Details

Autor(en) / Beteiligte

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

Titel

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

Ist Teil von

• Science (American Association for the Advancement of Science), 2017-12, Vol.358 (6369), p.1431-1434

Ort / Verlag

United States: American Association for the Advancement of Science

Erscheinungsjahr

2017

Quelle

American Association for the Advancement of Science

Beschreibungen/Notizen

• 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.