Nontoxic Nep1-like proteins of the downy mildew pathogen Hyaloperonospora arabidopsidis: repression of necrosis-inducing activity by a surface-exposed region.
Identifieur interne : 000519 ( Main/Exploration ); précédent : 000518; suivant : 000520Nontoxic Nep1-like proteins of the downy mildew pathogen Hyaloperonospora arabidopsidis: repression of necrosis-inducing activity by a surface-exposed region.
Auteurs : Adriana Cabral [Pays-Bas] ; Stan Oome ; Nick Sander ; Isabell Küfner ; Thorsten Nürnberger ; Guido Van Den AckervekenSource :
- Molecular plant-microbe interactions : MPMI [ 0894-0282 ] ; 2012.
Descripteurs français
- KwdFr :
- ADN complémentaire (génétique), ARN messager (génétique), Alignement de séquences (MeSH), Arabidopsis (microbiologie), Chimère (MeSH), Données de séquences moléculaires (MeSH), Famille multigénique (génétique), Feuilles de plante (microbiologie), Interactions hôte-pathogène (MeSH), Maladies des plantes (microbiologie), Modèles moléculaires (MeSH), Mutation (MeSH), Oomycetes (génétique), Oomycetes (immunologie), Oomycetes (métabolisme), Phylogenèse (MeSH), Protéines (composition chimique), Protéines (génétique), Protéines (métabolisme), Régulation de l'expression des gènes végétaux (génétique), Spécificité d'espèce (MeSH), Structure tertiaire des protéines (MeSH), Séquence d'acides aminés (MeSH), Tabac (microbiologie).
- MESH :
- composition chimique : Protéines.
- génétique : ADN complémentaire, ARN messager, Famille multigénique, Oomycetes, Protéines, Régulation de l'expression des gènes végétaux.
- immunologie : Oomycetes.
- microbiologie : Arabidopsis, Feuilles de plante, Maladies des plantes, Tabac.
- métabolisme : Oomycetes, Protéines.
- Alignement de séquences, Chimère, Données de séquences moléculaires, Interactions hôte-pathogène, Modèles moléculaires, Mutation, Phylogenèse, Spécificité d'espèce, Structure tertiaire des protéines, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Arabidopsis (microbiology), Chimera (MeSH), DNA, Complementary (genetics), Gene Expression Regulation, Plant (genetics), Host-Pathogen Interactions (MeSH), Models, Molecular (MeSH), Molecular Sequence Data (MeSH), Multigene Family (genetics), Mutation (MeSH), Oomycetes (genetics), Oomycetes (immunology), Oomycetes (metabolism), Phylogeny (MeSH), Plant Diseases (microbiology), Plant Leaves (microbiology), Protein Structure, Tertiary (MeSH), Proteins (chemistry), Proteins (genetics), Proteins (metabolism), RNA, Messenger (genetics), Sequence Alignment (MeSH), Species Specificity (MeSH), Tobacco (microbiology).
- MESH :
- chemical , chemistry : Proteins.
- chemical , genetics : DNA, Complementary, Proteins, RNA, Messenger.
- genetics : Gene Expression Regulation, Plant, Multigene Family, Oomycetes.
- immunology : Oomycetes.
- metabolism : Oomycetes, Proteins.
- microbiology : Arabidopsis, Plant Diseases, Plant Leaves, Tobacco.
- Amino Acid Sequence, Chimera, Host-Pathogen Interactions, Models, Molecular, Molecular Sequence Data, Mutation, Phylogeny, Protein Structure, Tertiary, Sequence Alignment, Species Specificity.
Abstract
The genome of the downy mildew pathogen Hyaloperonospora arabidopsidis encodes necrosis and ethylene-inducing peptide 1 (Nep1)-like proteins (NLP). Although NLP are widely distributed in eukaryotic and prokaryotic plant pathogens, it was surprising to find these proteins in the obligate biotrophic oomycete H. arabidopsidis. Therefore, we analyzed the H. arabidopsidis NLP (HaNLP) family and identified 12 HaNLP genes and 15 pseudogenes. Most of the 27 genes form an H. arabidopsidis-specific cluster when compared with other oomycete NLP genes, suggesting this class of effectors has recently expanded in H. arabidopsidis. HaNLP transcripts were mainly detected during early infection stages. Agrobacterium tumefaciens-mediated transient expression and infiltration of recombinant NLP into tobacco and Arabidopsis leaves revealed that all HaNLP tested are noncytotoxic proteins. Even HaNLP3, which is most similar to necrosis-inducing NLP proteins of other oomycetes and which contains all amino acids that are critical for necrosis-inducing activity, did not induce necrosis. Chimeras constructed between HaNLP3 and the necrosis-inducing PsojNIP protein demonstrated that most of the HaNLP3 protein is functionally equivalent to PsojNIP, except for an exposed domain that prevents necrosis induction. The early expression and species-specific expansion of the HaNLP genes is suggestive of an alternative function of noncytolytic NLP proteins during biotrophic infection of plants.
DOI: 10.1094/MPMI-10-11-0269
PubMed: 22235872
Affiliations:
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Although NLP are widely distributed in eukaryotic and prokaryotic plant pathogens, it was surprising to find these proteins in the obligate biotrophic oomycete H. arabidopsidis. Therefore, we analyzed the H. arabidopsidis NLP (HaNLP) family and identified 12 HaNLP genes and 15 pseudogenes. Most of the 27 genes form an H. arabidopsidis-specific cluster when compared with other oomycete NLP genes, suggesting this class of effectors has recently expanded in H. arabidopsidis. HaNLP transcripts were mainly detected during early infection stages. Agrobacterium tumefaciens-mediated transient expression and infiltration of recombinant NLP into tobacco and Arabidopsis leaves revealed that all HaNLP tested are noncytotoxic proteins. Even HaNLP3, which is most similar to necrosis-inducing NLP proteins of other oomycetes and which contains all amino acids that are critical for necrosis-inducing activity, did not induce necrosis. Chimeras constructed between HaNLP3 and the necrosis-inducing PsojNIP protein demonstrated that most of the HaNLP3 protein is functionally equivalent to PsojNIP, except for an exposed domain that prevents necrosis induction. The early expression and species-specific expansion of the HaNLP genes is suggestive of an alternative function of noncytolytic NLP proteins during biotrophic infection of plants.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">22235872</PMID><DateCompleted><Year>2014</Year><Month>05</Month><Day>12</Day></DateCompleted><DateRevised><Year>2012</Year><Month>04</Month><Day>09</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0894-0282</ISSN><JournalIssue CitedMedium="Print"><Volume>25</Volume><Issue>5</Issue><PubDate><Year>2012</Year><Month>May</Month></PubDate></JournalIssue><Title>Molecular plant-microbe interactions : MPMI</Title><ISOAbbreviation>Mol Plant Microbe Interact</ISOAbbreviation></Journal><ArticleTitle>Nontoxic Nep1-like proteins of the downy mildew pathogen Hyaloperonospora arabidopsidis: repression of necrosis-inducing activity by a surface-exposed region.</ArticleTitle><Pagination><MedlinePgn>697-708</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1094/MPMI-10-11-0269</ELocationID><Abstract><AbstractText>The genome of the downy mildew pathogen Hyaloperonospora arabidopsidis encodes necrosis and ethylene-inducing peptide 1 (Nep1)-like proteins (NLP). Although NLP are widely distributed in eukaryotic and prokaryotic plant pathogens, it was surprising to find these proteins in the obligate biotrophic oomycete H. arabidopsidis. Therefore, we analyzed the H. arabidopsidis NLP (HaNLP) family and identified 12 HaNLP genes and 15 pseudogenes. Most of the 27 genes form an H. arabidopsidis-specific cluster when compared with other oomycete NLP genes, suggesting this class of effectors has recently expanded in H. arabidopsidis. HaNLP transcripts were mainly detected during early infection stages. Agrobacterium tumefaciens-mediated transient expression and infiltration of recombinant NLP into tobacco and Arabidopsis leaves revealed that all HaNLP tested are noncytotoxic proteins. Even HaNLP3, which is most similar to necrosis-inducing NLP proteins of other oomycetes and which contains all amino acids that are critical for necrosis-inducing activity, did not induce necrosis. Chimeras constructed between HaNLP3 and the necrosis-inducing PsojNIP protein demonstrated that most of the HaNLP3 protein is functionally equivalent to PsojNIP, except for an exposed domain that prevents necrosis induction. The early expression and species-specific expansion of the HaNLP genes is suggestive of an alternative function of noncytolytic NLP proteins during biotrophic infection of plants.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Cabral</LastName><ForeName>Adriana</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Plant-microbe interactions, Department of Biology, Utrecht University, Padualaan 8, 3508 CH Utrecht, The Netherlands.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Oome</LastName><ForeName>Stan</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Sander</LastName><ForeName>Nick</ForeName><Initials>N</Initials></Author><Author ValidYN="Y"><LastName>Küfner</LastName><ForeName>Isabell</ForeName><Initials>I</Initials></Author><Author ValidYN="Y"><LastName>Nürnberger</LastName><ForeName>Thorsten</ForeName><Initials>T</Initials></Author><Author ValidYN="Y"><LastName>Van den 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PubStatus="entrez"><Year>2012</Year><Month>1</Month><Day>13</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2012</Year><Month>1</Month><Day>13</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2014</Year><Month>5</Month><Day>13</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">22235872</ArticleId><ArticleId IdType="doi">10.1094/MPMI-10-11-0269</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Pays-Bas</li></country><region><li>Utrecht (province)</li></region><settlement><li>Utrecht</li></settlement><orgName><li>Université d'Utrecht</li></orgName></list><tree><noCountry><name sortKey="Kufner, Isabell" sort="Kufner, Isabell" uniqKey="Kufner I" first="Isabell" last="Küfner">Isabell Küfner</name><name sortKey="Nurnberger, Thorsten" sort="Nurnberger, Thorsten" uniqKey="Nurnberger T" first="Thorsten" last="Nürnberger">Thorsten Nürnberger</name><name sortKey="Oome, Stan" sort="Oome, Stan" uniqKey="Oome S" first="Stan" last="Oome">Stan Oome</name><name sortKey="Sander, Nick" sort="Sander, Nick" uniqKey="Sander N" first="Nick" last="Sander">Nick Sander</name><name sortKey="Van Den Ackerveken, Guido" sort="Van Den Ackerveken, Guido" uniqKey="Van Den Ackerveken G" first="Guido" last="Van Den Ackerveken">Guido Van Den Ackerveken</name></noCountry><country name="Pays-Bas"><region name="Utrecht (province)"><name sortKey="Cabral, Adriana" sort="Cabral, Adriana" uniqKey="Cabral A" first="Adriana" last="Cabral">Adriana Cabral</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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