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

by Böhm, Hannah , Žagar, Ema , Podobnik, Marjetka , Yamaji-Hasegawa, Akiko , Nürnberger, Thorsten , Greimel, Peter , Lins, Laurence , Pirc, Katja , Gömann, Jasmin , Zienkiewicz, Agnieszka , Mongrand, Sébastien , Pruitt, Rory , Mortimer, Jenny C. , Hodnik, Vesna , Fang, Lin , Deleu, Magali , Albert, Isabell , Kobayashi, Toshihide , Zavec, Apolonija B. , Oecking, Claudia , Mamode-Cassim, Adiilah , Anderluh, Gregor , Lenarčič, Tea , Feussner, Ivo , Pahovnik, David

in Bacteria / Binding sites / Biochemistry, biophysics & molecular biology / Biochimie, biophysique & biologie moléculaire / Biotechnology / Crystallography / Cytolysins / Cytotoxins / Ethylene / Fungi / Gangrene / Hexose / Hexoses / Host plants / Life Sciences / Lysis / Microorganisms / Necrosis / Phospholipids / Proteins / Receptors / Sciences du vivant / Selectivity / Sphingolipids / Sugar / Toxins / X-ray crystallography

2017

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

2017

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

2017

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Journal Article

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

Böhm, Hannah,

Žagar, Ema,

Podobnik, Marjetka,

Yamaji-Hasegawa, Akiko,

Nürnberger, Thorsten,

Greimel, Peter,

Lins, Laurence,

Pirc, Katja,

Gömann, Jasmin,

Zienkiewicz, Agnieszka,

Mongrand, Sébastien,

Pruitt, Rory,

Mortimer, Jenny C.,

Hodnik, Vesna,

Fang, Lin,

Deleu, Magali,

Albert, Isabell,

Kobayashi, Toshihide,

Zavec, Apolonija B.,

Oecking, Claudia,

Mamode-Cassim, Adiilah,

Anderluh, Gregor,

Lenarčič, Tea,

Feussner, Ivo,

Pahovnik, David

2017

Overview

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.

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Publisher

American Association for the Advancement of Science,The American Association for the Advancement of Science,American Association for the Advancement of Science (AAAS)

Subject

Bacteria

/ Binding sites

/ Biochemistry, biophysics & molecular biology

/ Biochimie, biophysique & biologie moléculaire

/ Fungi