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Science. 2017 Dec 15;358(6369):1431-1434. doi: 10.1126/science.aan6874.

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

Author information

1
Department for Molecular Biology and Nanobiotechnology, National Institute of Chemistry, Hajdrihova 19, 1000 Ljubljana, Slovenia.
2
Centre of Plant Molecular Biology, Eberhard-Karls-University Tübingen, Auf der Morgenstelle 32, 72076 Tübingen, Germany.
3
Department of Biology, Biotechnical Faculty, University of Ljubljana, Jamnikarjeva 101, 1000 Ljubljana, Slovenia.
4
Department of Polymer Chemistry and Technology, National Institute of Chemistry, Hajdrihova 19, 1000 Ljubljana, Slovenia.
5
Lipid Biology Laboratory, RIKEN, Wako Saitama 351-0198, Japan.
6
Laboratory for Cell Function Dynamics, Brain Science Institute, RIKEN Institute, Wako, Saitama 351-0198, Japan.
7
Molecular Membrane Neuroscience, Brain Science Institute, RIKEN Institute, Wako, Saitama 351-0198, Japan.
8
UMR 7213 CNRS, University of Strasbourg, 67401 Illkirch, France.
9
Department of Plant Biochemistry, Albrecht-von-Haller-Institute for Plant Sciences, University of Göttingen, Germany.
10
Göttingen Center for Molecular Biosciences, University of Göttingen, Germany.
11
Joint Bioenergy Institute, Emeryville, CA 94608, USA.
12
Biosciences Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA.
13
Laboratoire de Biogenèse Membranaire, UMR 5200 CNRS-Université de Bordeaux, 71 Avenue Edouard Bourlaux, 33883 Villenave-d'Ornon Cedex, France.
14
Laboratory of Molecular Biophysics at Interfaces, University of Liège, Gembloux, Belgium.
15
Department for Molecular Biology and Nanobiotechnology, National Institute of Chemistry, Hajdrihova 19, 1000 Ljubljana, Slovenia. gregor.anderluh@ki.si nuernberger@uni-tuebingen.de.
16
Centre of Plant Molecular Biology, Eberhard-Karls-University Tübingen, Auf der Morgenstelle 32, 72076 Tübingen, Germany. gregor.anderluh@ki.si nuernberger@uni-tuebingen.de.

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.

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PMID:
29242345
DOI:
10.1126/science.aan6874
[Indexed for MEDLINE]

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