PhytophthoraV1, Main, Exploration, bibRecord, 000909

The RxLR Motif of the Host Targeting Effector AVR3a of Phytophthora infestans Is Cleaved before Secretion.

Identifieur interne : 000909 ( Main/Exploration ); précédent : 000908; suivant : 000910

The RxLR Motif of the Host Targeting Effector AVR3a of Phytophthora infestans Is Cleaved before Secretion.

Auteurs : Stephan Wawra [Royaume-Uni] ; Franziska Trusch [Royaume-Uni] ; Anja Matena [Allemagne] ; Kostis Apostolakis [Royaume-Uni] ; Uwe Linne [Allemagne] ; Igor Zhukov [Pologne] ; Jan Stanek [Pologne] ; Wiktor Ko Mi Ski [Pologne] ; Ian Davidson [Royaume-Uni] ; Chris J. Secombes [Royaume-Uni] ; Peter Bayer [Allemagne] ; Pieter Van West [Royaume-Uni]

Source :

The Plant cell [ 1532-298X ] ; 2017.

RBID : pubmed:28522546

Descripteurs français

KwdFr :
- Motifs d'acides aminés (génétique), Motifs d'acides aminés (physiologie), Phytophthora infestans (génétique), Phytophthora infestans (métabolisme), Phytophthora infestans (pathogénicité), Protéines fongiques (composition chimique), Protéines fongiques (génétique), Protéines fongiques (métabolisme), Solanum tuberosum (microbiologie), Spectrométrie de masse (MeSH).
MESH :
- composition chimique : Protéines fongiques.
- génétique : Motifs d'acides aminés, Phytophthora infestans, Protéines fongiques.
- microbiologie : Solanum tuberosum.
- métabolisme : Phytophthora infestans, Protéines fongiques.
- pathogénicité : Phytophthora infestans.
- physiologie : Motifs d'acides aminés.
- Spectrométrie de masse.

English descriptors

KwdEn :
- Amino Acid Motifs (genetics), Amino Acid Motifs (physiology), Fungal Proteins (chemistry), Fungal Proteins (genetics), Fungal Proteins (metabolism), Mass Spectrometry (MeSH), Phytophthora infestans (genetics), Phytophthora infestans (metabolism), Phytophthora infestans (pathogenicity), Solanum tuberosum (microbiology).
MESH :
- chemical , chemistry : Fungal Proteins.
- genetics : Amino Acid Motifs, Fungal Proteins, Phytophthora infestans.
- chemical , metabolism : Fungal Proteins, Phytophthora infestans.
- microbiology : Solanum tuberosum.
- pathogenicity : Phytophthora infestans.
- physiology : Amino Acid Motifs.
- Mass Spectrometry.

Abstract

When plant-pathogenic oomycetes infect their hosts, they employ a large arsenal of effector proteins to establish a successful infection. Some effector proteins are secreted and are destined to be translocated and function inside host cells. The largest group of translocated proteins from oomycetes is the RxLR effectors, defined by their conserved N-terminal Arg-Xaa-Leu-Arg (RxLR) motif. However, the precise role of this motif in the host cell translocation process is unclear. Here, detailed biochemical studies of the RxLR effector AVR3a from the potato pathogen Phytophthora infestans are presented. Mass spectrometric analysis revealed that the RxLR sequence of native AVR3a is cleaved off prior to secretion by the pathogen and the N terminus of the mature effector was found likely to be acetylated. High-resolution NMR structure analysis of AVR3a indicates that the RxLR motif is well accessible to potential processing enzymes. Processing and modification of AVR3a is to some extent similar to events occurring with the export element (PEXEL) found in malaria effector proteins from Plasmodium falciparum These findings imply a role for the RxLR motif in the secretion of AVR3a by the pathogen, rather than a direct role in the host cell entry process itself.

DOI: 10.1105/tpc.16.00552
PubMed: 28522546
PubMed Central: PMC5502441

Affiliations:

Links toward previous steps (curation, corpus...)

to stream Main, to step Corpus: 000973
to stream Main, to step Curation: 000973

Le document en format XML

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 Is Cleaved before Secretion.</title>
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<sourceDesc><biblStruct><analytic><title xml:lang="en">The RxLR Motif of the Host Targeting Effector AVR3a of <i>Phytophthora infestans</i>
 Is Cleaved before Secretion.</title>
<author><name sortKey="Wawra, Stephan" sort="Wawra, Stephan" uniqKey="Wawra S" first="Stephan" last="Wawra">Stephan Wawra</name>
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<affiliation wicri:level="1"><nlm:affiliation>Aberdeen Oomycete Laboratory, Institute of Medical Sciences, University of Aberdeen, Foresterhill, Aberdeen AB25 2ZD, United Kingdom.</nlm:affiliation>
<country xml:lang="fr">Royaume-Uni</country>
<wicri:regionArea>Aberdeen Oomycete Laboratory, Institute of Medical Sciences, University of Aberdeen, Foresterhill, Aberdeen AB25 2ZD</wicri:regionArea>
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<author><name sortKey="Stanek, Jan" sort="Stanek, Jan" uniqKey="Stanek J" first="Jan" last="Stanek">Jan Stanek</name>
<affiliation wicri:level="1"><nlm:affiliation>Biological and Chemical Research Centre (CENT III), Faculty of Chemistry, University of Warsaw, 02-089 Warsaw, Poland.</nlm:affiliation>
<country xml:lang="fr">Pologne</country>
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<author><name sortKey="Ko Mi Ski, Wiktor" sort="Ko Mi Ski, Wiktor" uniqKey="Ko Mi Ski W" first="Wiktor" last="Ko Mi Ski">Wiktor Ko Mi Ski</name>
<affiliation wicri:level="1"><nlm:affiliation>Biological and Chemical Research Centre (CENT III), Faculty of Chemistry, University of Warsaw, 02-089 Warsaw, Poland.</nlm:affiliation>
<country xml:lang="fr">Pologne</country>
<wicri:regionArea>Biological and Chemical Research Centre (CENT III), Faculty of Chemistry, University of Warsaw, 02-089 Warsaw</wicri:regionArea>
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<author><name sortKey="Davidson, Ian" sort="Davidson, Ian" uniqKey="Davidson I" first="Ian" last="Davidson">Ian Davidson</name>
<affiliation wicri:level="1"><nlm:affiliation>Proteomics Facility, Institute of Medical Sciences, University of Aberdeen, Foresterhill, Aberdeen AB25 2ZD, United Kingdom.</nlm:affiliation>
<country xml:lang="fr">Royaume-Uni</country>
<wicri:regionArea>Proteomics Facility, Institute of Medical Sciences, University of Aberdeen, Foresterhill, Aberdeen AB25 2ZD</wicri:regionArea>
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<author><name sortKey="Secombes, Chris J" sort="Secombes, Chris J" uniqKey="Secombes C" first="Chris J" last="Secombes">Chris J. Secombes</name>
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<author><name sortKey="Bayer, Peter" sort="Bayer, Peter" uniqKey="Bayer P" first="Peter" last="Bayer">Peter Bayer</name>
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<country xml:lang="fr">Allemagne</country>
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<author><name sortKey="Van West, Pieter" sort="Van West, Pieter" uniqKey="Van West P" first="Pieter" last="Van West">Pieter Van West</name>
<affiliation wicri:level="1"><nlm:affiliation>Aberdeen Oomycete Laboratory, Institute of Medical Sciences, University of Aberdeen, Foresterhill, Aberdeen AB25 2ZD, United Kingdom p.vanwest@abdn.ac.uk.</nlm:affiliation>
<country wicri:rule="url">Royaume-Uni</country>
<wicri:regionArea>Aberdeen Oomycete Laboratory, Institute of Medical Sciences, University of Aberdeen, Foresterhill, Aberdeen AB25 2ZD</wicri:regionArea>
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<series><title level="j">The Plant cell</title>
<idno type="eISSN">1532-298X</idno>
<imprint><date when="2017" type="published">2017</date>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Motifs (genetics)</term>
<term>Amino Acid Motifs (physiology)</term>
<term>Fungal Proteins (chemistry)</term>
<term>Fungal Proteins (genetics)</term>
<term>Fungal Proteins (metabolism)</term>
<term>Mass Spectrometry (MeSH)</term>
<term>Phytophthora infestans (genetics)</term>
<term>Phytophthora infestans (metabolism)</term>
<term>Phytophthora infestans (pathogenicity)</term>
<term>Solanum tuberosum (microbiology)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Motifs d'acides aminés (génétique)</term>
<term>Motifs d'acides aminés (physiologie)</term>
<term>Phytophthora infestans (génétique)</term>
<term>Phytophthora infestans (métabolisme)</term>
<term>Phytophthora infestans (pathogénicité)</term>
<term>Protéines fongiques (composition chimique)</term>
<term>Protéines fongiques (génétique)</term>
<term>Protéines fongiques (métabolisme)</term>
<term>Solanum tuberosum (microbiologie)</term>
<term>Spectrométrie de masse (MeSH)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Fungal Proteins</term>
</keywords>
<keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Protéines fongiques</term>
</keywords>
<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Amino Acid Motifs</term>
<term>Fungal Proteins</term>
<term>Phytophthora infestans</term>
</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Motifs d'acides aminés</term>
<term>Phytophthora infestans</term>
<term>Protéines fongiques</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Fungal Proteins</term>
<term>Phytophthora infestans</term>
</keywords>
<keywords scheme="MESH" qualifier="microbiologie" xml:lang="fr"><term>Solanum tuberosum</term>
</keywords>
<keywords scheme="MESH" qualifier="microbiology" xml:lang="en"><term>Solanum tuberosum</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Phytophthora infestans</term>
<term>Protéines fongiques</term>
</keywords>
<keywords scheme="MESH" qualifier="pathogenicity" xml:lang="en"><term>Phytophthora infestans</term>
</keywords>
<keywords scheme="MESH" qualifier="pathogénicité" xml:lang="fr"><term>Phytophthora infestans</term>
</keywords>
<keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Motifs d'acides aminés</term>
</keywords>
<keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Amino Acid Motifs</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Mass Spectrometry</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Spectrométrie de masse</term>
</keywords>
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<front><div type="abstract" xml:lang="en">When plant-pathogenic oomycetes infect their hosts, they employ a large arsenal of effector proteins to establish a successful infection. Some effector proteins are secreted and are destined to be translocated and function inside host cells. The largest group of translocated proteins from oomycetes is the RxLR effectors, defined by their conserved N-terminal Arg-Xaa-Leu-Arg (RxLR) motif. However, the precise role of this motif in the host cell translocation process is unclear. Here, detailed biochemical studies of the RxLR effector AVR3a from the potato pathogen <i>Phytophthora infestans</i>
 are presented. Mass spectrometric analysis revealed that the RxLR sequence of native AVR3a is cleaved off prior to secretion by the pathogen and the N terminus of the mature effector was found likely to be acetylated. High-resolution NMR structure analysis of AVR3a indicates that the RxLR motif is well accessible to potential processing enzymes. Processing and modification of AVR3a is to some extent similar to events occurring with the export element (PEXEL) found in malaria effector proteins from <i>Plasmodium falciparum</i>
 These findings imply a role for the RxLR motif in the secretion of AVR3a by the pathogen, rather than a direct role in the host cell entry process itself.</div>
</front>
</TEI>
<pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">28522546</PMID>
<DateCompleted><Year>2017</Year>
<Month>12</Month>
<Day>29</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>29</Volume>
<Issue>6</Issue>
<PubDate><Year>2017</Year>
<Month>Jun</Month>
</PubDate>
</JournalIssue>
<Title>The Plant cell</Title>
<ISOAbbreviation>Plant Cell</ISOAbbreviation>
</Journal>
<ArticleTitle>The RxLR Motif of the Host Targeting Effector AVR3a of <i>Phytophthora infestans</i>
 Is Cleaved before Secretion.</ArticleTitle>
<Pagination><MedlinePgn>1184-1195</MedlinePgn>
</Pagination>
<ELocationID EIdType="doi" ValidYN="Y">10.1105/tpc.16.00552</ELocationID>
<Abstract><AbstractText>When plant-pathogenic oomycetes infect their hosts, they employ a large arsenal of effector proteins to establish a successful infection. Some effector proteins are secreted and are destined to be translocated and function inside host cells. The largest group of translocated proteins from oomycetes is the RxLR effectors, defined by their conserved N-terminal Arg-Xaa-Leu-Arg (RxLR) motif. However, the precise role of this motif in the host cell translocation process is unclear. Here, detailed biochemical studies of the RxLR effector AVR3a from the potato pathogen <i>Phytophthora infestans</i>
 are presented. Mass spectrometric analysis revealed that the RxLR sequence of native AVR3a is cleaved off prior to secretion by the pathogen and the N terminus of the mature effector was found likely to be acetylated. High-resolution NMR structure analysis of AVR3a indicates that the RxLR motif is well accessible to potential processing enzymes. Processing and modification of AVR3a is to some extent similar to events occurring with the export element (PEXEL) found in malaria effector proteins from <i>Plasmodium falciparum</i>
 These findings imply a role for the RxLR motif in the secretion of AVR3a by the pathogen, rather than a direct role in the host cell entry process itself.</AbstractText>
<CopyrightInformation>© 2017 American Society of Plant Biologists. All rights reserved.</CopyrightInformation>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Wawra</LastName>
<ForeName>Stephan</ForeName>
<Initials>S</Initials>
<AffiliationInfo><Affiliation>Aberdeen Oomycete Laboratory, Institute of Medical Sciences, University of Aberdeen, Foresterhill, Aberdeen AB25 2ZD, United Kingdom.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Trusch</LastName>
<ForeName>Franziska</ForeName>
<Initials>F</Initials>
<Identifier Source="ORCID">http://orcid.org/0000-0003-0608-202X</Identifier>
<AffiliationInfo><Affiliation>Aberdeen Oomycete Laboratory, Institute of Medical Sciences, University of Aberdeen, Foresterhill, Aberdeen AB25 2ZD, United Kingdom.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Matena</LastName>
<ForeName>Anja</ForeName>
<Initials>A</Initials>
<AffiliationInfo><Affiliation>Structural and Medicinal Biochemistry, Centre of Medicinal Biotechnology, University of Duisburg-Essen, 45141 Essen, Germany.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Apostolakis</LastName>
<ForeName>Kostis</ForeName>
<Initials>K</Initials>
<AffiliationInfo><Affiliation>Aberdeen Oomycete Laboratory, Institute of Medical Sciences, University of Aberdeen, Foresterhill, Aberdeen AB25 2ZD, United Kingdom.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Linne</LastName>
<ForeName>Uwe</ForeName>
<Initials>U</Initials>
<AffiliationInfo><Affiliation>Core Facility for Mass Spectrometry and Chemistry, Philipps-Universität Marburg, D-35032 Marburg, Germany.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Zhukov</LastName>
<ForeName>Igor</ForeName>
<Initials>I</Initials>
<Identifier Source="ORCID">http://orcid.org/0000-0002-9912-1018</Identifier>
<AffiliationInfo><Affiliation>Institute of Biochemistry and Biophysics, Polish Academy of Sciences, 02-106 Warsaw, Poland.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>NanoBioMedical Centre, Adam Mickiewicz University, 61-614 Poznań, Poland.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Stanek</LastName>
<ForeName>Jan</ForeName>
<Initials>J</Initials>
<Identifier Source="ORCID">http://orcid.org/0000-0003-1660-168X</Identifier>
<AffiliationInfo><Affiliation>Biological and Chemical Research Centre (CENT III), Faculty of Chemistry, University of Warsaw, 02-089 Warsaw, Poland.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Koźmiński</LastName>
<ForeName>Wiktor</ForeName>
<Initials>W</Initials>
<Identifier Source="ORCID">http://orcid.org/0000-0003-2319-4525</Identifier>
<AffiliationInfo><Affiliation>Biological and Chemical Research Centre (CENT III), Faculty of Chemistry, University of Warsaw, 02-089 Warsaw, Poland.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Davidson</LastName>
<ForeName>Ian</ForeName>
<Initials>I</Initials>
<AffiliationInfo><Affiliation>Proteomics Facility, Institute of Medical Sciences, University of Aberdeen, Foresterhill, Aberdeen AB25 2ZD, United Kingdom.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Secombes</LastName>
<ForeName>Chris J</ForeName>
<Initials>CJ</Initials>
<Identifier Source="ORCID">http://orcid.org/0000-0001-8781-176X</Identifier>
<AffiliationInfo><Affiliation>Scottish Fish Immunology Research Centre, Institute of Biological and Environmental Sciences, University of Aberdeen, Aberdeen AB24 2TZ, United Kingdom.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Bayer</LastName>
<ForeName>Peter</ForeName>
<Initials>P</Initials>
<Identifier Source="ORCID">http://orcid.org/0000-0003-0435-7202</Identifier>
<AffiliationInfo><Affiliation>Structural and Medicinal Biochemistry, Centre of Medicinal Biotechnology, University of Duisburg-Essen, 45141 Essen, Germany.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>van West</LastName>
<ForeName>Pieter</ForeName>
<Initials>P</Initials>
<Identifier Source="ORCID">http://orcid.org/0000-0002-0767-6017</Identifier>
<AffiliationInfo><Affiliation>Aberdeen Oomycete Laboratory, Institute of Medical Sciences, University of Aberdeen, Foresterhill, Aberdeen AB25 2ZD, United Kingdom p.vanwest@abdn.ac.uk.</Affiliation>
</AffiliationInfo>
</Author>
</AuthorList>
<Language>eng</Language>
<GrantList CompleteYN="Y"><Grant><GrantID>BB/G012075/1</GrantID>
<Agency>Biotechnology and Biological Sciences Research Council</Agency>
<Country>United Kingdom</Country>
</Grant>
</GrantList>
<PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType>
</PublicationTypeList>
<ArticleDate DateType="Electronic"><Year>2017</Year>
<Month>05</Month>
<Day>18</Day>
</ArticleDate>
</Article>
<MedlineJournalInfo><Country>United States</Country>
<MedlineTA>Plant Cell</MedlineTA>
<NlmUniqueID>9208688</NlmUniqueID>
<ISSNLinking>1040-4651</ISSNLinking>
</MedlineJournalInfo>
<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D005656">Fungal Proteins</NameOfSubstance>
</Chemical>
</ChemicalList>
<CitationSubset>IM</CitationSubset>
<CommentsCorrectionsList><CommentsCorrections RefType="CommentIn"><RefSource>Plant Cell. 2017 Jun;29(6):1177-1178</RefSource>
<PMID Version="1">28600391</PMID>
</CommentsCorrections>
</CommentsCorrectionsList>
<MeshHeadingList><MeshHeading><DescriptorName UI="D020816" MajorTopicYN="N">Amino Acid Motifs</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D005656" MajorTopicYN="N">Fungal Proteins</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D013058" MajorTopicYN="N">Mass Spectrometry</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D055750" MajorTopicYN="N">Phytophthora infestans</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
<QualifierName UI="Q000472" MajorTopicYN="Y">pathogenicity</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D011198" MajorTopicYN="N">Solanum tuberosum</DescriptorName>
<QualifierName UI="Q000382" MajorTopicYN="Y">microbiology</QualifierName>
</MeshHeading>
</MeshHeadingList>
</MedlineCitation>
<PubmedData><History><PubMedPubDate PubStatus="received"><Year>2016</Year>
<Month>07</Month>
<Day>08</Day>
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<PubMedPubDate PubStatus="revised"><Year>2017</Year>
<Month>04</Month>
<Day>04</Day>
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<PubMedPubDate PubStatus="accepted"><Year>2017</Year>
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<Day>10</Day>
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<affiliations><list><country><li>Allemagne</li>
<li>Pologne</li>
<li>Royaume-Uni</li>
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<region><li>District de Giessen</li>
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<settlement><li>Marbourg</li>
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<name sortKey="Secombes, Chris J" sort="Secombes, Chris J" uniqKey="Secombes C" first="Chris J" last="Secombes">Chris J. Secombes</name>
<name sortKey="Trusch, Franziska" sort="Trusch, Franziska" uniqKey="Trusch F" first="Franziska" last="Trusch">Franziska Trusch</name>
<name sortKey="Van West, Pieter" sort="Van West, Pieter" uniqKey="Van West P" first="Pieter" last="Van West">Pieter Van West</name>
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<country name="Allemagne"><noRegion><name sortKey="Matena, Anja" sort="Matena, Anja" uniqKey="Matena A" first="Anja" last="Matena">Anja Matena</name>
</noRegion>
<name sortKey="Bayer, Peter" sort="Bayer, Peter" uniqKey="Bayer P" first="Peter" last="Bayer">Peter Bayer</name>
<name sortKey="Linne, Uwe" sort="Linne, Uwe" uniqKey="Linne U" first="Uwe" last="Linne">Uwe Linne</name>
</country>
<country name="Pologne"><noRegion><name sortKey="Zhukov, Igor" sort="Zhukov, Igor" uniqKey="Zhukov I" first="Igor" last="Zhukov">Igor Zhukov</name>
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<name sortKey="Ko Mi Ski, Wiktor" sort="Ko Mi Ski, Wiktor" uniqKey="Ko Mi Ski W" first="Wiktor" last="Ko Mi Ski">Wiktor Ko Mi Ski</name>
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   |étape=   Exploration
   |type=    RBID
   |clé=     pubmed:28522546
   |texte=   The RxLR Motif of the Host Targeting Effector AVR3a of Phytophthora infestans Is Cleaved before Secretion.
}}

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HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i   -Sk "pubmed:28522546" \
       | HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd   \
       | NlmPubMed2Wicri -a PhytophthoraV1

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Data generation: Fri Nov 20 11:20:57 2020. Site generation: Wed Mar 6 16:48:20 2024

	Serveur d'exploration Phytophthora
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Serveur d'exploration Phytophthora

The RxLR Motif of the Host Targeting Effector AVR3a of Phytophthora infestans Is Cleaved before Secretion.

The RxLR Motif of the Host Targeting Effector AVR3a of Phytophthora infestans Is Cleaved before Secretion.

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