Internalization of flax rust avirulence proteins into flax and tobacco cells can occur in the absence of the pathogen.
Identifieur interne : 000118 ( Main/Exploration ); précédent : 000117; suivant : 000119Internalization of flax rust avirulence proteins into flax and tobacco cells can occur in the absence of the pathogen.
Auteurs : Maryam Rafiqi [Australie] ; Pamela H P. Gan ; Michael Ravensdale ; Gregory J. Lawrence ; Jeffrey G. Ellis ; David A. Jones ; Adrienne R. Hardham ; Peter N. DoddsSource :
- The Plant cell [ 1532-298X ] ; 2010.
Descripteurs français
- KwdFr :
- Basidiomycota (pathogénicité), Cytoplasme (métabolisme), Données de séquences moléculaires (MeSH), Lin (immunologie), Lin (microbiologie), Maladies des plantes (microbiologie), Protéines fongiques (génétique), Protéines fongiques (métabolisme), Signaux de triage des protéines (MeSH), Séquence d'acides aminés (MeSH), Tabac (immunologie), Tabac (microbiologie), Transport des protéines (MeSH).
- MESH :
- génétique : Protéines fongiques.
- immunologie : Lin, Tabac.
- microbiologie : Lin, Maladies des plantes, Tabac.
- métabolisme : Cytoplasme, Protéines fongiques.
- pathogénicité : Basidiomycota.
- Données de séquences moléculaires, Signaux de triage des protéines, Séquence d'acides aminés, Transport des protéines.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Basidiomycota (pathogenicity), Cytoplasm (metabolism), Flax (immunology), Flax (microbiology), Fungal Proteins (genetics), Fungal Proteins (metabolism), Molecular Sequence Data (MeSH), Plant Diseases (microbiology), Protein Sorting Signals (MeSH), Protein Transport (MeSH), Tobacco (immunology), Tobacco (microbiology).
- MESH :
- chemical , genetics : Fungal Proteins.
- immunology : Flax, Tobacco.
- metabolism : Cytoplasm, Fungal Proteins.
- microbiology : Flax, Plant Diseases, Tobacco.
- pathogenicity : Basidiomycota.
- Amino Acid Sequence, Molecular Sequence Data, Protein Sorting Signals, Protein Transport.
Abstract
Translocation of pathogen effector proteins into the host cell cytoplasm is a key determinant for the pathogenicity of many bacterial and oomycete plant pathogens. A number of secreted fungal avirulence (Avr) proteins are also inferred to be delivered into host cells, based on their intracellular recognition by host resistance proteins, including those of flax rust (Melampsora lini). Here, we show by immunolocalization that the flax rust AvrM protein is secreted from haustoria during infection and accumulates in the haustorial wall. Five days after inoculation, the AvrM protein was also detected within the cytoplasm of a proportion of plant cells containing haustoria, confirming its delivery into host cells during infection. Transient expression of secreted AvrL567 and AvrM proteins fused to cerulean fluorescent protein in tobacco (Nicotiana tabacum) and flax cells resulted in intracellular accumulation of the fusion proteins. The rust Avr protein signal peptides were functional in plants and efficiently directed fused cerulean into the secretory pathway. Thus, these secreted effectors are internalized into the plant cell cytosol in the absence of the pathogen, suggesting that they do not require a pathogen-encoded transport mechanism. Uptake of these proteins is dependent on signals in their N-terminal regions, but the primary sequence features of these uptake regions are not conserved between different rust effectors.
DOI: 10.1105/tpc.109.072983
PubMed: 20525849
PubMed Central: PMC2910983
Affiliations:
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Le document en format XML
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A number of secreted fungal avirulence (Avr) proteins are also inferred to be delivered into host cells, based on their intracellular recognition by host resistance proteins, including those of flax rust (Melampsora lini). Here, we show by immunolocalization that the flax rust AvrM protein is secreted from haustoria during infection and accumulates in the haustorial wall. Five days after inoculation, the AvrM protein was also detected within the cytoplasm of a proportion of plant cells containing haustoria, confirming its delivery into host cells during infection. Transient expression of secreted AvrL567 and AvrM proteins fused to cerulean fluorescent protein in tobacco (Nicotiana tabacum) and flax cells resulted in intracellular accumulation of the fusion proteins. The rust Avr protein signal peptides were functional in plants and efficiently directed fused cerulean into the secretory pathway. Thus, these secreted effectors are internalized into the plant cell cytosol in the absence of the pathogen, suggesting that they do not require a pathogen-encoded transport mechanism. Uptake of these proteins is dependent on signals in their N-terminal regions, but the primary sequence features of these uptake regions are not conserved between different rust effectors.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">20525849</PMID><DateCompleted><Year>2010</Year><Month>10</Month><Day>18</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1532-298X</ISSN><JournalIssue CitedMedium="Internet"><Volume>22</Volume><Issue>6</Issue><PubDate><Year>2010</Year><Month>Jun</Month></PubDate></JournalIssue><Title>The Plant cell</Title><ISOAbbreviation>Plant Cell</ISOAbbreviation></Journal><ArticleTitle>Internalization of flax rust avirulence proteins into flax and tobacco cells can occur in the absence of the pathogen.</ArticleTitle><Pagination><MedlinePgn>2017-32</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1105/tpc.109.072983</ELocationID><Abstract><AbstractText>Translocation of pathogen effector proteins into the host cell cytoplasm is a key determinant for the pathogenicity of many bacterial and oomycete plant pathogens. A number of secreted fungal avirulence (Avr) proteins are also inferred to be delivered into host cells, based on their intracellular recognition by host resistance proteins, including those of flax rust (Melampsora lini). Here, we show by immunolocalization that the flax rust AvrM protein is secreted from haustoria during infection and accumulates in the haustorial wall. Five days after inoculation, the AvrM protein was also detected within the cytoplasm of a proportion of plant cells containing haustoria, confirming its delivery into host cells during infection. Transient expression of secreted AvrL567 and AvrM proteins fused to cerulean fluorescent protein in tobacco (Nicotiana tabacum) and flax cells resulted in intracellular accumulation of the fusion proteins. The rust Avr protein signal peptides were functional in plants and efficiently directed fused cerulean into the secretory pathway. Thus, these secreted effectors are internalized into the plant cell cytosol in the absence of the pathogen, suggesting that they do not require a pathogen-encoded transport mechanism. Uptake of these proteins is dependent on signals in their N-terminal regions, but the primary sequence features of these uptake regions are not conserved between different rust effectors.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Rafiqi</LastName><ForeName>Maryam</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Division of Plant Science, Research School of Biology, College of Medicine, Biology, and Environment, Australian National University, Canberra, Australian Capital Territory 0200, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Gan</LastName><ForeName>Pamela H P</ForeName><Initials>PH</Initials></Author><Author ValidYN="Y"><LastName>Ravensdale</LastName><ForeName>Michael</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Lawrence</LastName><ForeName>Gregory J</ForeName><Initials>GJ</Initials></Author><Author ValidYN="Y"><LastName>Ellis</LastName><ForeName>Jeffrey G</ForeName><Initials>JG</Initials></Author><Author ValidYN="Y"><LastName>Jones</LastName><ForeName>David A</ForeName><Initials>DA</Initials></Author><Author ValidYN="Y"><LastName>Hardham</LastName><ForeName>Adrienne R</ForeName><Initials>AR</Initials></Author><Author ValidYN="Y"><LastName>Dodds</LastName><ForeName>Peter N</ForeName><Initials>PN</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>R01 GM074265</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R01 GM074265-01A2</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>GM074265-01A2</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D052061">Research Support, N.I.H., 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sort="Dodds, Peter N" uniqKey="Dodds P" first="Peter N" last="Dodds">Peter N. Dodds</name><name sortKey="Ellis, Jeffrey G" sort="Ellis, Jeffrey G" uniqKey="Ellis J" first="Jeffrey G" last="Ellis">Jeffrey G. Ellis</name><name sortKey="Gan, Pamela H P" sort="Gan, Pamela H P" uniqKey="Gan P" first="Pamela H P" last="Gan">Pamela H P. Gan</name><name sortKey="Hardham, Adrienne R" sort="Hardham, Adrienne R" uniqKey="Hardham A" first="Adrienne R" last="Hardham">Adrienne R. Hardham</name><name sortKey="Jones, David A" sort="Jones, David A" uniqKey="Jones D" first="David A" last="Jones">David A. Jones</name><name sortKey="Lawrence, Gregory J" sort="Lawrence, Gregory J" uniqKey="Lawrence G" first="Gregory J" last="Lawrence">Gregory J. Lawrence</name><name sortKey="Ravensdale, Michael" sort="Ravensdale, Michael" uniqKey="Ravensdale M" first="Michael" last="Ravensdale">Michael Ravensdale</name></noCountry><country name="Australie"><noRegion><name sortKey="Rafiqi, Maryam" sort="Rafiqi, Maryam" uniqKey="Rafiqi M" first="Maryam" last="Rafiqi">Maryam Rafiqi</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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