinia laxa, was characterized. Phenotypic data, after artificial inoculations, revealed that 'RL' was relatively susceptible whereas 'RG' was moderately resistant to Monilinia spp. Comparative proteomic analysis identified mesocarp proteins of the 2 cultivars whose accumulation were altered by the 2 Monilinia species. Functional analysis indicated that pathogen-affected proteins in 'RG' were mainly involved in energy and metabolism, while, differentially accumulated proteins by the pathogen presence in 'RL' were involved in disease/defense and metabolism. A higher number of proteins was differentiated in 'RG' fruit compared to 'RL'. Upon Monilinia spp. infection, various proteins were-down accumulated in 'RL' fruit. Protein identification by mass spectrometric analysis revealed that several defense-related proteins including thaumatin, formate dehydrogenase, S-formylglutathione hydrolase, CBS domain-containing protein, HSP70, and glutathione S-transferase were up-accumulated in 'RG' fruit following inoculation. The expression profile of selected defense-related genes, such as major latex allergen, 1-aminocyclopropane-1-carboxylate deaminase and UDP-glycoltransferase was assessed by RT-PCR. This is the first study deciphering differential regulations of peach fruit proteome upon Monilinia infection elucidating resistance responses.</div></front></TEI><pubmed><MedlineCitation Status="In-Process" Owner="NLM"><PMID Version="1">32385387</PMID><DateRevised><Year>2020</Year><Month>10</Month><Day>02</Day></DateRevised><Article PubModel="Electronic"><Journal><ISSN IssnType="Electronic">2045-2322</ISSN><JournalIssue CitedMedium="Internet"><Volume>10</Volume><Issue>1</Issue><PubDate><Year>2020</Year><Month>05</Month><Day>08</Day></PubDate></JournalIssue><Title>Scientific reports</Title><ISOAbbreviation>Sci Rep</ISOAbbreviation></Journal><ArticleTitle>Proteomic analysis upon peach fruit infection with Monilinia fructicola and M. laxa identify responses contributing to brown rot resistance.</ArticleTitle><Pagination><MedlinePgn>7807</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1038/s41598-020-64864-x</ELocationID><Abstract><AbstractText>Brown rot, caused by Monilinia spp., is a major peach disease worldwide. In this study, the response of peach cultivars Royal Glory (RG) and Rich Lady (RL) to infection by Monilinia fructicola or Monilinia laxa, was characterized. Phenotypic data, after artificial inoculations, revealed that 'RL' was relatively susceptible whereas 'RG' was moderately resistant to Monilinia spp. Comparative proteomic analysis identified mesocarp proteins of the 2 cultivars whose accumulation were altered by the 2 Monilinia species. Functional analysis indicated that pathogen-affected proteins in 'RG' were mainly involved in energy and metabolism, while, differentially accumulated proteins by the pathogen presence in 'RL' were involved in disease/defense and metabolism. A higher number of proteins was differentiated in 'RG' fruit compared to 'RL'. Upon Monilinia spp. infection, various proteins were-down accumulated in 'RL' fruit. Protein identification by mass spectrometric analysis revealed that several defense-related proteins including thaumatin, formate dehydrogenase, S-formylglutathione hydrolase, CBS domain-containing protein, HSP70, and glutathione S-transferase were up-accumulated in 'RG' fruit following inoculation. The expression profile of selected defense-related genes, such as major latex allergen, 1-aminocyclopropane-1-carboxylate deaminase and UDP-glycoltransferase was assessed by RT-PCR. This is the first study deciphering differential regulations of peach fruit proteome upon Monilinia infection elucidating resistance responses.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Papavasileiou</LastName><ForeName>Antonios</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Laboratory of Plant Pathology, Faculty of Agriculture, Forestry and Natural Environment, Aristotle University, POB 269, 54124, Thessaloniki, Greece.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Tanou</LastName><ForeName>Georgia</ForeName><Initials>G</Initials><AffiliationInfo><Affiliation>Institute of Soil and Water Resources, ELGO-Demeter Thermi, Thessaloniki, Greece.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Samaras</LastName><ForeName>Anastasios</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Laboratory of Plant Pathology, Faculty of Agriculture, Forestry and Natural Environment, Aristotle University, POB 269, 54124, Thessaloniki, Greece.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Samiotaki</LastName><ForeName>Martina</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Biomedical Sciences Research Center "Alexander Fleming", Vari, 16672, Greece.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Molassiotis</LastName><ForeName>Athanassios</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Laboratory of Pomology, Faculty of Agriculture, Forestry and Natural Environment, Aristotle University, 570 01, Thessaloniki-Thermi, Greece. amolasio@agro.auth.gr.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Karaoglanidis</LastName><ForeName>George</ForeName><Initials>G</Initials><AffiliationInfo><Affiliation>Laboratory of Plant Pathology, Faculty of Agriculture, Forestry and Natural Environment, Aristotle University, POB 269, 54124, Thessaloniki, Greece. 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