Phytophthora infestans effector AVR3a is essential for virulence and manipulates plant immunity by stabilizing host E3 ligase CMPG1.
Identifieur interne : 001862 ( Main/Exploration ); précédent : 001861; suivant : 001863Phytophthora infestans effector AVR3a is essential for virulence and manipulates plant immunity by stabilizing host E3 ligase CMPG1.
Auteurs : Jorunn I B. Bos [Royaume-Uni] ; Miles R. Armstrong ; Eleanor M. Gilroy ; Petra C. Boevink ; Ingo Hein ; Rosalind M. Taylor ; Tian Zhendong ; Stefan Engelhardt ; Ramesh R. Vetukuri ; Brian Harrower ; Christina Dixelius ; Glenn Bryan ; Ari Sadanandom ; Stephen C. Whisson ; Sophien Kamoun ; Paul R J. BirchSource :
- Proceedings of the National Academy of Sciences of the United States of America [ 1091-6490 ] ; 2010.
Descripteurs français
- KwdFr :
- Données de séquences moléculaires (MeSH), Interactions hôte-pathogène (MeSH), Phytophthora infestans (génétique), Phytophthora infestans (immunologie), Phytophthora infestans (métabolisme), Phytophthora infestans (pathogénicité), Protéines d'algue (génétique), Protéines d'algue (immunologie), Protéines d'algue (métabolisme), Solanum tuberosum (enzymologie), Solanum tuberosum (immunologie), Solanum tuberosum (parasitologie), Stabilité enzymatique (MeSH), Ubiquitin-protein ligases (métabolisme), Virulence (MeSH).
- MESH :
- enzymologie : Solanum tuberosum.
- génétique : Phytophthora infestans, Protéines d'algue.
- immunologie : Phytophthora infestans, Protéines d'algue, Solanum tuberosum.
- métabolisme : Phytophthora infestans, Protéines d'algue, Ubiquitin-protein ligases.
- parasitologie : Solanum tuberosum.
- pathogénicité : Phytophthora infestans.
- Données de séquences moléculaires, Interactions hôte-pathogène, Stabilité enzymatique, Virulence.
English descriptors
- KwdEn :
- Algal Proteins (genetics), Algal Proteins (immunology), Algal Proteins (metabolism), Enzyme Stability (MeSH), Host-Pathogen Interactions (MeSH), Molecular Sequence Data (MeSH), Phytophthora infestans (genetics), Phytophthora infestans (immunology), Phytophthora infestans (metabolism), Phytophthora infestans (pathogenicity), Solanum tuberosum (enzymology), Solanum tuberosum (immunology), Solanum tuberosum (parasitology), Ubiquitin-Protein Ligases (metabolism), Virulence (MeSH).
- MESH :
- chemical , genetics : Algal Proteins.
- chemical , immunology : Algal Proteins.
- chemical , metabolism : Algal Proteins, Ubiquitin-Protein Ligases.
- enzymology : Solanum tuberosum.
- genetics : Phytophthora infestans.
- immunology : Phytophthora infestans, Solanum tuberosum.
- metabolism : Phytophthora infestans.
- parasitology : Solanum tuberosum.
- pathogenicity : Phytophthora infestans.
- Enzyme Stability, Host-Pathogen Interactions, Molecular Sequence Data, Virulence.
Abstract
Fungal and oomycete plant pathogens translocate effector proteins into host cells to establish infection. However, virulence targets and modes of action of their effectors are unknown. Effector AVR3a from potato blight pathogen Phytophthora infestans is translocated into host cells and occurs in two forms: AVR3a(KI), which is detected by potato resistance protein R3a, strongly suppresses infestin 1 (INF1)-triggered cell death (ICD), whereas AVR3a(EM), which evades recognition by R3a, weakly suppresses host ICD. Here we show that AVR3a interacts with and stabilizes host U-box E3 ligase CMPG1, which is required for ICD. In contrast, AVR3a(KI/Y147del), a mutant with a deleted C-terminal tyrosine residue that fails to suppress ICD, cannot interact with or stabilize CMPG1. CMPG1 is stabilized by the inhibitors MG132 and epoxomicin, indicating that it is degraded by the 26S proteasome. CMPG1 is degraded during ICD. However, it is stabilized by mutations in the U-box that prevent its E3 ligase activity. In stabilizing CMPG1, AVR3a thus modifies its normal activity. Remarkably, given the potential for hundreds of effector genes in the P. infestans genome, silencing Avr3a compromises P. infestans pathogenicity, suggesting that AVR3a is essential for virulence. Interestingly, Avr3a silencing can be complemented by in planta expression of Avr3a(KI) or Avr3a(EM) but not the Avr3a(KI/Y147del) mutant. Our data provide genetic evidence that AVR3a is an essential virulence factor that targets and stabilizes the plant E3 ligase CMPG1, potentially to prevent host cell death during the biotrophic phase of infection.
DOI: 10.1073/pnas.0914408107
PubMed: 20457921
PubMed Central: PMC2906857
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Bos</name><affiliation wicri:level="1"><nlm:affiliation>The Sainsbury Laboratory, John Innes Centre, Colney, Norwich NR4 7UH, UK.</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>The Sainsbury Laboratory, John Innes Centre, Colney, Norwich NR4 7UH</wicri:regionArea><wicri:noRegion>Norwich NR4 7UH</wicri:noRegion></affiliation></author><author><name sortKey="Armstrong, Miles R" sort="Armstrong, Miles R" uniqKey="Armstrong M" first="Miles R" last="Armstrong">Miles R. Armstrong</name></author><author><name sortKey="Gilroy, Eleanor M" sort="Gilroy, Eleanor M" uniqKey="Gilroy E" first="Eleanor M" last="Gilroy">Eleanor M. Gilroy</name></author><author><name sortKey="Boevink, Petra C" sort="Boevink, Petra C" uniqKey="Boevink P" first="Petra C" last="Boevink">Petra C. 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Birch</name></author></analytic><series><title level="j">Proceedings of the National Academy of Sciences of the United States of America</title><idno type="eISSN">1091-6490</idno><imprint><date when="2010" type="published">2010</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Algal Proteins (genetics)</term><term>Algal Proteins (immunology)</term><term>Algal Proteins (metabolism)</term><term>Enzyme Stability (MeSH)</term><term>Host-Pathogen Interactions (MeSH)</term><term>Molecular Sequence Data (MeSH)</term><term>Phytophthora infestans (genetics)</term><term>Phytophthora infestans (immunology)</term><term>Phytophthora infestans (metabolism)</term><term>Phytophthora infestans (pathogenicity)</term><term>Solanum tuberosum (enzymology)</term><term>Solanum tuberosum (immunology)</term><term>Solanum tuberosum (parasitology)</term><term>Ubiquitin-Protein Ligases (metabolism)</term><term>Virulence (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Données de séquences moléculaires (MeSH)</term><term>Interactions hôte-pathogène (MeSH)</term><term>Phytophthora infestans (génétique)</term><term>Phytophthora infestans (immunologie)</term><term>Phytophthora infestans (métabolisme)</term><term>Phytophthora infestans (pathogénicité)</term><term>Protéines d'algue (génétique)</term><term>Protéines d'algue (immunologie)</term><term>Protéines d'algue (métabolisme)</term><term>Solanum tuberosum (enzymologie)</term><term>Solanum tuberosum (immunologie)</term><term>Solanum tuberosum (parasitologie)</term><term>Stabilité enzymatique (MeSH)</term><term>Ubiquitin-protein ligases (métabolisme)</term><term>Virulence (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Algal Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="immunology" xml:lang="en"><term>Algal Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Algal Proteins</term><term>Ubiquitin-Protein Ligases</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Solanum tuberosum</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Solanum tuberosum</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Phytophthora infestans</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Phytophthora infestans</term><term>Protéines d'algue</term></keywords><keywords scheme="MESH" qualifier="immunologie" xml:lang="fr"><term>Phytophthora infestans</term><term>Protéines d'algue</term><term>Solanum tuberosum</term></keywords><keywords scheme="MESH" qualifier="immunology" xml:lang="en"><term>Phytophthora infestans</term><term>Solanum tuberosum</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Phytophthora infestans</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Phytophthora infestans</term><term>Protéines d'algue</term><term>Ubiquitin-protein ligases</term></keywords><keywords scheme="MESH" qualifier="parasitologie" xml:lang="fr"><term>Solanum tuberosum</term></keywords><keywords scheme="MESH" qualifier="parasitology" xml:lang="en"><term>Solanum tuberosum</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" xml:lang="en"><term>Enzyme Stability</term><term>Host-Pathogen Interactions</term><term>Molecular Sequence Data</term><term>Virulence</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Données de séquences moléculaires</term><term>Interactions hôte-pathogène</term><term>Stabilité enzymatique</term><term>Virulence</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Fungal and oomycete plant pathogens translocate effector proteins into host cells to establish infection. However, virulence targets and modes of action of their effectors are unknown. Effector AVR3a from potato blight pathogen Phytophthora infestans is translocated into host cells and occurs in two forms: AVR3a(KI), which is detected by potato resistance protein R3a, strongly suppresses infestin 1 (INF1)-triggered cell death (ICD), whereas AVR3a(EM), which evades recognition by R3a, weakly suppresses host ICD. Here we show that AVR3a interacts with and stabilizes host U-box E3 ligase CMPG1, which is required for ICD. In contrast, AVR3a(KI/Y147del), a mutant with a deleted C-terminal tyrosine residue that fails to suppress ICD, cannot interact with or stabilize CMPG1. CMPG1 is stabilized by the inhibitors MG132 and epoxomicin, indicating that it is degraded by the 26S proteasome. CMPG1 is degraded during ICD. However, it is stabilized by mutations in the U-box that prevent its E3 ligase activity. In stabilizing CMPG1, AVR3a thus modifies its normal activity. Remarkably, given the potential for hundreds of effector genes in the P. infestans genome, silencing Avr3a compromises P. infestans pathogenicity, suggesting that AVR3a is essential for virulence. Interestingly, Avr3a silencing can be complemented by in planta expression of Avr3a(KI) or Avr3a(EM) but not the Avr3a(KI/Y147del) mutant. Our data provide genetic evidence that AVR3a is an essential virulence factor that targets and stabilizes the plant E3 ligase CMPG1, potentially to prevent host cell death during the biotrophic phase of infection.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">20457921</PMID><DateCompleted><Year>2010</Year><Month>06</Month><Day>29</Day></DateCompleted><DateRevised><Year>2019</Year><Month>10</Month><Day>08</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1091-6490</ISSN><JournalIssue CitedMedium="Internet"><Volume>107</Volume><Issue>21</Issue><PubDate><Year>2010</Year><Month>May</Month><Day>25</Day></PubDate></JournalIssue><Title>Proceedings of the National Academy of Sciences of the United States of America</Title><ISOAbbreviation>Proc Natl Acad Sci U S A</ISOAbbreviation></Journal><ArticleTitle>Phytophthora infestans effector AVR3a is essential for virulence and manipulates plant immunity by stabilizing host E3 ligase CMPG1.</ArticleTitle><Pagination><MedlinePgn>9909-14</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1073/pnas.0914408107</ELocationID><Abstract><AbstractText>Fungal and oomycete plant pathogens translocate effector proteins into host cells to establish infection. However, virulence targets and modes of action of their effectors are unknown. Effector AVR3a from potato blight pathogen Phytophthora infestans is translocated into host cells and occurs in two forms: AVR3a(KI), which is detected by potato resistance protein R3a, strongly suppresses infestin 1 (INF1)-triggered cell death (ICD), whereas AVR3a(EM), which evades recognition by R3a, weakly suppresses host ICD. Here we show that AVR3a interacts with and stabilizes host U-box E3 ligase CMPG1, which is required for ICD. In contrast, AVR3a(KI/Y147del), a mutant with a deleted C-terminal tyrosine residue that fails to suppress ICD, cannot interact with or stabilize CMPG1. CMPG1 is stabilized by the inhibitors MG132 and epoxomicin, indicating that it is degraded by the 26S proteasome. CMPG1 is degraded during ICD. However, it is stabilized by mutations in the U-box that prevent its E3 ligase activity. In stabilizing CMPG1, AVR3a thus modifies its normal activity. Remarkably, given the potential for hundreds of effector genes in the P. infestans genome, silencing Avr3a compromises P. infestans pathogenicity, suggesting that AVR3a is essential for virulence. Interestingly, Avr3a silencing can be complemented by in planta expression of Avr3a(KI) or Avr3a(EM) but not the Avr3a(KI/Y147del) mutant. Our data provide genetic evidence that AVR3a is an essential virulence factor that targets and stabilizes the plant E3 ligase CMPG1, potentially to prevent host cell death during the biotrophic phase of infection.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Bos</LastName><ForeName>Jorunn I B</ForeName><Initials>JI</Initials><AffiliationInfo><Affiliation>The Sainsbury Laboratory, John Innes Centre, Colney, Norwich NR4 7UH, UK.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Armstrong</LastName><ForeName>Miles R</ForeName><Initials>MR</Initials></Author><Author ValidYN="Y"><LastName>Gilroy</LastName><ForeName>Eleanor M</ForeName><Initials>EM</Initials></Author><Author ValidYN="Y"><LastName>Boevink</LastName><ForeName>Petra C</ForeName><Initials>PC</Initials></Author><Author ValidYN="Y"><LastName>Hein</LastName><ForeName>Ingo</ForeName><Initials>I</Initials></Author><Author ValidYN="Y"><LastName>Taylor</LastName><ForeName>Rosalind M</ForeName><Initials>RM</Initials></Author><Author ValidYN="Y"><LastName>Zhendong</LastName><ForeName>Tian</ForeName><Initials>T</Initials></Author><Author ValidYN="Y"><LastName>Engelhardt</LastName><ForeName>Stefan</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Vetukuri</LastName><ForeName>Ramesh R</ForeName><Initials>RR</Initials></Author><Author ValidYN="Y"><LastName>Harrower</LastName><ForeName>Brian</ForeName><Initials>B</Initials></Author><Author ValidYN="Y"><LastName>Dixelius</LastName><ForeName>Christina</ForeName><Initials>C</Initials></Author><Author ValidYN="Y"><LastName>Bryan</LastName><ForeName>Glenn</ForeName><Initials>G</Initials></Author><Author ValidYN="Y"><LastName>Sadanandom</LastName><ForeName>Ari</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Whisson</LastName><ForeName>Stephen C</ForeName><Initials>SC</Initials></Author><Author ValidYN="Y"><LastName>Kamoun</LastName><ForeName>Sophien</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Birch</LastName><ForeName>Paul R J</ForeName><Initials>PR</Initials></Author></AuthorList><Language>eng</Language><DataBankList CompleteYN="Y"><DataBank><DataBankName>GENBANK</DataBankName><AccessionNumberList><AccessionNumber>HM150712</AccessionNumber><AccessionNumber>HM150713</AccessionNumber><AccessionNumber>HM150714</AccessionNumber><AccessionNumber>HM150715</AccessionNumber><AccessionNumber>HM150716</AccessionNumber></AccessionNumberList></DataBank></DataBankList><GrantList CompleteYN="Y"><Grant><GrantID>BB/C006488/1</GrantID><Agency>Biotechnology and Biological Sciences Research Council</Agency><Country>United Kingdom</Country></Grant><Grant><GrantID>BB/E007120/1</GrantID><Agency>Biotechnology and Biological Sciences Research Council</Agency><Country>United Kingdom</Country></Grant><Grant><GrantID>BB/G015244/1</GrantID><Agency>Biotechnology and Biological Sciences Research Council</Agency><Country>United Kingdom</Country></Grant><Grant><GrantID>BBS/B/07152</GrantID><Agency>Biotechnology and Biological Sciences Research Council</Agency><Country>United Kingdom</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2010</Year><Month>05</Month><Day>10</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Proc Natl Acad Sci U S A</MedlineTA><NlmUniqueID>7505876</NlmUniqueID><ISSNLinking>0027-8424</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D020418">Algal Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.3.2.27</RegistryNumber><NameOfSubstance UI="D044767">Ubiquitin-Protein Ligases</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><CommentsCorrectionsList><CommentsCorrections RefType="ErratumIn"><RefSource>Proc Natl Acad Sci U S A. 2020 Nov 10;117(45):28531-28533</RefSource><PMID Version="1">33106432</PMID></CommentsCorrections></CommentsCorrectionsList><MeshHeadingList><MeshHeading><DescriptorName UI="D020418" MajorTopicYN="N">Algal Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000276" MajorTopicYN="Y">immunology</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004795" MajorTopicYN="N">Enzyme Stability</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D054884" MajorTopicYN="N">Host-Pathogen Interactions</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D055750" MajorTopicYN="N">Phytophthora infestans</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000276" MajorTopicYN="Y">immunology</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName><QualifierName UI="Q000472" MajorTopicYN="N">pathogenicity</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011198" MajorTopicYN="N">Solanum tuberosum</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000276" MajorTopicYN="Y">immunology</QualifierName><QualifierName UI="Q000469" MajorTopicYN="N">parasitology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D044767" MajorTopicYN="N">Ubiquitin-Protein Ligases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014774" MajorTopicYN="N">Virulence</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2010</Year><Month>5</Month><Day>12</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2010</Year><Month>5</Month><Day>12</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2010</Year><Month>6</Month><Day>30</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">20457921</ArticleId><ArticleId IdType="pii">0914408107</ArticleId><ArticleId IdType="doi">10.1073/pnas.0914408107</ArticleId><ArticleId IdType="pmc">PMC2906857</ArticleId></ArticleIdList><ReferenceList><Reference><Citation>Annu Rev Microbiol. 2006;60:425-49</Citation><ArticleIdList><ArticleId IdType="pubmed">16753033</ArticleId></ArticleIdList></Reference><Reference><Citation>Mol Plant Microbe 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Armstrong</name><name sortKey="Birch, Paul R J" sort="Birch, Paul R J" uniqKey="Birch P" first="Paul R J" last="Birch">Paul R J. Birch</name><name sortKey="Boevink, Petra C" sort="Boevink, Petra C" uniqKey="Boevink P" first="Petra C" last="Boevink">Petra C. Boevink</name><name sortKey="Bryan, Glenn" sort="Bryan, Glenn" uniqKey="Bryan G" first="Glenn" last="Bryan">Glenn Bryan</name><name sortKey="Dixelius, Christina" sort="Dixelius, Christina" uniqKey="Dixelius C" first="Christina" last="Dixelius">Christina Dixelius</name><name sortKey="Engelhardt, Stefan" sort="Engelhardt, Stefan" uniqKey="Engelhardt S" first="Stefan" last="Engelhardt">Stefan Engelhardt</name><name sortKey="Gilroy, Eleanor M" sort="Gilroy, Eleanor M" uniqKey="Gilroy E" first="Eleanor M" last="Gilroy">Eleanor M. Gilroy</name><name sortKey="Harrower, Brian" sort="Harrower, Brian" uniqKey="Harrower B" first="Brian" last="Harrower">Brian Harrower</name><name sortKey="Hein, Ingo" sort="Hein, Ingo" uniqKey="Hein I" first="Ingo" last="Hein">Ingo Hein</name><name sortKey="Kamoun, Sophien" sort="Kamoun, Sophien" uniqKey="Kamoun S" first="Sophien" last="Kamoun">Sophien Kamoun</name><name sortKey="Sadanandom, Ari" sort="Sadanandom, Ari" uniqKey="Sadanandom A" first="Ari" last="Sadanandom">Ari Sadanandom</name><name sortKey="Taylor, Rosalind M" sort="Taylor, Rosalind M" uniqKey="Taylor R" first="Rosalind M" last="Taylor">Rosalind M. Taylor</name><name sortKey="Vetukuri, Ramesh R" sort="Vetukuri, Ramesh R" uniqKey="Vetukuri R" first="Ramesh R" last="Vetukuri">Ramesh R. Vetukuri</name><name sortKey="Whisson, Stephen C" sort="Whisson, Stephen C" uniqKey="Whisson S" first="Stephen C" last="Whisson">Stephen C. Whisson</name><name sortKey="Zhendong, Tian" sort="Zhendong, Tian" uniqKey="Zhendong T" first="Tian" last="Zhendong">Tian Zhendong</name></noCountry><country name="Royaume-Uni"><noRegion><name sortKey="Bos, Jorunn I B" sort="Bos, Jorunn I B" uniqKey="Bos J" first="Jorunn I B" last="Bos">Jorunn I B. Bos</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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