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Eudicot plant-specific sphingolipids determine host selectivity of microbial NLP cytolysins.

Identifieur interne : 000A09 ( Main/Exploration ); précédent : 000A08; suivant : 000A10

Eudicot plant-specific sphingolipids determine host selectivity of microbial NLP cytolysins.

Auteurs : Tea Lenar I [Slovénie] ; Isabell Albert [Allemagne] ; Hannah Böhm [Allemagne] ; Vesna Hodnik [Slovénie] ; Katja Pirc [Slovénie] ; Apolonija B. Zavec [Slovénie] ; Marjetka Podobnik [Slovénie] ; David Pahovnik [Slovénie] ; Ema Žagar [Slovénie] ; Rory Pruitt [Allemagne] ; Peter Greimel [Japon] ; Akiko Yamaji-Hasegawa [Japon] ; Toshihide Kobayashi [Japon, France] ; Agnieszka Zienkiewicz [Allemagne] ; Jasmin Gömann [Allemagne] ; Jenny C. Mortimer [États-Unis] ; Lin Fang [États-Unis] ; Adiilah Mamode-Cassim [France] ; Magali Deleu [Belgique] ; Laurence Lins [Belgique] ; Claudia Oecking [Allemagne] ; Ivo Feussner [Allemagne] ; Sébastien Mongrand [France] ; Gregor Anderluh [Slovénie] ; Thorsten Nürnberger [Allemagne]

Source :

RBID : pubmed:29242345

Descripteurs français

English descriptors

Abstract

Necrosis and ethylene-inducing peptide 1-like (NLP) proteins constitute a superfamily of proteins produced by plant pathogenic bacteria, fungi, and oomycetes. Many NLPs are cytotoxins that facilitate microbial infection of eudicot, but not of monocot plants. Here, we report glycosylinositol phosphorylceramide (GIPC) sphingolipids as NLP toxin receptors. Plant mutants with altered GIPC composition were more resistant to NLP toxins. Binding studies and x-ray crystallography showed that NLPs form complexes with terminal monomeric hexose moieties of GIPCs that result in conformational changes within the toxin. Insensitivity to NLP cytolysins of monocot plants may be explained by the length of the GIPC head group and the architecture of the NLP sugar-binding site. We unveil early steps in NLP cytolysin action that determine plant clade-specific toxin selectivity.

DOI: 10.1126/science.aan6874
PubMed: 29242345


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Le document en format XML

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<title xml:lang="en">Eudicot plant-specific sphingolipids determine host selectivity of microbial NLP cytolysins.</title>
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<name sortKey="Bohm, Hannah" sort="Bohm, Hannah" uniqKey="Bohm H" first="Hannah" last="Böhm">Hannah Böhm</name>
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<name sortKey="Hodnik, Vesna" sort="Hodnik, Vesna" uniqKey="Hodnik V" first="Vesna" last="Hodnik">Vesna Hodnik</name>
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<name sortKey="Pirc, Katja" sort="Pirc, Katja" uniqKey="Pirc K" first="Katja" last="Pirc">Katja Pirc</name>
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<name sortKey="Kobayashi, Toshihide" sort="Kobayashi, Toshihide" uniqKey="Kobayashi T" first="Toshihide" last="Kobayashi">Toshihide Kobayashi</name>
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<nlm:affiliation>UMR 7213 CNRS, University of Strasbourg, 67401 Illkirch, France.</nlm:affiliation>
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<name sortKey="Gomann, Jasmin" sort="Gomann, Jasmin" uniqKey="Gomann J" first="Jasmin" last="Gömann">Jasmin Gömann</name>
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<name sortKey="Lins, Laurence" sort="Lins, Laurence" uniqKey="Lins L" first="Laurence" last="Lins">Laurence Lins</name>
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<nlm:affiliation>Laboratory of Molecular Biophysics at Interfaces, University of Liège, Gembloux, Belgium.</nlm:affiliation>
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<name sortKey="Oecking, Claudia" sort="Oecking, Claudia" uniqKey="Oecking C" first="Claudia" last="Oecking">Claudia Oecking</name>
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<name sortKey="Feussner, Ivo" sort="Feussner, Ivo" uniqKey="Feussner I" first="Ivo" last="Feussner">Ivo Feussner</name>
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<name sortKey="Nurnberger, Thorsten" sort="Nurnberger, Thorsten" uniqKey="Nurnberger T" first="Thorsten" last="Nürnberger">Thorsten Nürnberger</name>
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<title level="j">Science (New York, N.Y.)</title>
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<keywords scheme="KwdEn" xml:lang="en">
<term>Arabidopsis (parasitology)</term>
<term>Binding Sites (MeSH)</term>
<term>Crystallography, X-Ray (MeSH)</term>
<term>Cytotoxins (chemistry)</term>
<term>Cytotoxins (metabolism)</term>
<term>Ethylenes (metabolism)</term>
<term>Host Specificity (MeSH)</term>
<term>Phytophthora (metabolism)</term>
<term>Plant Diseases (parasitology)</term>
<term>Pythium (metabolism)</term>
<term>Sphingolipids (chemistry)</term>
<term>Sphingolipids (metabolism)</term>
<term>Toxins, Biological (metabolism)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr">
<term>Arabidopsis (parasitologie)</term>
<term>Cristallographie aux rayons X (MeSH)</term>
<term>Cytotoxines (composition chimique)</term>
<term>Cytotoxines (métabolisme)</term>
<term>Maladies des plantes (parasitologie)</term>
<term>Phytophthora (métabolisme)</term>
<term>Pythium (métabolisme)</term>
<term>Sites de fixation (MeSH)</term>
<term>Sphingolipides (composition chimique)</term>
<term>Sphingolipides (métabolisme)</term>
<term>Spécificité d'hôte (MeSH)</term>
<term>Toxines biologiques (métabolisme)</term>
<term>Éthylènes (métabolisme)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en">
<term>Cytotoxins</term>
<term>Sphingolipids</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en">
<term>Cytotoxins</term>
<term>Ethylenes</term>
<term>Sphingolipids</term>
<term>Toxins, Biological</term>
</keywords>
<keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr">
<term>Cytotoxines</term>
<term>Sphingolipides</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en">
<term>Phytophthora</term>
<term>Pythium</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr">
<term>Cytotoxines</term>
<term>Phytophthora</term>
<term>Pythium</term>
<term>Sphingolipides</term>
<term>Toxines biologiques</term>
<term>Éthylènes</term>
</keywords>
<keywords scheme="MESH" qualifier="parasitologie" xml:lang="fr">
<term>Arabidopsis</term>
<term>Maladies des plantes</term>
</keywords>
<keywords scheme="MESH" qualifier="parasitology" xml:lang="en">
<term>Arabidopsis</term>
<term>Plant Diseases</term>
</keywords>
<keywords scheme="MESH" xml:lang="en">
<term>Binding Sites</term>
<term>Crystallography, X-Ray</term>
<term>Host Specificity</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr">
<term>Cristallographie aux rayons X</term>
<term>Sites de fixation</term>
<term>Spécificité d'hôte</term>
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<front>
<div type="abstract" xml:lang="en">Necrosis and ethylene-inducing peptide 1-like (NLP) proteins constitute a superfamily of proteins produced by plant pathogenic bacteria, fungi, and oomycetes. Many NLPs are cytotoxins that facilitate microbial infection of eudicot, but not of monocot plants. Here, we report glycosylinositol phosphorylceramide (GIPC) sphingolipids as NLP toxin receptors. Plant mutants with altered GIPC composition were more resistant to NLP toxins. Binding studies and x-ray crystallography showed that NLPs form complexes with terminal monomeric hexose moieties of GIPCs that result in conformational changes within the toxin. Insensitivity to NLP cytolysins of monocot plants may be explained by the length of the GIPC head group and the architecture of the NLP sugar-binding site. We unveil early steps in NLP cytolysin action that determine plant clade-specific toxin selectivity.</div>
</front>
</TEI>
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<DateCompleted>
<Year>2018</Year>
<Month>01</Month>
<Day>15</Day>
</DateCompleted>
<DateRevised>
<Year>2018</Year>
<Month>01</Month>
<Day>15</Day>
</DateRevised>
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<Journal>
<ISSN IssnType="Electronic">1095-9203</ISSN>
<JournalIssue CitedMedium="Internet">
<Volume>358</Volume>
<Issue>6369</Issue>
<PubDate>
<Year>2017</Year>
<Month>12</Month>
<Day>15</Day>
</PubDate>
</JournalIssue>
<Title>Science (New York, N.Y.)</Title>
<ISOAbbreviation>Science</ISOAbbreviation>
</Journal>
<ArticleTitle>Eudicot plant-specific sphingolipids determine host selectivity of microbial NLP cytolysins.</ArticleTitle>
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<MedlinePgn>1431-1434</MedlinePgn>
</Pagination>
<ELocationID EIdType="doi" ValidYN="Y">10.1126/science.aan6874</ELocationID>
<Abstract>
<AbstractText>Necrosis and ethylene-inducing peptide 1-like (NLP) proteins constitute a superfamily of proteins produced by plant pathogenic bacteria, fungi, and oomycetes. Many NLPs are cytotoxins that facilitate microbial infection of eudicot, but not of monocot plants. Here, we report glycosylinositol phosphorylceramide (GIPC) sphingolipids as NLP toxin receptors. Plant mutants with altered GIPC composition were more resistant to NLP toxins. Binding studies and x-ray crystallography showed that NLPs form complexes with terminal monomeric hexose moieties of GIPCs that result in conformational changes within the toxin. Insensitivity to NLP cytolysins of monocot plants may be explained by the length of the GIPC head group and the architecture of the NLP sugar-binding site. We unveil early steps in NLP cytolysin action that determine plant clade-specific toxin selectivity.</AbstractText>
<CopyrightInformation>Copyright © 2017 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works.</CopyrightInformation>
</Abstract>
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<LastName>Lenarčič</LastName>
<ForeName>Tea</ForeName>
<Initials>T</Initials>
<Identifier Source="ORCID">0000-0003-2590-0323</Identifier>
<AffiliationInfo>
<Affiliation>Department for Molecular Biology and Nanobiotechnology, National Institute of Chemistry, Hajdrihova 19, 1000 Ljubljana, Slovenia.</Affiliation>
</AffiliationInfo>
</Author>
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<LastName>Albert</LastName>
<ForeName>Isabell</ForeName>
<Initials>I</Initials>
<Identifier Source="ORCID">0000-0003-2223-496X</Identifier>
<AffiliationInfo>
<Affiliation>Centre of Plant Molecular Biology, Eberhard-Karls-University Tübingen, Auf der Morgenstelle 32, 72076 Tübingen, Germany.</Affiliation>
</AffiliationInfo>
</Author>
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<LastName>Böhm</LastName>
<ForeName>Hannah</ForeName>
<Initials>H</Initials>
<Identifier Source="ORCID">0000-0002-0932-332X</Identifier>
<AffiliationInfo>
<Affiliation>Centre of Plant Molecular Biology, Eberhard-Karls-University Tübingen, Auf der Morgenstelle 32, 72076 Tübingen, Germany.</Affiliation>
</AffiliationInfo>
</Author>
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<LastName>Hodnik</LastName>
<ForeName>Vesna</ForeName>
<Initials>V</Initials>
<Identifier Source="ORCID">0000-0002-7681-038X</Identifier>
<AffiliationInfo>
<Affiliation>Department for Molecular Biology and Nanobiotechnology, National Institute of Chemistry, Hajdrihova 19, 1000 Ljubljana, Slovenia.</Affiliation>
</AffiliationInfo>
<AffiliationInfo>
<Affiliation>Department of Biology, Biotechnical Faculty, University of Ljubljana, Jamnikarjeva 101, 1000 Ljubljana, Slovenia.</Affiliation>
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<Affiliation>Department for Molecular Biology and Nanobiotechnology, National Institute of Chemistry, Hajdrihova 19, 1000 Ljubljana, Slovenia.</Affiliation>
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<Affiliation>Department of Polymer Chemistry and Technology, National Institute of Chemistry, Hajdrihova 19, 1000 Ljubljana, Slovenia.</Affiliation>
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<LastName>Žagar</LastName>
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<AffiliationInfo>
<Affiliation>Department of Polymer Chemistry and Technology, National Institute of Chemistry, Hajdrihova 19, 1000 Ljubljana, Slovenia.</Affiliation>
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<LastName>Pruitt</LastName>
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<Affiliation>Centre of Plant Molecular Biology, Eberhard-Karls-University Tübingen, Auf der Morgenstelle 32, 72076 Tübingen, Germany.</Affiliation>
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</Author>
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<LastName>Greimel</LastName>
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<AffiliationInfo>
<Affiliation>Lipid Biology Laboratory, RIKEN, Wako Saitama 351-0198, Japan.</Affiliation>
</AffiliationInfo>
<AffiliationInfo>
<Affiliation>Laboratory for Cell Function Dynamics, Brain Science Institute, RIKEN Institute, Wako, Saitama 351-0198, Japan.</Affiliation>
</AffiliationInfo>
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<LastName>Yamaji-Hasegawa</LastName>
<ForeName>Akiko</ForeName>
<Initials>A</Initials>
<AffiliationInfo>
<Affiliation>Lipid Biology Laboratory, RIKEN, Wako Saitama 351-0198, Japan.</Affiliation>
</AffiliationInfo>
<AffiliationInfo>
<Affiliation>Molecular Membrane Neuroscience, Brain Science Institute, RIKEN Institute, Wako, Saitama 351-0198, Japan.</Affiliation>
</AffiliationInfo>
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<LastName>Kobayashi</LastName>
<ForeName>Toshihide</ForeName>
<Initials>T</Initials>
<AffiliationInfo>
<Affiliation>Lipid Biology Laboratory, RIKEN, Wako Saitama 351-0198, Japan.</Affiliation>
</AffiliationInfo>
<AffiliationInfo>
<Affiliation>UMR 7213 CNRS, University of Strasbourg, 67401 Illkirch, France.</Affiliation>
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<LastName>Zienkiewicz</LastName>
<ForeName>Agnieszka</ForeName>
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<AffiliationInfo>
<Affiliation>Department of Plant Biochemistry, Albrecht-von-Haller-Institute for Plant Sciences, University of Göttingen, Germany.</Affiliation>
</AffiliationInfo>
<AffiliationInfo>
<Affiliation>Göttingen Center for Molecular Biosciences, University of Göttingen, Germany.</Affiliation>
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<AffiliationInfo>
<Affiliation>Department of Plant Biochemistry, Albrecht-von-Haller-Institute for Plant Sciences, University of Göttingen, Germany.</Affiliation>
</AffiliationInfo>
<AffiliationInfo>
<Affiliation>Göttingen Center for Molecular Biosciences, University of Göttingen, Germany.</Affiliation>
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<LastName>Mortimer</LastName>
<ForeName>Jenny C</ForeName>
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<Affiliation>Joint Bioenergy Institute, Emeryville, CA 94608, USA.</Affiliation>
</AffiliationInfo>
<AffiliationInfo>
<Affiliation>Biosciences Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA.</Affiliation>
</AffiliationInfo>
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<Affiliation>Joint Bioenergy Institute, Emeryville, CA 94608, USA.</Affiliation>
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<AffiliationInfo>
<Affiliation>Biosciences Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA.</Affiliation>
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<Affiliation>Laboratory of Molecular Biophysics at Interfaces, University of Liège, Gembloux, Belgium.</Affiliation>
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<Affiliation>Laboratory of Molecular Biophysics at Interfaces, University of Liège, Gembloux, Belgium.</Affiliation>
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<Affiliation>Centre of Plant Molecular Biology, Eberhard-Karls-University Tübingen, Auf der Morgenstelle 32, 72076 Tübingen, Germany.</Affiliation>
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<Affiliation>Department of Plant Biochemistry, Albrecht-von-Haller-Institute for Plant Sciences, University of Göttingen, Germany.</Affiliation>
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<Affiliation>Göttingen Center for Molecular Biosciences, University of Göttingen, Germany.</Affiliation>
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<Affiliation>Laboratoire de Biogenèse Membranaire, UMR 5200 CNRS-Université de Bordeaux, 71 Avenue Edouard Bourlaux, 33883 Villenave-d'Ornon Cedex, France.</Affiliation>
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<LastName>Anderluh</LastName>
<ForeName>Gregor</ForeName>
<Initials>G</Initials>
<Identifier Source="ORCID">0000-0002-9916-8465</Identifier>
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<Affiliation>Department for Molecular Biology and Nanobiotechnology, National Institute of Chemistry, Hajdrihova 19, 1000 Ljubljana, Slovenia. gregor.anderluh@ki.si nuernberger@uni-tuebingen.de.</Affiliation>
</AffiliationInfo>
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<LastName>Nürnberger</LastName>
<ForeName>Thorsten</ForeName>
<Initials>T</Initials>
<Identifier Source="ORCID">0000-0003-3992-0149</Identifier>
<AffiliationInfo>
<Affiliation>Centre of Plant Molecular Biology, Eberhard-Karls-University Tübingen, Auf der Morgenstelle 32, 72076 Tübingen, Germany. gregor.anderluh@ki.si nuernberger@uni-tuebingen.de.</Affiliation>
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<Chemical>
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<RefSource>Science. 2017 Dec 15;358(6369):1383-1384</RefSource>
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<MeshHeading>
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<MeshHeading>
<DescriptorName UI="D003603" MajorTopicYN="N">Cytotoxins</DescriptorName>
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<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D005030" MajorTopicYN="N">Ethylenes</DescriptorName>
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<MeshHeading>
<DescriptorName UI="D058507" MajorTopicYN="Y">Host Specificity</DescriptorName>
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<MeshHeading>
<DescriptorName UI="D010935" MajorTopicYN="N">Plant Diseases</DescriptorName>
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<MeshHeading>
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<MeshHeading>
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<MeshHeading>
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<name sortKey="Kobayashi, Toshihide" sort="Kobayashi, Toshihide" uniqKey="Kobayashi T" first="Toshihide" last="Kobayashi">Toshihide Kobayashi</name>
<name sortKey="Yamaji Hasegawa, Akiko" sort="Yamaji Hasegawa, Akiko" uniqKey="Yamaji Hasegawa A" first="Akiko" last="Yamaji-Hasegawa">Akiko Yamaji-Hasegawa</name>
<name sortKey="Yamaji Hasegawa, Akiko" sort="Yamaji Hasegawa, Akiko" uniqKey="Yamaji Hasegawa A" first="Akiko" last="Yamaji-Hasegawa">Akiko Yamaji-Hasegawa</name>
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<country name="France">
<region name="Grand Est">
<name sortKey="Kobayashi, Toshihide" sort="Kobayashi, Toshihide" uniqKey="Kobayashi T" first="Toshihide" last="Kobayashi">Toshihide Kobayashi</name>
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<name sortKey="Mamode Cassim, Adiilah" sort="Mamode Cassim, Adiilah" uniqKey="Mamode Cassim A" first="Adiilah" last="Mamode-Cassim">Adiilah Mamode-Cassim</name>
<name sortKey="Mongrand, Sebastien" sort="Mongrand, Sebastien" uniqKey="Mongrand S" first="Sébastien" last="Mongrand">Sébastien Mongrand</name>
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<country name="États-Unis">
<region name="Californie">
<name sortKey="Mortimer, Jenny C" sort="Mortimer, Jenny C" uniqKey="Mortimer J" first="Jenny C" last="Mortimer">Jenny C. Mortimer</name>
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<name sortKey="Fang, Lin" sort="Fang, Lin" uniqKey="Fang L" first="Lin" last="Fang">Lin Fang</name>
<name sortKey="Fang, Lin" sort="Fang, Lin" uniqKey="Fang L" first="Lin" last="Fang">Lin Fang</name>
<name sortKey="Mortimer, Jenny C" sort="Mortimer, Jenny C" uniqKey="Mortimer J" first="Jenny C" last="Mortimer">Jenny C. Mortimer</name>
</country>
<country name="Belgique">
<region name="Région wallonne">
<name sortKey="Deleu, Magali" sort="Deleu, Magali" uniqKey="Deleu M" first="Magali" last="Deleu">Magali Deleu</name>
</region>
<name sortKey="Lins, Laurence" sort="Lins, Laurence" uniqKey="Lins L" first="Laurence" last="Lins">Laurence Lins</name>
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</tree>
</affiliations>
</record>

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